Journal articles: 'CSPs'

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Chen, Jia-Yun, Xin-Yuan Sun, and Jian-Ming Ouyang. "Modulation of Calcium Oxalate Crystal Growth and Protection from Oxidatively Damaged Renal Epithelial Cells of Corn Silk Polysaccharides with Different Molecular Weights." Oxidative Medicine and Cellular Longevity 2020 (January 22, 2020): 1–19. http://dx.doi.org/10.1155/2020/6982948.

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Corn silk polysaccharide (CSP0; molecular weight=124 kDa) was degraded by ultrasonication to obtain five degraded polysaccharides, namely, CSP1, CSP2, CSP3, CSP4, and CSP5, with molecular weights of 26.1, 12.2, 6.0, 3.5, and 2.0 kDa, respectively. The structures of these polysaccharides were characterized by FT-IR, 1H NMR, and 13C NMR analyses. The antioxidant activities, including scavenging ability for hydroxyl radicals and DPPH free radicals, chelation ability for Fe2+ ions, and reducing ability of CSP increased with decreased molecular weight of CSPs within 6.0 to 124 kDa. However, antioxidant activity weakened when the molecular weight of CSPs reached 3.5 and 2 kDa. CSP3 with a molecular weight of 6.0 kDa exhibited the strongest antioxidant activity. After protection with 60 μg/mL CSPs, the viability of human renal proximal tubular epithelial cells (HK-2) damaged by nano-COM crystals increased, the level of reactive oxygen species decreased, and the amount of COM crystal adhered onto the cell surface decreased. The ability of CSPs to protect cells from CaOx crystal damage was consistent with their antioxidant activity. CSPs can specifically combine with CaOx crystal to inhibit the conversion of calcium oxalate dihydrate crystal to calcium oxalate monohydrate crystal. All these results showed that the activity of CSPs was closely correlated with molecular weight. A very high or low molecular weight of CSPs was not conducive to their activity. CSPs, especially CSP3 with a molecular weight of 6.0 kDa, can be used as a potential antistone drug.

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Wemekamp-Kamphuis, Henrike H., Andreas K. Karatzas, Jeroen A. Wouters, and Tjakko Abee. "Enhanced Levels of Cold Shock Proteins in Listeria monocytogenes LO28 upon Exposure to Low Temperature and High Hydrostatic Pressure." Applied and Environmental Microbiology 68, no. 2 (February 2002): 456–63. http://dx.doi.org/10.1128/aem.68.2.456-463.2002.

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ABSTRACT Listeria monocytogenes is a psychrotrophic food-borne pathogen that is problematic for the food industry because of its ubiquitous distribution in nature and its ability to grow at low temperatures and in the presence of high salt concentrations. Here we demonstrate that the process of adaptation to low temperature after cold shock includes elevated levels of cold shock proteins (CSPs) and that the levels of CSPs are also elevated after treatment with high hydrostatic pressure (HHP). Two-dimensional gel electrophoresis combined with Western blotting performed with anti-CspB of Bacillus subtilis was used to identify four 7-kDa proteins, designated Csp1, Csp2, Csp3, and Csp4. In addition, Southern blotting revealed four chromosomal DNA fragments that reacted with a csp probe, which also indicated that a CSP family is present in L. monocytogenes LO28. After a cold shock in which the temperature was decreased from 37Ã¯Â¿Â½C to 10Ã¯Â¿Â½C the levels of Csp1 and Csp3 increased 10- and 3.5-fold, respectively, but the levels of Csp2 and Csp4 were not elevated. Pressurization of L. monocytogenes LO28 cells resulted in 3.5- and 2-fold increases in the levels of Csp1 and Csp2, respectively. Strikingly, the level of survival after pressurization of cold-shocked cells was 100-fold higher than that of cells growing exponentially at 37Ã¯Â¿Â½C. These findings imply that cold-shocked cells are protected from HHP treatment, which may affect the efficiency of combined preservation techniques.

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Ma, Chao, Yang Yue, Yan Zhang, Zhen-Ya Tian, Hong-Song Chen, Jian-Ying Guo, and Zhong-Shi Zhou. "Scanning Electron Microscopic Analysis of Antennal Sensilla and Tissue-Expression Profiles of Chemosensory Protein Genes in Ophraella communa (Coleoptera: Chrysomelidae)." Insects 13, no. 2 (February 9, 2022): 183. http://dx.doi.org/10.3390/insects13020183.

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Ophraella communa is an efficient biocontrol agent used against the invasive weed Ambrosia artemisiifolia. It is an herbivorous insect that feeds on specific plants; the olfactory functions of this insects plays an important role in their search for host plants. There are no reports on O. communa sensilla types, morphology, or chemosensory protein (CSP) genes. In this study, we observed the external structure and distribution of antennal sensilla in adult O. communa antennae by scanning electron microscopy; moreover, we cloned 11 CSPs (CSP1–CSP11) and elucidated their tissue-expression profiles using quantitative real-time polymerase chain reaction. Six types of sensilla were identified: sensilla trichodea (including two subtypes), sensilla chaetica, sensilla basiconica (including two subtypes), sensilla styloconica, sensilla coeloconica, and Böhm bristles. Both male and female antennae had all six types of sensilla, and no sexual dimorphism was noted in sensillar types or distribution. We also found that the expression levels of CSP2, CSP3, CSP4, CSP6, and CSP7 in male and female antennae were higher than those in other tissues, which suggests that these five CSPs may be related to olfactory function in O. communa. Ultimately, our results lay the foundation for interpreting the olfactory functions of adult O. communa.

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Stübs, Dorothee, Thilo M. Fuchs, Boris Schneider, Armin Bosserhoff, and Roy Gross. "Identification and regulation of cold-inducible factors of Bordetella bronchiseptica." Microbiology 151, no. 6 (June 1, 2005): 1895–909. http://dx.doi.org/10.1099/mic.0.27785-0.

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The expression of bacterial cold-shock proteins (CSPs) is highly induced in response to cold shock, and some CSPs are essential for cells to resume growth at low temperature. Bordetella bronchiseptica encodes five CSPs (named CspA to CspE) with significant amino acid homology to CspA of Escherichia coli. In contrast to E. coli, the insertional knock-out of a single csp gene (cspB) strongly affected growth of B. bronchiseptica independent of temperature. In the case of three of the csp genes (cspA, cspB, cspC) more than one specific transcript could be detected. The net amount of cspA, cspB and cspC transcripts increased strongly after cold shock, while no such effect could be observed for cspD and cspE. The exposure to other stress conditions, including translation inhibitors, heat shock, osmotic stress and nutrient deprivation in the stationary phase, indicated that the csp genes are also responsive to these conditions. The coding regions of all of the cold-shock genes are preceded by a long non-translated upstream region (5′-UTR). In the case of the cspB gene, a deletion of parts of this region led to a significant reduction of translation of the resulting truncated transcript, indicating a role of the 5′-UTR in translational control. The cold-shock stimulon was investigated by 2D-PAGE and mass spectrometric characterization, leading to the identification of additional cold-inducible proteins (CIPs). Interestingly, two cold-shock genes (cspC and cspD) were found to be under the negative control of the BvgAS system, the main transcriptional regulator of Bordetella virulence genes. Moreover, a negative effect of slight overexpression of CspB, but not of the other CSPs, on the transcription of the adenylate cyclase toxin CyaA of Bordetella pertussis was observed, suggesting cross-talk between the CSP-mediated stress response stimulon and the Bordetella virulence regulon.

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Wouters, Jeroen A., Marielle Mailhes, Frank M. Rombouts, Willem M. de Vos, Oscar P. Kuipers, and Tjakko Abee. "Physiological and Regulatory Effects of Controlled Overproduction of Five Cold Shock Proteins of Lactococcus lactisMG1363." Applied and Environmental Microbiology 66, no. 9 (September 1, 2000): 3756–63. http://dx.doi.org/10.1128/aem.66.9.3756-3763.2000.

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ABSTRACT The physiological and regulatory effects of overproduction of five cold shock proteins (CSPs) of Lactococcus lactis were studied. CspB, CspD, and CspE could be overproduced at high levels (up to 19% of the total protein), whereas for CspA and CspC limited overproduction (0.3 to 0.5% of the total protein) was obtained. Northern blot analysis revealed low abundance of the cspCtranscript, indicating that the stability of cspC mRNA is low. The limited overproduction of CspA is likely to be caused by low stability of CspA since when there was an Arg-Pro mutation at position 58, the level of CspA production increased. Using two-dimensional gel electrophoresis, it was found that upon overproduction of the CSPs several proteins, including a number of cold-induced proteins ofL. lactis, were induced. Strikingly, upon overproduction of CspC induction of CspB, putative CspF, and putative CspG was also observed. Overproduction of CspB and overproduction of CspE result in increased survival when L. lactis is frozen (maximum increases, 10- and 5-fold, respectively, after 4 freeze-thaw cycles). It is concluded that in L. lactis CSPs play a regulatory role in the cascade of events that are initiated by cold shock treatment and that they either have a direct protective effect during freezing (e.g., RNA stabilization) or induce other factors involved in the freeze-adaptive response or both.

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Xu, Hongfei, Kunpeng Yan, Yaping Ding, Yuntong Lv, Jianyi Li, Fengting Yang, Xuewei Chen, Xiwu Gao, Yiou Pan, and Qingli Shang. "Chemosensory Proteins Are Associated with Thiamethoxam and Spirotetramat Tolerance in Aphis gossypii Glover." International Journal of Molecular Sciences 23, no. 4 (February 21, 2022): 2356. http://dx.doi.org/10.3390/ijms23042356.

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Chemosensory proteins (CSPs) are a class of transporters in arthropods. Deeper research on CSPs showed that CSPs may be involved in some physiological processes beyond chemoreception, such as insect resistance to pesticides. We identified two upregulated CSPs in two resistant strains of Aphis gossypii Glover. To understand their role in the resistance of aphids to pesticides, we performed the functional verification of CSP1 and CSP4 in vivo and in vitro. Results showed that the sensitivity of the thiamethoxam-resistant strain to thiamethoxam increased significantly with the silencing of CSP1 and CSP4 by RNAi (RNA interference), and the sensitivity of the spirotetramat-resistant strain to spirotetramat increased significantly with the silencing of CSP4. Transgenic Drosophila melanogaster expressing CSPs exhibited stronger resistance to thiamethoxam, spirotetramat, and alpha-cypermethrin than the control did. In the bioassay of transgenic Drosophila, CSPs showed different tolerance mechanisms for different pesticides, and the overexpressed CSPs may play a role in processes other than resistance to pesticides. In brief, the present results prove that CSPs are related to the resistance of cotton aphids to insecticides.

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Weber, Michael H. W., Arsen V. Volkov, Ingo Fricke, Mohamed A. Marahiel, and Peter L. Graumann. "Localization of Cold Shock Proteins to Cytosolic Spaces Surrounding Nucleoids in Bacillus subtilis Depends on Active Transcription." Journal of Bacteriology 183, no. 21 (November 1, 2001): 6435–43. http://dx.doi.org/10.1128/jb.183.21.6435-6443.2001.

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ABSTRACT Using immunofluorescence microscopy and a fusion of a cold shock protein (CSP), CspB, to green fluorescent protein (GFP), we showed that in growing cells Bacillus subtilis CSPs specifically localize to cytosolic regions surrounding the nucleoid. The subcellular localization of CSPs is influenced by the structure of the nucleoid. Decondensed chromosomes in smc mutant cells reduced the sizes of the regions in which CSPs localized, while cold shock-induced chromosome compaction was accompanied by an expansion of the space in which CSPs were present. As a control, histone-like protein HBsu localized to the nucleoids, while β-galactosidase and GFP were detectable throughout the cell. After inhibition of translation, CspB-GFP was still present around the nucleoids in a manner similar to that in cold-shocked cells. However, in stationary-phase cells and after inhibition of transcription, CspB was distributed throughout the cell, indicating that specific localization of CspB depends on active transcription and is not due to simple exclusion from the nucleoid. Furthermore, we observed that nucleoids are more condensed and frequently abnormal incspB cspC and cspB cspDdouble-mutant cells. This suggests that the function of CSPs affects chromosome structure, probably through coupling of transcription to translation, which is thought to decondense nucleoids. In addition, we found that cspB cspD and cspB cspC double mutants are defective in sporulation, with a block at or before stage 0. Interestingly, CspB and CspC are depleted from the forespore compartment but not from the mother cell. In toto, our findings suggest that CSPs localize to zones of newly synthesized RNA, coupling transcription with initiation of translation.

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LIMTHAMMAHISORN, SUTTINEE, YOLANDA J. BRADY, and COVADONGA R. ARIAS. "Gene Expression of Cold Shock and Other Stress-Related Genes in Vibrio vulniflcus Grown in Pure Culture under Shellstock Temperature Control Conditions." Journal of Food Protection 71, no. 1 (January 1, 2008): 157–64. http://dx.doi.org/10.4315/0362-028x-71.1.157.

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Shellstock refrigeration after harvesting is recommended to prevent further increases in Vibrio vulniflcus numbers in oysters, but it could potentially induce a cold shock response in this bacterium. V. vulniflcus was incubated at 35, 25, 20, and 15°C and then subjected to 7.2 and 4°C for 1 week. A cold-adaptation response that enhanced cell culturability was observed when cells were incubated at 15°C prior to cold shock at 7.2°C. In vitro cold shock gene expression was analyzed by reverse transcriptase PCR (RT-PCR). The expression of cold shock genes csp1 and csp5 (homologous genes to cspA and cspV) remained constant, despite cold shock. However, the transcript of csp3 was constitutively expressed before and after cold shock, with a few exceptions. The synthesis of csp3 mRNA in V. vulniflcus C7184Tr (an avirulent strain) was induced only after 15°C incubation and cold shock at 4°C. The expression of csp4 was repressed after cold shock. Our data showed that the csps tested in this study are not cold inducible. The transcripts of two oxidative stress-related genes, oxyR and katG, showed different induction patterns among strains after cold shock, suggesting that V. vulniflcus cells encountered oxidative stress during cold shock.

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Mazzon, Ricardo R., Elza A. S. Lang, Carolina A. P. T. Silva, and Marilis V. Marques. "Cold Shock GenescspAandcspBfrom Caulobacter crescentus Are Posttranscriptionally Regulated and Important for Cold Adaptation." Journal of Bacteriology 194, no. 23 (September 21, 2012): 6507–17. http://dx.doi.org/10.1128/jb.01422-12.

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ABSTRACTCold shock proteins (CSPs) are nucleic acid binding chaperones, first described as being induced to solve the problem of mRNA stabilization after temperature downshift.Caulobacter crescentushas four CSPs: CspA and CspB, which are cold induced, and CspC and CspD, which are induced only in stationary phase. In this work we have determined that the synthesis of both CspA and CspB reaches the maximum levels early in the acclimation phase. The deletion ofcspAcauses a decrease in growth at low temperature, whereas the strain with a deletion ofcspBhas a very subtle and transient cold-related growth phenotype. ThecspA cspBdouble mutant has a slightly more severe phenotype than that of thecspAmutant, suggesting that although CspA may be more important to cold adaptation than CspB, both proteins have a role in this process. Gene expression analyses were carried out usingcspAandcspBregulatory fusions to thelacZreporter gene and showed that both genes are regulated at the transcriptional and posttranscriptional levels. Deletion mapping of the long 5′-untranslated region (5′-UTR) of each gene identified a common region important for cold induction, probably via translation enhancement. In contrast to what was reported for other bacteria, these cold shock genes have no regulatory regions downstream from ATG that are important for cold induction. This work shows that the importance of CspA and CspB toC. crescentuscold adaptation, mechanisms of regulation, and pattern of expression during the acclimation phase apparently differs in many aspects from what has been described so far for other bacteria.

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Schmid, Barbara, Jochen Klumpp, Eveline Raimann, Martin J. Loessner, Roger Stephan, and Taurai Tasara. "Role of Cold Shock Proteins in Growth of Listeria monocytogenes under Cold and Osmotic Stress Conditions." Applied and Environmental Microbiology 75, no. 6 (January 16, 2009): 1621–27. http://dx.doi.org/10.1128/aem.02154-08.

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ABSTRACT The gram-positive bacterium Listeria monocytogenes is a food-borne pathogen of both public health and food safety significance. It possesses three small, highly homologous protein members of the cold shock protein (Csp) family. We used gene expression analysis and a set of mutants with single, double, and triple deletions of the csp genes to evaluate the roles of CspA, CspB, and CspD in the cold and osmotic (NaCl) stress adaptation responses of L. monocytogenes. All three Csps are dispensable for growth at optimal temperature (37°C). These proteins are, however, required for efficient cold and osmotic stress tolerance of this bacterium. The hierarchies of their functional importance differ, depending on the environmental stress conditions: CspA>CspD>CspB in response to cold stress versus CspD>CspA/CspB in response to NaCl salt osmotic stress. The fact that Csps are promoting L. monocytogenes adaptation against both cold and NaCl stress has significant implications in view of practical food microbial control measures. The combined or sequential exposure of L. monocytogenes cells to these two stresses in food environments might inadvertently induce cross-protection responses.

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Campbell, Chantal, Mobolaji Adeolu, and Radhey S. Gupta. "Genome-based taxonomic framework for the class Negativicutes: division of the class Negativicutes into the orders Selenomonadales emend., Acidaminococcales ord. nov. and Veillonellales ord. nov." International Journal of Systematic and Evolutionary Microbiology 65, Pt_9 (September 1, 2015): 3203–15. http://dx.doi.org/10.1099/ijs.0.000347.

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The class Negativicutes is currently divided into one order and two families on the basis of 16S rRNA gene sequence phylogenies. We report here comprehensive comparative genomic analyses of the sequenced members of the class Negativicutes to demarcate its different evolutionary groups in molecular terms, independently of phylogenetic trees. Our comparative genomic analyses have identified 14 conserved signature indels (CSIs) and 48 conserved signature proteins (CSPs) that either are specific for the entire class or differentiate four main groups within the class. Two CSIs and nine CSPs are shared uniquely by all or most members of the class Negativicutes, distinguishing this class from all other sequenced members of the phylum Firmicutes. Four other CSIs and six CSPs were specific characteristics of the family Acidaminococcaceae, two CSIs and four CSPs were uniquely present in the family Veillonellaceae, six CSIs and eight CSPs were found only in Selenomonas and related genera, and 17 CSPs were identified uniquely in Sporomusa and related genera. Four additional CSPs support a pairing of the groups containing the genera Selenomonas and Sporomusa. We also report detailed phylogenetic analyses for the Negativicutes based on core protein sequences and 16S rRNA gene sequences, which strongly support the four main groups identified by CSIs and by CSPs. Based on the results from different lines of investigation, we propose a division of the class Negativicutes into an emended order Selenomonadales containing the new families Selenomonadaceae fam. nov. and Sporomusaceae fam. nov. and two new orders, Acidaminococcales ord. nov. and Veillonellales ord. nov., respectively containing the families Acidaminococcaceae and Veillonellaceae.

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Muchaamba, Francis, Roger Stephan, and Taurai Tasara. "Listeria monocytogenes Cold Shock Proteins: Small Proteins with A Huge Impact." Microorganisms 9, no. 5 (May 14, 2021): 1061. http://dx.doi.org/10.3390/microorganisms9051061.

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Listeria monocytogenes has evolved an extensive array of mechanisms for coping with stress and adapting to changing environmental conditions, ensuring its virulence phenotype expression. For this reason, L. monocytogenes has been identified as a significant food safety and public health concern. Among these adaptation systems are cold shock proteins (Csps), which facilitate rapid response to stress exposure. L. monocytogenes has three highly conserved csp genes, namely, cspA, cspB, and cspD. Using a series of csp deletion mutants, it has been shown that L. monocytogenes Csps are important for biofilm formation, motility, cold, osmotic, desiccation, and oxidative stress tolerance. Moreover, they are involved in overall virulence by impacting the expression of virulence-associated phenotypes, such as hemolysis and cell invasion. It is postulated that during stress exposure, Csps function to counteract harmful effects of stress, thereby preserving cell functions, such as DNA replication, transcription and translation, ensuring survival and growth of the cell. Interestingly, it seems that Csps might suppress tolerance to some stresses as their removal resulted in increased tolerance to stresses, such as desiccation for some strains. Differences in csp roles among strains from different genetic backgrounds are apparent for desiccation tolerance and biofilm production. Additionally, hierarchical trends for the different Csps and functional redundancies were observed on their influences on stress tolerance and virulence. Overall current data suggest that Csps have a wider role in bacteria physiology than previously assumed.

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CHAMBERLAIN, Luke H., and Robert D. BURGOYNE. "Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein." Biochemical Journal 322, no. 3 (March 15, 1997): 853–58. http://dx.doi.org/10.1042/bj3220853.

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DnaJ proteins are characterized by a ‘J‘ domain which is homologous to a region of the Escherichia coli protein DnaJ. DnaJ has been shown to interact with the chaperone protein DnaK, and a number of eukaryotic DnaJ-like proteins have been found to interact with the 70 kDa heat-shock protein/70 kDa heat-shock cognate protein (Hsp70/Hsc70), the eukaryotic homologues of DnaK. Cysteine-string proteins (Csps) are believed to function in calcium-stimulated exocytosis and in this paper we describe a specific ATP-dependent interaction between a Csp (Csp1) and Hsc70/Hsp70. We also show that Csp1 can stimulate the ATPase activity of both Hsc70 and Hsp70 several-fold. Furthermore, we demonstrate that Csp2, a Csp variant found in adrenal chromaffin cells, can enhance the ATPase activity of Hsc70 to a similar extent as Csp1, whereas Csp(137–198), a truncated protein lacking the ‘J’ domain of Csp1 is unable to stimulate the ATPase activity of Hsc70. This suggests that the functions of Csp1 and Csp2 must differ in some aspect other than interaction with Hsc70. This study is also important from a general view of DnaJ/Hsc70 interactions, as Csps lack a G/F-rich region which has been suggested to be essential for activation of the ATPase activity of DnaK by DnaJ. Thus, this work would imply that a G/F-rich region is not an essential feature of DnaJ proteins for stimulation of the ATPase activity of Hsp70 proteins.

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Wouters, Jeroen A., Hélène Frenkiel, Willem M. de Vos, Oscar P. Kuipers, and Tjakko Abee. "Cold Shock Proteins of Lactococcus lactis MG1363 Are Involved in Cryoprotection and in the Production of Cold-Induced Proteins." Applied and Environmental Microbiology 67, no. 11 (November 1, 2001): 5171–78. http://dx.doi.org/10.1128/aem.67.11.5171-5178.2001.

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ABSTRACT Members of the group of 7-kDa cold-shock proteins (CSPs) are the proteins with the highest level of induction upon cold shock in the lactic acid bacterium Lactococcus lactis MG1363. By using double-crossover recombination, two L. lactis strains were generated in which genes encoding CSPs are disrupted: L. lactis NZ9000ΔAB lacks the tandemly orientatedcspA and cspB genes, and NZ9000ΔABE lackscspA, cspB, and cspE. Both strains showed no differences in growth at normal and at low temperatures compared to that of the wild-type strain, L. lactis NZ9000. Two-dimensional gel electrophoresis showed that upon disruption of thecspAB genes, the production of remaining CspE at low temperature increased, and upon disruption of cspA, cspB, and cspE, the production of CspD at normal growth temperatures increased. Northern blot analysis showed that control is most likely at the transcriptional level. Furthermore, it was established by a proteomics approach that some (non-7-kDa) cold-induced proteins (CIPs) are not cold induced in the csp-lacking strains, among others the histon-like protein HslA and the signal transduction protein LlrC. This supports earlier observations (J. A. Wouters, M. Mailhes, F. M. Rombouts, W. M. De Vos, O. P. Kuipers, and T. Abee, Appl. Environ. Microbiol. 66:3756–3763, 2000). that the CSPs of L. lactis might be directly involved in the production of some CIPs upon low-temperature exposure. Remarkably, the adaptive response to freezing by prior exposure to 10°C was significantly reduced in strain NZ9000ΔABE but not in strain NZ9000ΔAB compared to results with wild-type strain NZ9000, indicating a notable involvement of CspE in cryoprotection.

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LaGier, Michael J. "Predicted Cold Shock Proteins from the Extremophilic Bacterium Deinococcus maricopensis and Related Deinococcus Species." International Journal of Microbiology 2017 (2017): 1–10. http://dx.doi.org/10.1155/2017/5231424.

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While many studies have examined the mechanisms by which extremophilic Deinococci survive exposure to ionizing radiation, very few publications have characterized the cold shock adaptations of this group, despite many species being found in persistent cold environments and environments prone to significant daily temperature fluctuations. Bacterial cold shock proteins (Csps) are a family of conserved, RNA chaperone proteins that commonly play a role in cold temperature adaptation, including a downward shift in temperature (i.e., cold shock). The primary aim of this study was to test whether a representative, desert-dwelling Deinococcus, Deinococcus maricopensis, encodes Csps as part of its genome. Bioinformatic approaches were used to identify a Csp from D. maricopensis LB-34. The Csp, termed Dm-Csp1, contains sequence features of Csps including a conserved cold shock domain and nucleic acid binding motifs. A tertiary model of Dm-Csp1 revealed an anticipated Csp structure containing five anti-parallel beta-strands, and ligand prediction experiments identified N-terminally located residues capable of binding single-stranded nucleic acids. Putative Csps were identified from 100% of (27 of 27) Deinococci species for which genome information is available; and the Deinococci-encoded Csps identified contain a C-terminally located region that appears to be limited to members of the class Deinococci.

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Ravinesan, Dasha A., and Radhey S. Gupta. "Molecular signatures for members of the genus Dehalococcoides and the class Dehalococcoidia." International Journal of Systematic and Evolutionary Microbiology 64, Pt_6 (June 1, 2014): 2176–81. http://dx.doi.org/10.1099/ijs.0.057919-0.

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The bacteria belonging to the class Dehalococcoidia , due to their ability to dehalogenate chlorinated compounds, are of much interest for bioremediation of contaminated sites. We report here comparative analyses on different genes/proteins from the genomes of members of the class Dehalococcoidia . These studies have identified numerous novel molecular markers in the forms of conserved signature indels (CSIs) in broadly distributed proteins and conserved signature genes/proteins (CSPs), which are uniquely found in members of the class Dehalococcoidia , but except for an isolated exception, they are not found in other sequenced bacterial genomes. Of these molecular markers, nine CSIs in divergent proteins and 19 CSPs are specific for members of the genera Dehalococcoides and Dehalogenimonas , providing potential molecular markers for the bacterial class Dehalococcoidia . Additionally, four CSIs in divergent proteins and 28 CSPs are only found in all members of the genus Dehalococcoides for which genome sequences are available, but they are absent in Dehalogenimonas lykanthroporepellens and in other bacteria. The gene sequences of several of these CSPs exhibiting specificity for the genus Dehalococcoides or the class Dehalococcoidia are highly conserved and PCR primers based upon them provide a novel means for identification of other related bacteria. Two other CSIs identified in this study in the SecD and aspartate carbomyltransferase proteins weakly support an affiliation of the class Dehalococcoidia with the other members of the phylum Chloroflexi.

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Stanković, Aleksa. "On regularity of Max-CSPs and Min-CSPs." Information Processing Letters 176 (June 2022): 106244. http://dx.doi.org/10.1016/j.ipl.2022.106244.

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Naushad, Hafiz Sohail, Brian Lee, and Radhey S. Gupta. "Conserved signature indels and signature proteins as novel tools for understanding microbial phylogeny and systematics: identification of molecular signatures that are specific for the phytopathogenic genera Dickeya, Pectobacterium and Brenneria." International Journal of Systematic and Evolutionary Microbiology 64, Pt_2 (February 1, 2014): 366–83. http://dx.doi.org/10.1099/ijs.0.054213-0.

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Genome sequences are enabling applications of different approaches to more clearly understand microbial phylogeny and systematics. Two of these approaches involve identification of conserved signature indels (CSIs) and conserved signature proteins (CSPs) that are specific for different lineages. These molecular markers provide novel and more definitive means for demarcation of prokaryotic taxa and for identification of species from these groups. Genome sequences are also enabling determination of phylogenetic relationships among species based upon sequences for multiple proteins. In this work, we have used all of these approaches for studying the phytopathogenic bacteria belonging to the genera Dickeya , Pectobacterium and Brenneria . Members of these genera, which cause numerous diseases in important food crops and ornamental plants, are presently distinguished mainly on the basis of their branching in phylogenetic trees. No biochemical or molecular characteristic is known that is uniquely shared by species from these genera. Hence, detailed studies using the above approaches were carried out on proteins from the genomes of these bacteria to identify molecular markers that are specific for them. In phylogenetic trees based upon concatenated sequences for 23 conserved proteins, members of the genera Dickeya , Pectobacterium and Brenneria formed a strongly supported clade within the other Enterobacteriales . Comparative analysis of protein sequences from the Dickeya , Pectobacterium and Brenneria genomes has identified 10 CSIs and five CSPs that are either uniquely or largely found in all genome-sequenced species from these genera, but not present in any other bacteria in the database. In addition, our analyses have identified 10 CSIs and 17 CSPs that are specifically present in either all or most sequenced Dickeya species/strains, and six CSIs and 19 CSPs that are uniquely found in the sequenced Pectobacterium genomes. Finally, our analysis also identified three CSIs and one CSP that are specifically shared by members of the genera Pectobacterium and Brenneria , but absent in species of the genus Dickeya , indicating that the former two genera shared a common ancestor exclusive of Dickeya . The identified CSIs and CSPs provide novel tools for identification of members of the genera Dickeya and Pectobacterium and for delimiting these taxa in molecular terms. Descriptions of the genera Dickeya and Pectobacterium have been revised to provide information for these molecular markers. Biochemical studies on these CSIs and CSPs, which are specific for these genera, may lead to discovery of novel properties that are unique to these bacteria and which could be targeted to develop antibacterial agents that are specific for these plant-pathogenic bacteria.

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Phadtare, Sangita, and Masayori Inouye. "Genome-Wide Transcriptional Analysis of the Cold Shock Response in Wild-Type and Cold-Sensitive, Quadruple-csp-Deletion Strains of Escherichia coli." Journal of Bacteriology 186, no. 20 (October 15, 2004): 7007–14. http://dx.doi.org/10.1128/jb.186.20.7007-7014.2004.

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ABSTRACT A DNA microarray-based global transcript profiling of Escherichia coli in response to cold shock showed that in addition to the known cold shock-inducible genes, new genes such as the flagellar operon, those encoding proteins involved in sugar transport and metabolism, and remarkably, genes encoding certain heat shock proteins are induced by cold shock. In the light of strong reduction in metabolic activity of the cell after temperature downshift, the induction of sugar metabolism machinery is unexpected. The deletion of four csps (cspA, cspB, cspG, and cspE) affected cold shock induction of mostly those genes that are transiently induced in the acclimation phase, emphasizing that CspA homologues are essential in the acclimation phase. Relevance of these findings with respect to the known RNA chaperone function of CspA homologues is discussed.

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Viola, Caterina, and Stanislav Živný. "The Combined Basic LP and Affine IP Relaxation for Promise VCSPs on Infinite Domains." ACM Transactions on Algorithms 17, no. 3 (August 2021): 1–23. http://dx.doi.org/10.1145/3458041.

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Convex relaxations have been instrumental in solvability of constraint satisfaction problems (CSPs), as well as in the three different generalisations of CSPs: valued CSPs, infinite-domain CSPs, and most recently promise CSPs. In this work, we extend an existing tractability result to the three generalisations of CSPs combined: We give a sufficient condition for the combined basic linear programming and affine integer programming relaxation for exact solvability of promise valued CSPs over infinite-domains. This extends a result of Brakensiek and Guruswami (SODA’20) for promise (non-valued) CSPs (on finite domains).

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Hunger, Karen, Carsten L. Beckering, Frank Wiegeshoff, Peter L. Graumann, and Mohamed A. Marahiel. "Cold-Induced Putative DEAD Box RNA Helicases CshA and CshB Are Essential for Cold Adaptation and Interact with Cold Shock Protein B in Bacillus subtilis." Journal of Bacteriology 188, no. 1 (January 1, 2006): 240–48. http://dx.doi.org/10.1128/jb.188.1.240-248.2006.

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ABSTRACT The nucleic acid binding cold shock proteins (CSPs) and the cold-induced DEAD box RNA helicases have been proposed separately to act as RNA chaperones, but no experimental evidence has been reported on a direct cooperation. To investigate the possible interaction of the putative RNA helicases CshA and CshB and the CSPs from Bacillus subtilis during cold shock, we performed genetic as well as fluorescence resonance energy transfer (FRET) experiments. Both cshA and cshB genes could be deleted only in the presence of a cshB copy in trans, showing that the presence of one csh gene is essential for viability. The combined gene deletion of cshB and cspD resulted in a cold-sensitive phenotype that was not observed for either helicase or csp single mutants. In addition to the colocalization of the putative helicases CshA and CshB with CspB and the ribosomes in areas surrounding the nucleoid, we detected a strong FRET interaction in vivo between CshB and CspB that depended on active transcription. In contrast, a FRET interaction was not observed for CshB and the ribosomal protein L1. Therefore, we propose a model in which the putative cold-induced helicases and the CSPs work in conjunction to rescue misfolded mRNA molecules and maintain proper initiation of translation at low temperatures in B. subtilis.

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Bistarelli, Stefano, and Giorgio Gosti. "Solving Distributed CSPs Probabilistically." Fundamenta Informaticae 105, no. 1-2 (2010): 57–78. http://dx.doi.org/10.3233/fi-2010-358.

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Dalmau, Víctor, and Andrei Krokhin. "Robust Satisfiability for CSPs." ACM Transactions on Computation Theory 5, no. 4 (November 2013): 1–25. http://dx.doi.org/10.1145/2540090.

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Butti, Silvia, and Stanislav Živný. "Sparsification of Binary CSPs." SIAM Journal on Discrete Mathematics 34, no. 1 (January 2020): 825–42. http://dx.doi.org/10.1137/19m1242446.

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Nazerali, Rahim, and Michael S. Wong. "Ninth Dedicated CSPS Annals." Annals of Plastic Surgery 84 (May 2020): S241—S244. http://dx.doi.org/10.1097/sap.0000000000002401.

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Fulla, Peter, and Stanislav Živný. "On planar valued CSPs." Journal of Computer and System Sciences 87 (August 2017): 104–18. http://dx.doi.org/10.1016/j.jcss.2017.03.005.

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Parkinson, Charles R., Muhammad Siddiqi, Stephen Mason, Frank Lippert, Anderson T. Hara, and Domenick T. Zero. "Anticaries Potential of a Sodium Monofluorophosphate Dentifrice Containing Calcium Sodium Phosphosilicate: Exploratory in situ Randomized Trial." Caries Research 51, no. 2 (2017): 170–78. http://dx.doi.org/10.1159/000453622.

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Calcium sodium phosphosilicate (CSPS) is a bioactive glass material that alleviates dentin hypersensitivity and is postulated to confer remineralization of caries lesions. This single-centre, randomized, single (investigator)-blind, placebo-controlled, crossover, in situ study explored whether the addition of 5% CSPS to a nonaqueous fluoride (F) such as sodium monofluorophosphate (SMFP)-containing dentifrice affects its cariostatic ability. Seventy-seven subjects wore 4 gauze-covered enamel specimens with preformed lesions (2 surface-softened and 2 subsurface) placed buccally on their mandibular bilateral dentures for up to 4 weeks. Subjects brushed twice daily with 1 of the 5 study dentifrices: 927 ppm F/5% CSPS, 927 ppm F/0% CSPS, 250 ppm F/0% CSPS, 0 ppm F/5% CSPS, or 0 ppm F/0% CSPS. Specimens were retrieved after either 21 (surface-softened lesions; analyzed by Knoop surface microhardness [SMH]) or 28 days (subsurface lesions; analyzed by transverse microradiography). The enamel fluoride uptake was determined for all specimens using a microbiopsy technique. The concentrations of fluoride and calcium in gauze-retrieved plaque were also evaluated. Higher dentifrice fluoride concentrations led to greater remineralization and fluoridation of both lesion types and increased plaque fluoride concentrations. CSPS did not improve the cariostatic properties of SMFP; there were no statistically significant differences between 927 ppm F/5% CSPS and 927 ppm F/0% CSPS in percent SMH recovery (p = 0.6788), change in integrated mineral loss (p = 0.5908), or lesion depth (p = 0.6622). Likewise, 0 ppm F/5% CSPS did not provide any benefits in comparison to 0 ppm F/0% CSPS. In conclusion, CSPS does not negatively impact nor does it improve the ability of an SMFP dentifrice to affect remineralization of caries lesions.

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Chen, Xiaoming, Chiyo Yamamoto, and Yoshio Okamoto. "Polysaccharide derivatives as useful chiral stationary phases in high-performance liquid chromatography." Pure and Applied Chemistry 79, no. 9 (January 1, 2007): 1561–73. http://dx.doi.org/10.1351/pac200779091561.

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The chromatographic separation of enantiomers using chiral stationary phases (CSPs) has significantly advanced. The esters and carbamates of polysaccharides coated on silica gel have been extensively studied and widely used as CSPs for high-performance liquid chromatography (HPLC). In order to overcome the strict solvent limitation on these coated CSPs, the preparation of a new generation of CSPs consisting of immobilized polysaccharide derivatives has become increasingly important. The universal solvent compatibility of the new CSPs provides flexibility in both analytical and preparative chromatographies.

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Dong, Yonghao, Tong Li, Jin Liu, Meixue Sun, Xingyu Chen, Yongjie Liu, and Pengjun Xu. "Sex- and stage-dependent expression patterns of odorant-binding and chemosensory protein genes in Spodoptera exempta." PeerJ 9 (September 13, 2021): e12132. http://dx.doi.org/10.7717/peerj.12132.

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As potential molecular targets for developing novel pest management strategies, odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) have been considered to initiate odor recognition in insects. Herein, we investigated the OBPs and CSPs in a major global crop pest (Spodoptera exempta). Using transcriptome analysis, we identified 40 OBPs and 33 CSPs in S. exempta, among which 35 OBPs and 29 CSPs had intact open reading frames. Sequence alignment indicated that 30 OBPs and 23 CSPs completely contained the conserved cysteines. OBPs of lepidopteran insects usually belonged to classical, minus-C, and plus-C groups. However, phylogenetic analyses indicated that we only identified 28 classical and seven minus-C OBPs in S. exempta, suggesting that we might have missed some typical OBPs in lepidopteran insects, probably due to their low expression levels. All of the CSPs from S. exempta clustered with the orthologs of other moths. The identification and expression of the OBPs and CSPs were well studied in insect adults by transcriptional analyses, and herein we used samples at different stages to determine the expression of OBPs and CSPs in S. exempta. Interestingly, our data indicated that several OBPs and CSPs were especially or more highly expressed in larvae or pupae than other stages, including three exclusively (SexeOBP13, SexeOBP16 and SexeCSP23) and six more highly (SexeOBP15, SexeOBP37, SexeCSP4, SexeCSP8, SexeCSP19, and SexeCSP33) expressed in larvae, two exclusively (SexeCSP6 and SexeCSP20) and three more highly (SexeOBP18, SexeCSP17, and SexeCSP26) expressed in pupae. Usually, OBPs and CSPs had both male- and female-biased expression patterns in adult antennae. However, our whole-body data indicated that all highly expressed OBPs and CSPs in adults were male-biased or did not differ, suggesting diverse OBP and CSP functions in insect adults. Besides identifying OBPs and CSPs as well as their expression patterns, these results provide a molecular basis to facilitate functional studies of OBPs and CSPs for exploring novel management strategies to control S. exempta.

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Wu, Ding-Tao, Wen Liu, Qiao-Hong Han, Ping Wang, Xian-Rong Xiang, Ye Ding, Li Zhao, Qing Zhang, Su-Qing Li, and Wen Qin. "Extraction Optimization, Structural Characterization, and Antioxidant Activities of Polysaccharides from Cassia Seed (Cassia obtusifolia)." Molecules 24, no. 15 (August 2, 2019): 2817. http://dx.doi.org/10.3390/molecules24152817.

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In order to explore Cassia seed polysaccharides (CSPs) as natural antioxidants for application in the functional-food industry, microwave-assisted extraction (MAE) was optimized for the extraction of CSPs by using a response surface methodology. Furthermore, the chemical structures and antioxidant activities of CSPs extracted by MAE and hot water extraction were investigated and compared. The maximum extraction yield of CSPs extracted by MAE (8.02 ± 0.19%) was obtained at the optimized extraction parameters as follows: microwave power (415 W), extraction time (7.0 min), and ratio of water to raw material (51 mL/g). Additionally, the contents of the uronic acids, molecular weight, ratio of constituent monosaccharides, intrinsic viscosities, and degrees of esterification of CSPs were significantly affected by the MAE method. Moreover, CSPs exhibited remarkable 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) ABTS, 2,2-diphenyl-1-(2,4,6-trinitrophenyl) hydrazyl DPPH, nitric oxide, and hydroxyl radical scavenging activities as well as reducing power. The high antioxidant activities observed in CSPs extracted by MAE could be partially attributed to its low molecular weights and high content of unmethylated galacturonic acid. Results indicate that the MAE method could be an efficient technique for the extraction of CSPs with high antioxidant activity, and CSPs could be further explored as functional food ingredients.

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Oyama, Tomomi, Toshio Nagai, Hiroshi Wada, Atsuhiko Thomas Naito, Katsuhisa Matsuura, Koji Iwanaga, Toshinao Takahashi, et al. "Cardiac side population cells have a potential to migrate and differentiate into cardiomyocytes in vitro and in vivo." Journal of Cell Biology 176, no. 3 (January 29, 2007): 329–41. http://dx.doi.org/10.1083/jcb.200603014.

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Side population (SP) cells, which can be identified by their ability to exclude Hoechst 33342 dye, are one of the candidates for somatic stem cells. Although bone marrow SP cells are known to be long-term repopulating hematopoietic stem cells, there is little information about the characteristics of cardiac SP cells (CSPs). When cultured CSPs from neonatal rat hearts were treated with oxytocin or trichostatin A, some CSPs expressed cardiac-specific genes and proteins and showed spontaneous beating. When green fluorescent protein–positive CSPs were intravenously infused into adult rats, many more (∼12-fold) CSPs were migrated and homed in injured heart than in normal heart. CSPs in injured heart differentiated into cardiomyocytes, endothelial cells, or smooth muscle cells (4.4%, 6.7%, and 29% of total CSP-derived cells, respectively). These results suggest that CSPs are intrinsic cardiac stem cells and involved in the regeneration of diseased hearts.

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Lang, Elza A. S., and Marilis V. Marques. "Identification and Transcriptional Control of Caulobacter crescentus Genes Encoding Proteins Containing a Cold Shock Domain." Journal of Bacteriology 186, no. 17 (September 1, 2004): 5603–13. http://dx.doi.org/10.1128/jb.186.17.5603-5613.2004.

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ABSTRACT The cold shock proteins are small peptides that share a conserved domain, called the cold shock domain (CSD), that is important for nucleic acid binding. The Caulobacter crescentus genome has four csp genes that encode proteins containing CSDs. Three of these (cspA, cspB, and cspC) encode peptides of about 7 kDa and are very similar to the cold shock proteins of other bacteria. Analysis by reverse transcription-PCR of the fourth gene (cspD), which was previously annotated as encoding a 7-kDa protein, revealed that the mRNA is larger and probably encodes a putative 21-kDa protein, containing two CSDs. A search in protein sequences databases revealed that this new domain arrangement has thus far only been found among deduced peptides of α-proteobacteria. Expression of each Caulobacter csp gene was studied both in response to cold shock and to growth phase, and we have found that only cspA and cspB are induced by cold shock, whereas cspC and cspD are induced at stationary phase, with different induction rates. The transcription start sites were determined for each gene, and a deletion mapping of the cspD promoter region defined a sequence required for maximal levels of expression, indicating that regulation of this gene occurs at the transcriptional level. Deletion of cspA, but not cspD, caused a reduction in viability when cells were incubated at 10°C for prolonged times, suggesting that cspA is important for adaptation to a low temperature.

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Cooper, Martin C., Achref El Mouelhi, and Cyril Terrioux. "Variable Elimination in Binary CSPs." Journal of Artificial Intelligence Research 66 (October 30, 2019): 589–624. http://dx.doi.org/10.1613/jair.1.11295.

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We investigate rules which allow variable elimination in binary CSP (constraint satisfaction problem) instances while conserving satisfiability. We study variable-elimination rules based on the language of forbidden patterns enriched with counting and quantification over variables and values. We propose new rules and compare them, both theoretically and experimentally. We give optimised algorithms to apply these rules and show that each define a novel tractable class. Using our variable-elimination rules in preprocessing allowed us to solve more benchmark problems than without.

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Mouhoub, Malek. "Dynamic arc consistency for CSPs." International Journal of Knowledge-based and Intelligent Engineering Systems 13, no. 2 (August 28, 2009): 45–58. http://dx.doi.org/10.3233/jad-2009-0173.

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Wong, Michael S. "The Third Dedicated CSPS Annals." Annals of Plastic Surgery 72 (May 2014): S1. http://dx.doi.org/10.1097/sap.0000000000000260.

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Huber, Anna, Andrei Krokhin, and Robert Powell. "Skew Bisubmodularity and Valued CSPs." SIAM Journal on Computing 43, no. 3 (January 2014): 1064–84. http://dx.doi.org/10.1137/120893549.

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Jonsson, Peter, and Johan Thapper. "Tractability conditions for numeric CSPs." Theoretical Computer Science 715 (March 2018): 21–34. http://dx.doi.org/10.1016/j.tcs.2018.01.013.

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Maher, Michael J. "Local consistency for extended CSPs." Theoretical Computer Science 410, no. 46 (November 2009): 4769–83. http://dx.doi.org/10.1016/j.tcs.2009.07.042.

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Salido, Miguel A., and Federico Barber. "Distributed CSPs by graph partitioning." Applied Mathematics and Computation 183, no. 1 (December 2006): 491–98. http://dx.doi.org/10.1016/j.amc.2006.05.090.

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Carbonnel, Clément, Miguel Romero, and Stanislav Živný. "Point-Width and Max-CSPs." ACM Transactions on Algorithms 16, no. 4 (September 25, 2020): 1–28. http://dx.doi.org/10.1145/3409447.

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Gupta, D. K. "Using Tabu search in CSPS." Korean Journal of Computational & Applied Mathematics 8, no. 1 (January 2001): 181–97. http://dx.doi.org/10.1007/bf03011631.

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Zivan, Roie, and Amnon Meisels. "Concurrent search for distributed CSPs." Artificial Intelligence 170, no. 4-5 (April 2006): 440–61. http://dx.doi.org/10.1016/j.artint.2005.12.005.

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Mouhoub, Malek, and Amrudee Sukpan. "Conditional and composite temporal CSPs." Applied Intelligence 36, no. 1 (July 30, 2010): 90–107. http://dx.doi.org/10.1007/s10489-010-0246-z.

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Mouhoub, Malek, and Amrudee Sukpan. "Managing dynamic CSPs with preferences." Applied Intelligence 37, no. 3 (February 2, 2012): 446–62. http://dx.doi.org/10.1007/s10489-012-0338-z.

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Stynes, David, and Kenneth N. Brown. "Value ordering for quantified CSPs." Constraints 14, no. 1 (July 23, 2008): 16–37. http://dx.doi.org/10.1007/s10601-008-9052-1.

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Ray, Semanti, Rochelle Da Costa, Samriddhi Thakur, and Dipankar Nandi. "Salmonella Typhimurium encoded cold shock protein E is essential for motility and biofilm formation." Microbiology 166, no. 5 (May 1, 2020): 460–73. http://dx.doi.org/10.1099/mic.0.000900.

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The ability of bacteria to form biofilms increases their survival under adverse environmental conditions. Biofilms have enormous medical and environmental impact; consequently, the factors that influence biofilm formation are an important area of study. In this investigation, the roles of two cold shock proteins (CSP) during biofilm formation were investigated in Salmonella Typhimurium, which is a major foodborne pathogen. Among all CSP transcripts studied, the expression of cspE (STM14_0732) was higher during biofilm growth. The cspE deletion strain (ΔcspE) did not form biofilms on a cholesterol coated glass surface; however, complementation with WT cspE, but not the F30V mutant, was able to rescue this phenotype. Transcript levels of other CSPs demonstrated up-regulation of cspA (STM14_4399) in ΔcspE. The cspA deletion strain (ΔcspA) did not affect biofilm formation; however, ΔcspEΔcspA exhibited higher biofilm formation compared to ΔcspE. Most likely, the higher cspA amounts in ΔcspE reduced biofilm formation, which was corroborated using cspA over-expression studies. Further functional studies revealed that ΔcspE and ΔcspEΔcspA exhibited slow swimming but no swarming motility. Although cspA over-expression did not affect motility, cspE complementation restored the swarming motility of ΔcspE. The transcript levels of the major genes involved in motility in ΔcspE demonstrated lower expression of the class III (fliC, motA, cheY), but not class I (flhD) or class II (fliA, fliL), flagellar regulon genes. Overall, this study has identified the interplay of two CSPs in regulating two biological processes: CspE is essential for motility in a CspA-independent manner whereas biofilm formation is CspA-dependent.

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Gupta, Radhey S., Sohail Naushad, and Sheridan Baker. "Phylogenomic analyses and molecular signatures for the class Halobacteria and its two major clades: a proposal for division of the class Halobacteria into an emended order Halobacteriales and two new orders, Haloferacales ord. nov. and Natrialbales ord. nov., containing the novel families Haloferacaceae fam. nov. and Natrialbaceae fam. nov." International Journal of Systematic and Evolutionary Microbiology 65, Pt_3 (March 1, 2015): 1050–69. http://dx.doi.org/10.1099/ijs.0.070136-0.

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The Halobacteria constitute one of the largest groups within the Archaea . The hierarchical relationship among members of this large class, which comprises a single order and a single family, has proven difficult to determine based upon 16S rRNA gene trees and morphological and physiological characteristics. This work reports detailed phylogenetic and comparative genomic studies on >100 halobacterial (haloarchaeal) genomes containing representatives from 30 genera to investigate their evolutionary relationships. In phylogenetic trees reconstructed on the basis of 32 conserved proteins, using both neighbour-joining and maximum-likelihood methods, two major clades (clades A and B) encompassing nearly two-thirds of the sequenced haloarchaeal species were strongly supported. Clades grouping the same species/genera were also supported by the 16S rRNA gene trees and trees for several individual highly conserved proteins (RpoC, EF-Tu, UvrD, GyrA, EF-2/EF-G). In parallel, our comparative analyses of protein sequences from haloarchaeal genomes have identified numerous discrete molecular markers in the form of conserved signature indels (CSI) in protein sequences and conserved signature proteins (CSPs) that are found uniquely in specific groups of haloarchaea. Thirteen CSIs in proteins involved in diverse functions and 68 CSPs that are uniquely present in all or most genome-sequenced haloarchaea provide novel molecular means for distinguishing members of the class Halobacteria from all other prokaryotes. The members of clade A are distinguished from all other haloarchaea by the unique shared presence of two CSIs in the ribose operon protein and small GTP-binding protein and eight CSPs that are found specifically in members of this clade. Likewise, four CSIs in different proteins and five other CSPs are present uniquely in members of clade B and distinguish them from all other haloarchaea. Based upon their specific clustering in phylogenetic trees for different gene/protein sequences and the unique shared presence of large numbers of molecular signatures, members of clades A and B are indicated to be distinct from all other haloarchaea because of their uniquely shared evolutionary histories. Based upon these results, it is proposed that clades A and B be recognized as two new orders, Natrialbales ord. nov. and Haloferacales ord. nov., within the class Halobacteria , containing the novel families Natrialbaceae fam. nov. and Haloferacaceae fam. nov. Other members of the class Halobacteria that are not members of these two orders will remain part of the emended order Halobacteriales in an emended family Halobacteriaceae .

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Cornelisse, Vincent J., David Priest, Christopher K. Fairley, Sandra Walker, Catriona S. Bradshaw, Tiffany Phillips, and Eric PF Chow. "The frequency of kissing as part of sexual activity differs depending on how men meet their male casual sexual partners." International Journal of STD & AIDS 29, no. 6 (December 19, 2017): 598–602. http://dx.doi.org/10.1177/0956462417748717.

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Previous studies have shown that men who have sex with men (MSM) who use smartphone dating applications (apps) are at higher risk of gonorrhoea, but not HIV. We have hypothesised that kissing may be a risk factor for oropharyngeal gonorrhoea. We measured differences in kissing practices among MSM who use different methods to find male casual sexual partners (CSPs). If MSM who use apps kiss more CSPs, then this may help to explain why these men are at increased risk of gonorrhoea but not HIV. This was a cross-sectional questionnaire-based study of MSM attending Melbourne Sexual Health Centre, Australia, between March and September 2015. We measured differences in kissing practices among MSM who use different methods to find male casual sexual partners (CSPs). The questionnaire included questions about numbers of CSPs, numbers of CSPs kissed, and how men found CSPs. We surveyed 753 MSM with a median age of 29 years (interquartile range 25–36). Six hundred and one men (79.8%) reported using apps to find CSPs in the last three months. Users of apps had a higher number of CSPs than non-users (5.0 vs. 3.2; p < 0.001). Users of apps kissed a higher number (4.6 vs. 2.2; p < 0.001), and a higher proportion (90.4% vs. 71.0%; p < 0.001) of CSPs compared to non-users. We are currently investigating whether kissing is a significant mode of transmission of gonorrhoea, and if this proves correct then this study suggests that users of apps would particularly benefit from health promotion that addresses this mode of transmission.

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Uppal, Sheetal, and Narendra Jawali. "Cyclic AMP receptor protein (CRP) regulates the expression of cspA, cspB, cspG and cspI, members of cspA family, in Escherichia coli." Archives of Microbiology 197, no. 3 (January 31, 2015): 497–501. http://dx.doi.org/10.1007/s00203-015-1085-4.

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Raikar, Prachi, Bannimath M. Gurupadayya, Sripuram Subramanyam, and Gunnam Srinivasu. "Analysis of Orphenadrine Citrate in Various Chiral Stationary Phases: A Comparative Study." Current Chromatography 7, no. 2 (December 29, 2020): 91–100. http://dx.doi.org/10.2174/2213240607999200621202159.

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Background: Polysaccharide based chiral stationary phases (CSPs) were used to perform enantiomeric separation of Orphenadrine Citrate by Ultra-Fast Liquid Chromatography (UFLC) technique. Trials were conducted using the polar mode, reverse phase mode and normal phase mode. Amylose and Cellulose-based CSPs were used for the same. Materials and Methods: Eight Amylose-based CSPs and four Cellulose-based CSPs were used in the reverse phase mode. Five Amylose-based CSPs and two Cellulose-based CSPs were used in polar mode. The only Cellulose-based CSP used in the normal phase mode could effectively separate Orphenadrine Citrate enantiomers with a good resolution. Results and Discussion: Successful enantioseparation was obtained using Chiralcel OD-H containing Cellulose tris (3, 5- dimethylphenylcarbamate) as a chiral selector and n-hexane: Ethanol: Diethylamine (95: 05: 0.1, v/v/v) as the mobile phase. The developed method was validated in accordance with ICH guidelines (Q2R1). Conclusion: The proposed objectives were successfully accomplished as the developed method could effectively resolve Orphenadrine Citrate enantiomers.

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Journal articles on the topic 'CSPs'

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