Статті в журналах: "L18A"

1

Aoyama, Yuji, Yuen-Ling Chan, Oded Meyuhas, and Ira G. Wool. "The primary structure of rat ribosomal protein L18a." FEBS Letters 247, no. 2 (April 24, 1989): 242–46. http://dx.doi.org/10.1016/0014-5793(89)81344-4.

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2

Han, Sun‐Young, and Mieyoung Choi. "Human ribosomal protein L18a interacts with hnRNP E1." Animal Cells and Systems 12, no. 3 (January 2008): 143–48. http://dx.doi.org/10.1080/19768354.2008.9647167.

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3

Sommer, W., C. Arlinde, L. Caberlotto, A. Thorsell, P. Hyytia, and M. Heilig. "CNS expression of diacylglycerol kinase iota and L18A mRNAs." Molecular Psychiatry 6, no. 1 (December 14, 2000): 5. http://dx.doi.org/10.1038/sj.mp.4000831.

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4

Dhar, D., K. Mapa, R. Pudi, P. Srinivasan, K. Bodhinathan, and S. Das. "Human ribosomal protein L18a interacts with hepatitis C virus internal ribosome entry site." Archives of Virology 151, no. 3 (September 30, 2005): 509–24. http://dx.doi.org/10.1007/s00705-005-0642-6.

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5

Ntwasa, Monde, Sean G. S. C. Buchanan, and Nicholas J. Gay. "Drosophila ribosomal protein L18a: cDNA sequence, expression and chromosomal localization of the gene." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1218, no. 2 (June 1994): 210–12. http://dx.doi.org/10.1016/0167-4781(94)90014-0.

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6

Yant, Stephen R., Julie Park, Yong Huang, Jacob Giehm Mikkelsen, and Mark A. Kay. "Mutational Analysis of the N-Terminal DNA-Binding Domain of Sleeping Beauty Transposase: Critical Residues for DNA Binding and Hyperactivity in Mammalian Cells." Molecular and Cellular Biology 24, no. 20 (October 15, 2004): 9239–47. http://dx.doi.org/10.1128/mcb.24.20.9239-9247.2004.

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ABSTRACT The N-terminal domain of the Sleeping Beauty (SB) transposase mediates transposon DNA binding, subunit multimerization, and nuclear translocation in vertebrate cells. For this report, we studied the relative contributions of 95 different residues within this multifunctional domain by large-scale mutational analysis. We found that each of four amino acids (leucine 25, arginine 36, isoleucine 42, and glycine 59) contributes to DNA binding in the context of the N-terminal 123 amino acids of SB transposase, as indicated by electrophoretic mobility shift analysis, and to functional activity of the full-length transposase, as determined by a quantitative HeLa cell-based transposition assay. Moreover, we show that amino acid substitutions within either the putative oligomerization domain (L11A, L18A, L25A, and L32A) or the nuclear localization signal (K104A and R105A) severely impair its ability to mediate DNA transposition in mammalian cells. In contrast, each of 10 single amino acid changes within the bipartite DNA-binding domain is shown to greatly enhance SB's transpositional activity in mammalian cells. These hyperactive mutations functioned synergistically when combined and are shown to significantly improve transposase affinity for transposon end sequences. Finally, we show that enhanced DNA-binding activity results in improved cleavage kinetics, increased SB element mobilization from host cell chromosomes, and dramatically improved gene transfer capabilities of SB in vivo in mice. These studies provide important insights into vertebrate transposon biology and indicate that Sleeping Beauty can be readily improved for enhanced genetic research applications in mammals.

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7

Gazda, Hanna T., Mee Rie Sheen, Natasha Darras, Hal Shneider, Colin A. Sieff, Sarah E. Ball, Edyta Niewiadomska, et al. "Mutations of the Genes for Ribosomal Proteins L5 and L11 Are a Common Cause of Diamond-Blackfan Anemia." Blood 110, no. 11 (November 16, 2007): 421. http://dx.doi.org/10.1182/blood.v110.11.421.421.

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Abstract Diamond-Blackfan anemia (DBA), a form of congenital red cell aplasia with marked clinical heterogeneity and increased risk of malignancy, has been associated with mutations in ribosomal protein (RP) gene RPS19 in 25% of probands and in RPS24 or RPS17 in ∼2% of patients. Thus, DBA appears to be a disorder of ribosome synthesis. To test the hypothesis that mutations in other RP genes may also cause DBA, we carried out direct sequencing of candidate RP genes. Genomic DNA samples from 96 unrelated DBA probands (14 familial and 82 sporadic cases) without RPS19 or RPS24 mutations were screened for mutations in RPS3a, RPS13, and RPS16 (previous studies revealed that RPs S19, S24, S3a, S13, and S16 are involved in binding of eIF-2 to the 40S subunit); RP genes L18, L13A, L36, L28, L18A, L40, S5, S9, S11, and S28 (located on chromosome 19); and RP genes, L5, L11, L22, S8, and S27 (on chromosome 1). PCR primers were designed to amplify the coding exons and intron/exon boundaries. We found multiple mutations in two RP genes, L5 and L11. Subsequently we sequenced these two genes in 42 additional DNA samples from DBA probands. In total, we screened 5′UTR, promoter and coding regions, and exon/intron boundaries of RPL5 and RPL11 in 138 DBA unrelated probands. We identified 14 mutations in RPL5 in 138 probands (∼10%), 13 of which are nonsense mutations, deletions or insertions of 1–5 nucleotides causing frameshift and premature termination. One missense mutation, 418G>A, results in a G140S substitution. We found nine mutations in RPL11 in138 DBA probands (6.5%), including five acceptor or donor splice site mutations (introns 1–4) and four deletions or insertions of 1–4 nucleotides causing frameshifts (codons 32-120). None of these sequence changes were found on the NCBI (http://www.ncbi.nlm.nih.gov/SNP/) or the HapMap (http://www.hapmap.org/) SNP lists. Both genes, as well as RPL23 have recently been demonstrated by others to activate the p53 tumor suppressor protein by inhibiting MDM2-mediated p53 ubiquitination and degradation. Moreover, knockdown of any of these genes by siRNAs markedly reduced p53 induction by the ribosomal biogenesis stressor, actinomycin-D. These findings suggest that DBA patients with mutated L5 and L11 proteins may have inadequate p53 pathway activation and (consistent with clinical observations) be at increased risk for neoplasia. We are currently investigating the role of RPL5 and RPL11 mutations in ribosomal biogenesis and in the p53-mediated cell cycle arrest and apoptosis in DBA patients.

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8

Zhang, Yihao, Yuying Jin, Qian Gong, Zhi Li, Lihong Zhao, Xiao Han, Jinglong Zhou, Fuguang Li, and Zhaoen Yang. "Mechanismal analysis of resistance to Verticillium dahliae in upland cotton conferred by overexpression of RPL18A-6 (Ribosomal Protein L18A-6)." Industrial Crops and Products 141 (December 2019): 111742. http://dx.doi.org/10.1016/j.indcrop.2019.111742.

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9

Sommer, W., C. Arlinde, L. Caberlotto, A. Thorsell, P. Hyytia, and M. Heilig. "Differential expression of diacylglycerol kinase iota and L18A mRNAs in the brains of alcohol-preferring AA and alcohol-avoiding ANA rats." Molecular Psychiatry 6, no. 1 (December 14, 2000): 103–8. http://dx.doi.org/10.1038/sj.mp.4000823.

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10

Mottaghi-Dastjerdi, N., M. Soltany-Rezaee-Rad, Z. Sepehrizadeh, G. Roshandel, F. Ebrahimifard, and N. Setayesh. "Identification of novel genes involved in gastric carcinogenesis by suppression subtractive hybridization." Human & Experimental Toxicology 34, no. 1 (May 8, 2014): 3–11. http://dx.doi.org/10.1177/0960327114532386.

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Gastric cancer (GC) is one of the most common and life-threatening types of malignancies. Identification of the differentially expressed genes in GC is one of the best approaches for establishing new diagnostic and therapeutic targets. Furthermore, these investigations could advance our knowledge about molecular biology and the carcinogenesis of this cancer. To screen for the overexpressed genes in gastric adenocarcinoma, we performed suppression subtractive hybridization (SSH) on gastric adenocarcinoma tissue and the corresponding normal gastric tissue, and eight genes were found to be overexpressed in the tumor compared with those of the normal tissue. The genes were ribosomal protein L18A, RNase H2 subunit B, SEC13, eukaryotic translation initiation factor 4A1, tetraspanin 8, cytochrome c oxidase subunit 2, NADH dehydrogenase subunit 4, and mitochondrially encoded ATP synthase 6. The common functions among the identified genes include involvement in protein synthesis, involvement in genomic stability maintenance, metastasis, metabolic improvement, cell signaling pathways, and chemoresistance. Our results provide new insights into the molecular biology of GC and drug discovery: each of the identified genes could be further investigated as targets for prognosis evaluation, diagnosis, treatment, evaluation of the response to new anticancer drugs, and determination of the molecular pathogenesis of GC.

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11

Millership, Joanne E., Daniel C. Devor, Kirk L. Hamilton, Corina M. Balut, Jason I. E. Bruce, and Ian M. Fearon. "Calcium-activated K+ channels increase cell proliferation independent of K+ conductance." American Journal of Physiology-Cell Physiology 300, no. 4 (April 2011): C792—C802. http://dx.doi.org/10.1152/ajpcell.00274.2010.

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The intermediate-conductance calcium-activated potassium channel (IK1) promotes cell proliferation of numerous cell types including endothelial cells, T lymphocytes, and several cancer cell lines. The mechanism underlying IK1-mediated cell proliferation was examined in human embryonic kidney 293 (HEK293) cells expressing recombinant human IK1 (hIK1) channels. Inhibition of hIK1 with TRAM-34 reduced cell proliferation, while expression of hIK1 in HEK293 cells increased proliferation. When HEK293 cells were transfected with a mutant (GYG/AAA) hIK1 channel, which neither conducts K+ ions nor promotes Ca2+ entry, proliferation was increased relative to mock-transfected cells. Furthermore, when HEK293 cells were transfected with a trafficking mutant (L18A/L25A) hIK1 channel, proliferation was also increased relative to control cells. The lack of functional activity of hIK1 mutants at the cell membrane was confirmed by a combination of whole cell patch-clamp electrophysiology and fura-2 imaging to assess store-operated Ca2+ entry and cell surface immunoprecipitation assays. Moreover, in cells expressing hIK1, inhibition of ERK1/2 and JNK kinases, but not of p38 MAP kinase, reduced cell proliferation. We conclude that functional K+ efflux at the plasma membrane and the consequent hyperpolarization and enhanced Ca2+ entry are not necessary for hIK1-induced HEK293 cell proliferation. Rather, our data suggest that hIK1-induced proliferation occurs by a direct interaction with ERK1/2 and JNK signaling pathways.

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12

Chan, Y. L., J. Olvera, and I. G. Wool. "The Primary Structures of Rat Ribosomal Proteins: The Characterization of the cDNAs for S21 and L39; Corrections in the Sequences of L7 and L18a and the Identification of L33." Biochemical and Biophysical Research Communications 213, no. 3 (August 1995): 1042–50. http://dx.doi.org/10.1006/bbrc.1995.2233.

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13

Pagani, L., A. Bacmann, F. Motte, L. Cambrésy, M. Fich, G. Lagache, M. A. Miville-Deschênes, J. R. Pardo, and A. J. Apponi. "L183 (L134N) Revisited." Astronomy & Astrophysics 417, no. 2 (March 19, 2004): 605–13. http://dx.doi.org/10.1051/0004-6361:20034087.

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14

Pagani, L., J. R. Pardo, A. J. Apponi, A. Bacmann, and S. Cabrit. "L183 (L134N) revisited." Astronomy & Astrophysics 429, no. 1 (December 13, 2004): 181–92. http://dx.doi.org/10.1051/0004-6361:20041044.

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15

Pagani, L., G. Lagache, A. Bacmann, F. Motte, L. Cambrésy, M. Fich, D. Teyssier, et al. "L183 (L134N) Revisited." Astronomy & Astrophysics 406, no. 3 (August 2003): L59—L62. http://dx.doi.org/10.1051/0004-6361:20030903.

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16

Donahue, John P., Rebecca T. Levinson, Jonathan H. Sheehan, Lorraine Sutton, Harry E. Taylor, Jens Meiler, Richard T. D'Aquila, and Chisu Song. "Genetic Analysis of the Localization of APOBEC3F to Human Immunodeficiency Virus Type 1 Virion Cores." Journal of Virology 89, no. 4 (December 10, 2014): 2415–24. http://dx.doi.org/10.1128/jvi.01981-14.

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ABSTRACTMembers of the APOBEC3 family of cytidine deaminases vary in their proportions of a virion-incorporated enzyme that is localized to mature retrovirus cores. We reported previously that APOBEC3F (A3F) was highly localized into mature human immunodeficiency virus type 1 (HIV-1) cores and identified that L306 in the C-terminal cytidine deaminase (CD) domain contributed to its core localization (C. Song, L. Sutton, M. Johnson, R. D'Aquila, J. Donahue, J Biol Chem287:16965–16974, 2012,http://dx.doi.org/10.1074/jbc.M111.310839). We have now determined an additional genetic determinant(s) for A3F localization to HIV-1 cores. We found that one pair of leucines in each of A3F's C-terminal and N-terminal CD domains jointly determined the degree of localization of A3F into HIV-1 virion cores. These are A3F L306/L368 (C-terminal domain) and A3F L122/L184 (N-terminal domain). Alterations to one of these specific leucine residues in either of the two A3F CD domains (A3F L368A, L122A, and L184A) decreased core localization and diminished HIV restriction without changing virion packaging. Furthermore, double mutants in these leucine residues in each of A3F's two CD domains (A3F L368A plus L184A or A3F L368A plus L122A) still were packaged into virions but completely lost core localization and anti-HIV activity. HIV virion core localization of A3F is genetically separable from its virion packaging, and anti-HIV activity requires some core localization.IMPORTANCESpecific leucine-leucine interactions are identified as necessary for A3F's core localization and anti-HIV activity but not for its packaging into virions. Understanding these signals may lead to novel strategies to enhance core localization that may augment effects of A3F against HIV and perhaps of other A3s against retroviruses, parvoviruses, and hepatitis B virus.

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17

Lillehoj, Erik P., Beom T. Kim, and K. Chul Kim. "Identification ofPseudomonas aeruginosaflagellin as an adhesin for Muc1 mucin." American Journal of Physiology-Lung Cellular and Molecular Physiology 282, no. 4 (April 1, 2002): L751—L756. http://dx.doi.org/10.1152/ajplung.00383.2001.

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We reported previously that Muc1 mucin on the epithelial cell surface is an adhesion site for Pseudomonas aeruginosa (Lillehoj EP, Hyun SW, Kim BT, Zhang XG, Lee DI, Rowland S, and Kim KC. Am J Physiol Lung Cell Mol Physiol 280: L181–L187, 2001). The present study was designed to identify the adhesin(s) responsible for bacterial binding to Muc1 mucin using genetic and biochemical approaches. Chinese hamster ovary (CHO) cells stably transfected with a Muc1 cDNA (CHO-Muc1) or empty plasmid (CHO-X) were compared for adhesion of P. aeruginosa strain PAK. Our results showed that 1) wild-type PAK and isogenic mutant strains lacking pili (PAK/NP) or flagella cap protein (PAK/ fliD) demonstrated significantly increased binding to CHO-Muc1 cells, whereas flagellin-deficient (PAK/ fliC) bacteria were no more adherent to CHO-Muc1 than CHO-X cells, and 2) P. aeruginosa adhesion was blocked by pretreatment of bacteria with antibody to flagellin or pretreatment of CHO-Muc1 cells with purified flagellin. We conclude that flagellin is an adhesin of P. aeruginosa responsible for its binding to Muc1 mucin on the epithelial cell surface.

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18

Zhou, Jian-Jun, Xing-Wu Zheng, and Yu-Xi Chen. "L183, a Quiescent Core?" Chinese Journal of Astronomy and Astrophysics 1, no. 3 (June 2001): 250–56. http://dx.doi.org/10.1088/1009-9271/1/3/250.

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19

Lee, M., and K. Struhl. "A severely defective TATA-binding protein-TFIIB interaction does not preclude transcriptional activation in vivo." Molecular and Cellular Biology 17, no. 3 (March 1997): 1336–45. http://dx.doi.org/10.1128/mcb.17.3.1336.

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In yeast cells, mutations in the TATA-binding protein (TBP) that disrupt the interaction with the TATA element or with TFIIA can selectively impair the response to acidic activator proteins. We analyzed the transcriptional properties of TBP derivatives in which residues that directly interact with TFIIB were replaced by alanines. Surprisingly, a derivative with a 50-fold defect in TBP-TFIIB-TATA complex formation in vitro (E188A) supports viability and responds efficiently to activators in vivo. The E186A derivative, which displays a 100-fold defect in TBP-TFIIB-TATA complex formation, does not support viability, yet it does respond to activators. Conversely, the L189A mutation, which has the mildest effect on the interaction with TFIIB (10-fold), can abolish transcriptional activation and cell viability when combined with mutations on the DNA-binding surface. This "synthetic lethal" effect is not observed with E188A, suggesting that the previously described role of L189 in transcriptional activation may be related to its location on the DNA-binding surface and not to its interaction with TFIIB. Finally, when using TBP mutants defective on multiple interaction surfaces, we observed synthetic lethal effects between mutations on the TFIIA and TFIIB interfaces but found that mutations implicated in association with polymerase II and TFIIF did not have significant effects in vivo. Taken together, these results argue that, unlike the TBP-TATA and TBP-TFIIA interactions, the TBP-TFIIB interaction is not generally limiting for transcriptional activation in vivo.

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20

Jahagirdar, Devashree, Shruti Purohit, and Nilesh K. Sharma. "Combinatorial Use of DNA Ligase Inhibitor L189 and Temozolomide Potentiates Cell Growth Arrest in HeLa." Current Cancer Therapy Reviews 15, no. 1 (February 22, 2019): 65–73. http://dx.doi.org/10.2174/1573394714666180216150332.

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Introduction: The issues of carcinoma drug resistance to alkylating agents such as Temozolomide (TMZ) are considered as a major concern in therapeutics. The potential ways to achieve better cancer cell growth arrest and cytotoxicity have been suggested including the combinatorial use of DNA repair protein inhibitors and genotoxic drug TMZ. Here, authors assess the ability of DNA ligase inhibitor (L189) to modulate TMZ mediated HeLa cell growth arrest and cytotoxicity. Materials and Methods: Here, authors have employed Trypan blue dye exclusion and propidium iodide (PI) using FACS to determine HeLa cell viability after exposure to TMZ with or without L189 inhibitor. Additionally, authors show the DNA ligase III protein level using ELISA and fluorescent microscopy to support the observed effects of combinatorial use of TMZ and L189. Results: In this paper, data indicate that the addition of L189 produced appreciable decrease in the growth of HeLa cells. However, combined treatment of L189 and TMZ showed enhanced TMZinduced HeLa growth arrest possibly in G2/M cell cycle phase without employing cell death mechanisms. Conclusions: These results underscore the combinatorial treatment using TMZ and L189 to bring desirable cancer cell growth arrest and future molecular study to dissect out the participating pathways.

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21

Clemens, Dan P. "THE OUTER MAGNETIC FIELD OF L183." Astrophysical Journal 748, no. 1 (February 29, 2012): 18. http://dx.doi.org/10.1088/0004-637x/748/1/18.

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22

Chaichanit, Netnapa, Monwadee Wonglapsuwan, and Wilaiwan Chotigeat. "Ribosomal protein L10A and signaling pathway." Gene 674 (October 2018): 170–77. http://dx.doi.org/10.1016/j.gene.2018.06.081.

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23

Kuwahara, Ippei, Erik P. Lillehoj, Akinori Hisatsune, Wenju Lu, Yoichiro Isohama, Takeshi Miyata, and K. Chul Kim. "Neutrophil elastase stimulatesMUC1gene expression through increased Sp1 binding to theMUC1promoter." American Journal of Physiology-Lung Cellular and Molecular Physiology 289, no. 2 (August 2005): L355—L362. http://dx.doi.org/10.1152/ajplung.00040.2005.

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We previously reported MUC1 was a cell surface receptor for Pseudomonas aeruginosa, and binding of bacteria to cells was significantly reduced by pretreatment with neutrophil elastase (NE) (Lillehoj EP, Hyun SW, Kim BT, Zhang XG, Lee DI, Rowland S, and Kim KC. Am J Physiol Lung Cell Mol Physiol 280: L181–L187, 2001). The current study was conducted to ascertain NE effects on MUC1 gene transcription, and MUC1 protein synthesis and degradation. A549 human lung carcinoma cells treated with NE exhibited significantly higher MUC1 protein levels in detergent lysates compared with cells treated with vehicle alone. Also, MUC1 protein shed into cell-conditioned medium was rapidly and completely degraded by NE. Actinomycin D blocked NE-stimulated increase in MUC1 protein expression, suggesting a mechanism of increased gene transcription that was confirmed by measurement of quantitatively greater MUC1 mRNA levels in NE-treated cells compared with controls. However, NE did not alter MUC1 mRNA stability, implying increased de novo transcription induced by the protease. NE increased promoter activity in A549 cells transfected with MUC1 gene promoter-luciferase reporter plasmid. This effect of NE was completely blocked by mithramycin A, an inhibitor of Sp1, as well as mutation of one of the putative Sp1 binding sites in MUC1 promoter located at −99/−90 relative to transcription initiation site. EMSA revealed NE enhanced binding of Sp1 to this 10-bp segment in a time-dependent manner. These results indicate the increase in MUC1 gene transcription by NE is mediated through increase in Sp1 binding to −99/−90 segment of MUC1 promoter.

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24

Di Fermo, Paola, Tecla Ciociola, Silvia Di Lodovico, Simonetta D’Ercole, Morena Petrini, Laura Giovati, Stefania Conti, Mara Di Giulio, and Luigina Cellini. "Antimicrobial Peptide L18R Displays a Modulating Action against Inter-Kingdom Biofilms in the Lubbock Chronic Wound Biofilm Model." Microorganisms 9, no. 8 (August 21, 2021): 1779. http://dx.doi.org/10.3390/microorganisms9081779.

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Chronic wound infections represent an important health problem due to the reduced response to antimicrobial treatment of the pathogens organized in structured biofilms. This study investigated the effects of the previously described antifungal peptide L18R against three representative wound pathogens: Staphylococcus aureus, Pseudomonas aeruginosa, and Candida albicans. The antimicrobial activity of L18R was evaluated (i) against single planktonic microbial populations; (ii) on single, dual, and triadic species of biofilms in both the early stage and mature stage; and (iii) in the polymicrobial Lubbock chronic wound biofilm (LCWB) model, mimicking spatial microbial colonization. This study used the evaluation of CFUs, biofilm biomass detection, and confocal and scanning electron microscopy analysis. L18R showed a significant antimicrobial activity against planktonic microorganisms and was able to differentially reduce the biomass of monomicrobial biofilms. No reduction of biomass was observed against the polymicrobial biofilm. In mature LCWB, L18R caused a moderate reduction in total CFU number, with a variable effect on the different microorganisms. Microscopy images confirmed a predominant presence of P.aeruginosa and a lower percentage of C. albicans cells. These findings suggest a modulating action of L18R and recommend further studies on its potential role in chronic wound management in association with conventional antibiotics or alternative treatments.

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25

Eric Almeida Xavier and Fabrício Castro Machado. "L18R a peptide with potential against melanoma." Open Access Research Journal of Biology and Pharmacy 4, no. 2 (April 30, 2022): 022–27. http://dx.doi.org/10.53022/oarjbp.2022.4.2.0038.

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Peptides have fantastic functions like defensins that make up the natural defense in different species from vertebrates to bacteria. Another fantastic example are prions that cause transmissible diseases devoid of nucleic acid. So, because of their high specificity, peptides can be used for different therapeutic goals. In this work we describe in vitro action of a peptide named L18R this sequence is part of a group of four distinct sequences that were previously tested and showed activity against fungi and tumors, which motivated us to investigate this activity against murine B16F10 melanoma. Thus, has been demonstrated that L18R had activity against tumor, for interfering in cell viability, migration and in cell cycle. To conclude, the present work suggests a functional molecule against tumor.

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26

Kasai, Hide, Daita Nadano, Eiko Hidaka, Kayoko Higuchi, Masatomo Kawakubo, Taka-Aki Sato, and Jun Nakayama. "Differential Expression of Ribosomal Proteins in Human Normal and Neoplastic Colorectum." Journal of Histochemistry & Cytochemistry 51, no. 5 (May 2003): 567–73. http://dx.doi.org/10.1177/002215540305100502.

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Ribosomal proteins are a major component of ribosomes and play critical roles in protein biosynthesis. Recently it has been shown that the ribosomal proteins also function during various cellular processes that are independent of protein biosynthesis therefore called extraribosomal functions. In this study we have, for the first time, determined the expression profile of 12 ribosomal proteins (Sa, S8, S11, S12, S18, S24, L7, L13a, L18, L28, L32, and L35a) in normal epithelia of human colorectal mucosa using immunohistochemistry (IHC) and then compared their expression patterns with those of colorectal cancer. In the normal mucosa, ribosomal proteins were largely associated with the ribosomes of mucosal epithelia, and the expression level of ribosomal proteins, except for S11 and L7 proteins, was markedly increased in associated with maturation of the mucosal cells. On the other hand, these ribosomal proteins were markedly decreased in colorectal cancer compared with the normal mucosa. By contrast, S11 and L7 ribosomal proteins were rarely associated with the ribosomes of colorectal epithlia except immature mucosal cells, whereas their expression levels were significantly enchanced in colorectal cancer cells. In addition, L7 ribosomal protien was detected in the secretory granules of the enterochromaffin cells in the colorectal mucosa and in carcinoma cells expressing chromogranin A. These results indicate that the expression of ribosomal proteins is differentially regulated not only in normal mucosa but also in carcinoma of human colorectum, and suggest an extraribosomal function of L7 ribosomal protein in neuroendocrine function.

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27

Eberhard, David A., Larry R. Karns, Scott R. VandenBerg, and Carl E. Creutz. "Control of the nuclear-cytoplasmic partitioning of annexin II by a nuclear export signal and by p11 binding." Journal of Cell Science 114, no. 17 (September 1, 2001): 3155–66. http://dx.doi.org/10.1242/jcs.114.17.3155.

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This study investigated mechanisms controlling the nuclear-cytoplasmic partitioning of annexin II (AnxII). AnxII and its ligand, p11, were localized by immunofluorescence to the cytoplasmic compartment of U1242MG cells, with minimal AnxII or p11 detected within nuclei. Similarly, GFP-AnxII and GFP-p11 chimeras localized to the endogenous proteins. Likewise, GFP-AnxII(1-22) was excluded from nuclei, whereas GFP-AnxII(23-338) and GFP alone were distributed throughout the cells. Immunoprecipitation and biochemical studies showed that GFP-AnxII did not form heteromeric complexes with endogenous p11 and AnxII. Thus, the AnxII N-tail is necessary and sufficient to cause nuclear exclusion of the GFP fusion protein but this does not involve p11 binding. A nuclear export signal consensus sequence was found in the AnxII 3-12 region. The consensus mutant GFP-AnxII(L10A/L12A) confirmed that these residues are necessary for nuclear exclusion. The nuclear exclusion of GFP-AnxII(1-22) was temperature-dependent and reversible, and the nuclear export inhibitor leptomycin B (LmB) caused GFP-AnxII or overexpressed AnxII monomer to accumulate in nuclei. Therefore, AnxII monomer can enter the nucleus and is actively exported. However, LmB had little effect on the localization of AnxII/p11 complex in U1242MG cells, indicating that the complex is sequestered in the cytoplasm. By contrast, LmB treatment of v-src-transformed fibroblasts caused endogenous AnxII to accumulate in nuclei. The LmB-induced nuclear accumulation of AnxII was accelerated by pervanadate and inhibited by genistein, suggesting that phosphorylation promotes nuclear entry of AnxII. Thus, nuclear exclusion of AnxII results from nuclear export of the monomer and sequestration of AnxII/p11 complex, and may be modulated by phosphorylation.

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McElroy, Mary C., Jean-François Pittet, Lennell Allen, Jeanine P. Wiener-Kronish, and Leland G. Dobbs. "Biochemical detection of type I cell damage after nitrogen dioxide-induced lung injury in rats." American Journal of Physiology-Lung Cellular and Molecular Physiology 273, no. 6 (December 1, 1997): L1228—L1234. http://dx.doi.org/10.1152/ajplung.1997.273.6.l1228.

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We have previously shown that injury to lung epithelial type I cells can be detected biochemically by measuring the airway fluid content of a type I cell-specific protein, rTI40, in a model of severe acute lung injury [M. C. McElroy, J.-F. Pittet, S. Hashimoto, L. Allen, J. P. Wiener-Kronish, and L. G. Dobbs. Am. J. Physiol. 268 ( Lung Cell. Mol. Physiol. 12): L181–L186, 1995]. The first objective of the present study was to evaluate the utility of rTI40 in the assessment of alveolar injury in a model of milder acute lung injury. Rats were exposed to 18 parts/million NO2 for 12 h; control rats received filtered air for 12 h. In NO2-exposed rats, the total amount of rTI40 in bronchoalveolar fluid was elevated 2-fold compared with control values ( P < 0.001); protein concentration was 8.5-fold of control values ( P < 0.001). The increase in rTI40 was associated with morphological evidence of injury to type I cells limited to the proximal alveolar regions of the lung. The second objective was to correlate the severity of alveolar type I cell injury with functional measurements of lung epithelial barrier integrity. NO2 inhalation stimulated distal air space fluid clearance despite a significant increase in lung endothelial and epithelial permeability to protein. These data demonstrate that rTI40 is a useful biochemical marker for mild focal injury and that exposure to NO2 alters lung barrier function. Taken together with our earlier studies, these results suggest that the quantity of recoverable rTI40 can be used as an index of the severity of damage to the alveolar epithelium.

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Lattanzi, Valerio, Luca Bizzocchi, Anton I. Vasyunin, Jorma Harju, Barbara M. Giuliano, Charlotte Vastel, and Paola Caselli. "Molecular complexity in pre-stellar cores: a 3 mm-band study of L183 and L1544." Astronomy & Astrophysics 633 (January 2020): A118. http://dx.doi.org/10.1051/0004-6361/201936884.

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Context. Pre-stellar cores (PSCs) are units of star formation. Besides representing early stages of the dynamical evolution leading to the formation of stars and planets, PSCs also provide a substrate for incipient chemical complexity in the interstellar space. Aims. Our aim is to understand the influence of external conditions on the chemical composition of PSCs. For this purpose, we compared molecular column densities in two typical PSCs, L183 and L1544, which are embedded in different environments. Methods. A single-pointing survey of L183 at λ = 3 mm was conducted using the IRAM 30-m single-dish antenna. This led to the detection of more than 100 emission lines from 46 molecular species. The molecular column densities and excitation temperatures derived from these lines were compared to the corresponding parameters in L1544. The data for L1544 were obtained from literature or publicly available surveys, and they were analysed using the same procedure as adopted for L183. An astrochemical model, previously developed for the interpretation of organic molecule emissions towards the methanol peak of L1544, was used to interpret the combined data. Results. Our analysis reveals clear chemical differences between the two PSCs. While L1544 is richer in carbon-bearing species, in particular carbon chains, oxygen-containing species are generally more abundant in L183. The results are well-reproduced by our chemical model. Conclusions. The observed chemical differentiation between the two PSCs is caused by the different environmental conditions: the core of L183 is deeply buried in the surrounding cloud, whereas L1544 lies close to the edge of the Taurus Molecular Cloud. The obscuration of L183 from the interstellar radiation field (ISRF) allows the carbon atoms to be locked in carbon monoxide, which ultimately leads to a large abundance of O-bearing species. In contrast, L1544, being more affected by the ISRF, can keep a fraction of carbon in atomic form, which is needed for the production of carbon chains.

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30

Kumar, Kotlo U., Sri P. Srivastava, and Randal J. Kaufman. "Double-Stranded RNA-Activated Protein Kinase (PKR) Is Negatively Regulated by 60S Ribosomal Subunit Protein L18." Molecular and Cellular Biology 19, no. 2 (February 1, 1999): 1116–25. http://dx.doi.org/10.1128/mcb.19.2.1116.

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ABSTRACT The double-stranded RNA (dsRNA)-activated protein kinase (PKR) provides a fundamental control step in the regulation of protein synthesis initiation through phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2α), a process that prevents polypeptide chain initiation. In such a manner, activated PKR inhibits cell growth and induces apoptosis, whereas disruption of normal PKR signaling results in unregulated cell growth. Therefore, tight control of PKR activity is essential for regulated cell growth. PKR is activated by dsRNA binding to two conserved dsRNA binding domains within its amino terminus. We isolated a ribosomal protein L18 by interaction with PKR. L18 is a 22-kDa protein that is overexpressed in colorectal cancer tissue. L18 competed with dsRNA for binding to PKR, reversed dsRNA binding to PKR, and did not directly bind dsRNA. Mutation of K64E within the first dsRNA binding domain of PKR destroyed both dsRNA binding and L18 interaction, suggesting that the two interactive sites overlap. L18 inhibited both PKR autophosphorylation and PKR-mediated phosphorylation of eIF-2α in vitro. Overexpression of L18 by transient DNA transfection reduced eIF-2α phosphorylation and stimulated translation of a reporter gene in vivo. These results demonstrate that L18 is a novel regulator of PKR activity, and we propose that L18 prevents PKR activation by dsRNA while PKR is associated with the ribosome. Overexpression of L18 may promote protein synthesis and cell growth in certain cancerous tissue through inhibition of PKR activity.

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31

Mergoni, Giovanni, Maddalena Manfredi, Pio Bertani, Tecla Ciociola, Stefania Conti, and Laura Giovati. "Activity of Two Antimicrobial Peptides against Enterococcus faecalis in a Model of Biofilm-Mediated Endodontic Infection." Antibiotics 10, no. 10 (October 7, 2021): 1220. http://dx.doi.org/10.3390/antibiotics10101220.

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Enterococcus faecalis is a common cause of biofilm-associated opportunistic infections, which are often difficult to treat. The formation of E. faecalis biofilms on the dentinal walls of the root canal is frequently the cause of endodontic treatment failure and secondary apical periodontitis. In a preliminary work, two recognized antifungal peptides, KP and L18R, showed antibacterial activity against planktonic E. faecalis cells at micromolar concentrations. Moreover, L18R proved to reduce the biomass in the early stage of E. faecalis biofilm development on polystyrene plates, while a qualitative biofilm inhibition was demonstrated on hydroxyapatite disks by confocal laser scanning microscopy (CLSM). The aim of this study was to better characterize the effect of both peptides on E. faecalis biofilm. A reduction in metabolic activity after peptide treatment was detected by Alamar Blue assay, while a remarkable impairment in the architecture of E. faecalis biofilms on hydroxyapatite disks, along with a significant reduction in viable bacteria, was caused mostly by L18R, as assessed by CLSM and scanning electron microscopy. The lack of cytotoxicity of the investigated peptides against L929 murine fibroblasts was also determined. Obtained results suggest L18R as a promising candidate for the development of new strategies for endodontic infection control.

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32

Noselli, Stéphane, and Alain Vincent. "The Drosophila melanogaster ribosomal protein L17A-encoding gene." Gene 118, no. 2 (September 1992): 273–78. http://dx.doi.org/10.1016/0378-1119(92)90199-y.

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33

Olvera, Joe, and Ira G. Wool. "The Primary Structure of Rat Ribosomal Protein L10a." Biochemical and Biophysical Research Communications 220, no. 3 (March 1996): 954–57. http://dx.doi.org/10.1006/bbrc.1996.0513.

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34

Hünig, T. R. "The ligand of the erythrocyte receptor of T lymphocytes: expression on white blood cells and possible involvement in T cell activation." Journal of Immunology 136, no. 6 (March 15, 1986): 2103–8. http://dx.doi.org/10.4049/jimmunol.136.6.2103.

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Abstract We have recently described a monoclonal antibody (mAb) to sheep erythrocytes, termed L180/1, that blocks the formation of E rosettes between human or sheep T lymphocytes and sheep red blood cells. The cell surface glycoprotein (GP) of 42,000 apparent m.w. recognized by mAb L180/1 was given the preliminary name T11 target structure or T11TS. In the present report, it is shown that T11TS is also expressed on sheep white blood cells, notably on activated T lymphocytes, that are shown to actively synthesize this cell surface GP. In addition, the mixed lymphocyte reaction between outbred sheep is inhibited by mAb L180/1 at an early stage of the response. Together with the known involvement of the E receptor in T lymphocyte activation, these results are taken to suggest that T11 and T11TS are complementary cell interaction molecules involved in regulating T cell proliferation.

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35

WOESTENENK, Esmeralda A., George M. GONGADZE, Dmitry V. SHCHERBAKOV, Alexey V. RAK, Maria B. GARBER, Torleif HÄRD, and Helena BERGLUND. "The solution structure of ribosomal protein L18 from Thermus thermophilus reveals a conserved RNA-binding fold." Biochemical Journal 363, no. 3 (April 24, 2002): 553–61. http://dx.doi.org/10.1042/bj3630553.

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We have determined the solution structure of ribosomal protein L18 from Thermus thermophilus. L18 is a 12.5kDa protein of the large subunit of the ribosome and binds to both 5S and 23S rRNA. In the uncomplexed state L18 folds to a mixed α/β globular structure with a long disordered N-terminal region. We compared our high-resolution structure with RNA-complexed L18 from Haloarcula marismortui and T. thermophilus to examine RNA-induced as well as species-dependent structural differences. We also identified T. thermophilus S11 as a structural homologue and found that the structures of the RNA-recognition sites are conserved. Important features, for instance a bulge in the RNA-contacting β-sheet, are conserved in both proteins. We suggest that the L18 fold recognizes a specific RNA motif and that the resulting RNA—protein-recognition module is tolerant to variations in sequence.

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36

He, Kai-Cyuan, Yi-Ru Chen, Chu-Ting Liang, Shi-Jie Huang, Chung-Ying Tzeng, Chi-Fon Chang, Shing-Jong Huang, Hsien-Bin Huang та Ta-Hsien Lin. "Conformational Characterization of Native and L17A/F19A-Substituted Dutch-Type β-Amyloid Peptides". International Journal of Molecular Sciences 21, № 7 (7 квітня 2020): 2571. http://dx.doi.org/10.3390/ijms21072571.

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Some mutations which occur in the α/β-discordant region (resides 15 to 23) of β-amyloid peptide (Aβ) lead to familial Alzheimer’s disease (FAD). In vitro studies have shown that these genetic mutations could accelerate Aβ aggregation. We recently showed that mutations in this region could alter the structural propensity, resulting in a different aggregative propensity of Aβ. Whether these genetic mutations display similar effects remains largely unknown. Here, we characterized the structural propensity and aggregation kinetics of Dutch-type Aβ40 (Aβ40(E22Q)) and its L17A/F19A-substituted mutant (Aβ40(L17A/F19A/E22Q)) using circular dichroism spectroscopy, nuclear magnetic spectroscopy, and thioflavin T fluorescence assay. In comparison with wild-type Aβ40, we found that Dutch-type mutation, unlike Artic-type mutation (E22G), does not reduce the α-helical propensity of the α/β-discordant region in sodium dodecyl sulfate micellar solution. Moreover, we found that Aβ40(L17A/F19A/E22Q) displays a higher α-helical propensity of the α/β-discordant region and a slower aggregation rate than Aβ40(E22Q), suggesting that the inhibition of aggregation might be via increasing the α-helical propensity of the α/β-discordant region, similar to that observed in wild-type and Artic-type Aβ40. Taken together, Dutch-type and Artic-type mutations adopt different mechanisms to promote Aβ aggregation, however, the L17A/F19A mutation could increase the α-helical propensities of both Dutch-type and Artic-type Aβ40 and inhibit their aggregation.

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37

Hünig, T. "The cell surface molecule recognized by the erythrocyte receptor of T lymphocytes. Identification and partial characterization using a monoclonal antibody." Journal of Experimental Medicine 162, no. 3 (September 1, 1985): 890–901. http://dx.doi.org/10.1084/jem.162.3.890.

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A monoclonal antibody (mAb) to sheep red blood cells (SRBC), termed L180/1, is described that completely blocks rosette formation between SRBC and human or sheep T lymphocytes. L180/1 precipitated a minor glycoprotein of about approximately 42,000 mol wt from surface-labeled SRBC. This glycoprotein was partially affinity purified and found to block E rosette formation and to compete with anti-T11 mAb for the E receptor. The molecule detected by mAb L180/1 thus appears to be recognized by the E receptor and was given the preliminary name, T11 target structure (T11TS). Since the mAb to sheep T11TS blocks the binding of SRBC to both human and sheep T cells, and mAb to T11 blocks the binding of red cells from human and sheep to the human E receptor, we concluded that analogous receptor-ligand (T11-T11TS) systems exist in man and sheep that are crossreactive over the species barrier. The possibility is discussed that the E receptor, which is known to be involved in T cell activation, and T11TS function as complementary cell interaction molecules in T cell responses.

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38

BALOGUN, OLUSEGUN S., LEIXIN XU, TOHRU TERAOKA, and DAIJIRO HOSOKAWA. "Effects of single and double infections with Potato virus X and Tobacco mosaic virus on disease development, plant growth, and virus accumulation in tomato." Fitopatologia Brasileira 27, no. 3 (June 2002): 241–48. http://dx.doi.org/10.1590/s0100-41582002000300001.

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The tomato cv. Fukuju nº. 2 was used for studying the effect of single and double infections with Potato virus X (PVX) and Tobacco mosaic virus (TMV). Mixed infection resulted in a synergistic increase of disease severity, where more growth reduction was seen with simultaneous inoculations than with sequential inoculations at four-day intervals. At five and 12 days post-inoculation, the increased severity of the disease coincided with enhancement of virus accumulation in the rapidly expanding upper leaves. The PVX concentration in leaves nº 5 to 7 of doubly infected plants was three to six fold that of singly infected ones, as determined by DAS-ELISA. Mixed infection with the L strain led to higher enhancement of PVX than with the TMV-L11A strain. The concentration of TMV-L was lower in double infection and significantly higher than TMV-L11A in both singly and doubly infected plants. Analyses of the PVX ORF2 by Western blot and Northern hybridization revealed the pattern of accumulation of the 25 kDa protein and the RNAs, respectively, following those of the virion and coat protein. The strain TMV-L11A overcame the resistance gene in cv. GCR 237 (Tm-1). In the upper leaf nº. 8, the concentration of PVX was three times higher in plants with mixed infection than with L11A. The concentrations of the L and OM (TMV strains) in both singly and doubly infected plants were at very low levels, and the synergistic effect on PVX concentration and disease severity was not observed.

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39

Karoly, Janik, Archana Soam, B.-G. Andersson, Simon Coudé, Pierre Bastien, John E. Vaillancourt, and Chang Won Lee. "Revisiting the Magnetic Field of the L183 Starless Core." Astrophysical Journal 900, no. 2 (September 15, 2020): 181. http://dx.doi.org/10.3847/1538-4357/abad37.

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40

Kilic, Ahmet, Eyyup Yasar, and Emine Aytar. "Neutral boron [(L1-3)BPh2] and cationic charged boron [(L1a-3a)BPh2] complexes for chemical CO2 conversion to obtain cyclic carbonates under ambient conditions." Sustainable Energy & Fuels 3, no. 4 (2019): 1066–77. http://dx.doi.org/10.1039/c8se00633d.

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Three neutral salen ligands (L1-3) with three cationic charged salen ligands (L1a-3a) and the corresponding neutral boron [(L1-3)BPh2] and cationic charged boron [(L1a-3a)BPh2] compounds have been successfully synthesized and characterized under ambient conditions.

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41

Zappe, Lisa, Charles Lochenie, Thomas Martin, and Birgit Weber. "Iron(II) Spin Crossover Polymers of Planar N2O2 Schiff Base Templates and 4,4’-bis(pyridyl)urea Bridges." Open Chemistry Journal 6, no. 1 (March 22, 2019): 10–18. http://dx.doi.org/10.2174/1874842201906010010.

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Introduction:The synthesis of four new iron(II) coordination polymers [Fe(L1a)(bpua)] (1), [Fe(L1b)(bpua)](0.5bpua) (2), [Fe(L2a)(bpua)] (3), [Fe(L1b)(bpua)](yEtOH) (5) and one trinuclear complex [{Fe(L1a)(bpua)(MeOH)}2-µ{Fe(L1a)}](xMeOH) (4) with Schiff base-like N2O2coordinating equatorial ligands (L1a, L1b and L2a) and 4,4’-bis(pyridyl)urea (bpua) as bridging axial ligand is described.Materials and Methods:Single crystal X-ray structure elucidation of the trinuclear module4and of the coordination polymer5reveals the presence of HS-LS-HS chains and all-HS infinite 1-D strands, respectively. As anticipated the presence of the bridging urea supports the supramolecular concatenation within an extended hydrogen-bonding network. Magnetic measurements reveal spin crossover behavior for four of the five complexes (1–4) that is strongly solvent dependent.Results and Conclusion:Interestingly, in two cases, complete removal of the solvent from the crystal packing leads to wider thermal hysteresis loops.

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42

BALANTEKIN, A. B., and H. YÜKSEL. "NEUTRINO PHYSICS AND NUCLEAR AXIAL TWO-BODY INTERACTIONS." International Journal of Modern Physics E 14, no. 01 (February 2005): 39–46. http://dx.doi.org/10.1142/s0218301305002758.

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We consider the counter-term describing isoscalar axial two-body currents in the nucleon–nucleon interaction, L1A, in the effective field theory approach. We determine this quantity using solar neutrino data. We investigate the variation of L1A when different sets of data are used.

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43

Vasapollo, B., G. P. Novelli, G. Gagliardi, M. G. Tiralongo, I. Pisani, D. Manfellotto, L. Giannini, and H. Valensise. "L18. Total Vascular Resistance in complicated pregnancies." Pregnancy Hypertension: An International Journal of Women's Cardiovascular Health 1, no. 3-4 (July 2011): 249. http://dx.doi.org/10.1016/j.preghy.2011.08.019.

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44

Holl-Ulrich, Konstanze. "L18. Granuloma formation in granulomatosis with polyangiitis." La Presse Médicale 42, no. 4 (April 2013): 555–58. http://dx.doi.org/10.1016/j.lpm.2013.01.017.

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45

H. Naruse, T. Udagawa, K. Ono, T. Ohtani, F. Yamaguchi, T. Une, R. Kanazawa, and S. Sasaki. "Pharmacokinetics of MDP-Lys (L18) in human." International Journal of Immunopharmacology 10 (January 1988): 140. http://dx.doi.org/10.1016/0192-0561(88)90510-3.

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46

Xia, Xuechun, Fajian Hou, Jie Li, and Huiling Nie. "Ribosomal protein L10a, a bridge between trichosanthin and the ribosome." Biochemical and Biophysical Research Communications 336, no. 1 (October 2005): 281–86. http://dx.doi.org/10.1016/j.bbrc.2005.08.074.

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47

Yuan, Fang-Ting, Tsutomu T. Takeuchi, Véronique Buat, Sébastien Heinis, Elodie Giovannoli, Katsuhiro L. Murata, Jorge Iglesias-Páramo, and Denis Burgarella. "AKARI/IRC broadband mid-infrared data as an indicator of the Star Formation Rate." Proceedings of the International Astronomical Union 7, S284 (September 2011): 357–59. http://dx.doi.org/10.1017/s1743921312009416.

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AbstractWith the goal of constructing Star-Formation Rates (SFR) from AKARI Infrared Camera (IRC) data, we analyzed an IR-selected GALEX-SDSS-2MASS-AKARI(IRC & Far-Infrared Surveyor) sample of 153 nearby galaxies. The far-infrared fluxes were obtained from AKARI diffuse maps to correct the underestimation for extended sources raised by PSF photometry. SFRs of these galaxies were derived using the SED fitting program CIGALE. In spite of complicated features contained in these bands, both the S9W and L18W emissions correlate with the SFR of galaxies. The SFR calibrations using S9W and L18W are presented for the first time. These calibrations agree well with previous work based on Spitzer data within the scatter, and should be applicable to dust-rich galaxies.

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48

Le, Trong V. "Effects of pre-sowing seed treatment with KCl on yield and quality of two peanut cultivars L12 and L18." Journal of Agriculture and Development 20, no. 1 (February 26, 2021): 1–9. http://dx.doi.org/10.52997/jad.1.01.2021.

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The study was conducted to evaluate the effect of 0.05% KCl on yield and quality of two peanut varieties L12 and L18 grown in Thanh Hoa province. The experiment was arranged in a completely randomized design with two factors (varieties and chemicals). After careful selection, L12 and L18 seeds were divided into two parts. Part 1 was treated with distilled water as control and part 2 was treated with 0.05% KCl. The results showed that pre-sowing seed treatment with 0.05% KCl increased the yield components and yield of both L12 and L18 when compared to the control, in which the yield of L18 in both treatments reached 37.37 quintals/ha and 39.54 quintals/ha and was higher than that of the L12 variety at 35.77 quintals/ha and 36.40 quintals/ha. Pre-sowing seed treatment with 0.05% KCl also increased the quality of peanuts such as starch content, reducing sugar, lipid, saponification value, protein, B vitamins, total amino acids and content of some mineral elements in peanuts such as N, K, Ca, Mg. Briefly, the results of this study indicated that pre-sowing seed with KCl increased the yield and quality of peanuts.

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49

Singh, Sanjesh, I. Darren Grice, Ian R. Peak, Thomas Frost, Geng Yue, and Jennifer C. Wilson. "The role of lipooligosaccharide in the biological activity of Moraxella bovis strains Epp63, Mb25 and L183/2, and isolation of capsular polysaccharide from L183/2." Carbohydrate Research 467 (September 2018): 1–7. http://dx.doi.org/10.1016/j.carres.2018.07.002.

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50

Dueck, Kevin J., YuanShen (Sandy) Hu, Peter Chen, Yvon Deschambault, Jocelyn Lee, Jessie Varga, and Jingxin Cao. "Mutational Analysis of Vaccinia Virus E3 Protein: the Biological Functions Do Not Correlate with Its Biochemical Capacity To Bind Double-Stranded RNA." Journal of Virology 89, no. 10 (March 4, 2015): 5382–94. http://dx.doi.org/10.1128/jvi.03288-14.

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ABSTRACTVaccinia E3 protein has the biochemical capacity of binding to double-stranded RNA (dsRNA). The best characterized biological functions of the E3 protein include its host range function, suppression of cytokine expression, and inhibition of interferon (IFN)-induced antiviral activity. Currently, the role of the dsRNA binding capacity in the biological functions of the E3 protein is not clear. To further understand the mechanism of the E3 protein biological functions, we performed alanine scanning of the entire dsRNA binding domain of the E3 protein to examine the link between its biochemical capacity of dsRNA binding and biological functions. Of the 115 mutants examined, 20 were defective in dsRNA binding. Although the majority of the mutants defective in dsRNA binding also showed defective replication in HeLa cells, nine mutants (I105A, Y125A, E138A, F148A, F159A, K171A, L182A, L183A, and I187/188A) retained the host range function to various degrees. Further examination of a set of representative E3L mutants showed that residues essential for dsRNA binding are not essential for the biological functions of E3 protein, such as inhibition of protein kinase R (PKR) activation, suppression of cytokine expression, and apoptosis. Thus, data described in this communication strongly indicate the E3 protein performs its biological functions via a novel mechanism which does not correlate with its dsRNA binding activity.IMPORTANCEdsRNAs produced during virus replication are important pathogen-associated molecular patterns (PAMPs) for inducing antiviral immune responses. One of the strategies used by many viruses to counteract such antiviral immune responses is achieved by producing dsRNA binding proteins, such as poxvirus E3 family proteins, influenza virus NS1, and Ebola virus V35 proteins. The most widely accepted model for the biological functions of this class of viral dsRNA binding proteins is that they bind to and sequester viral dsRNA PAMPs; thus, they suppress the related antiviral immune responses. However, no direct experimental data confirm such a model. In this study of vaccinia E3 protein, we found that the biological functions of the E3 protein are not necessarily linked to its biochemical capacity of dsRNA binding. Thus, our data strongly point to a new concept of virus modulation of cellular antiviral responses triggered by dsRNA PAMPs.

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