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Journal articles on the topic 'Cecropin B'

Author: Grafiati

Published: 28 June 2021

Last updated: 1 February 2022

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1

Wang, Jiarong, Kun Ma, Maosen Ruan, Yujuan Wang, Yan Li, Yu V. Fu, Yonghong Song, Hongbin Sun, and Junfeng Wang. "A novel cecropin B-derived peptide with antibacterial and potential anti-inflammatory properties." PeerJ 6 (July 25, 2018): e5369. http://dx.doi.org/10.7717/peerj.5369.

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Cecropins, originally found in insects, are a group of cationic antimicrobial peptides. Most cecropins have an amphipathic N-terminal segment and a largely hydrophobic C-terminal segment, and normally form a helix-hinge-helix structure. In this study, we developed the novel 32-residue cecropin-like peptide cecropin DH by deleting the hinge region (Alanine-Glycine-Proline) of cecropin B isolated from Chinese oak silk moth, Antheraea pernyi. Cecropin DH possesses effective antibacterial activity, particularly against Gram-negative bacteria, with very low cytotoxicity against mammalian cells. Interactions between cecropin DH and the highly anionic lipopolysaccharide (LPS) component of the Gram-negative bacterial outer membrane indicate that it is capable of dissociating LPS micelles and disrupting LPS aggregates into smaller assemblies, which may play a vital role in its antimicrobial activity. Using LPS-stimulated mouse macrophage RAW264.7 cells, we found that cecropin DH exerted higher potential anti-inflammatory activity than cecropin B, as demonstrated by the inhibition of pro-inflammatory cytokines nitric oxide production and secretion of tumor necrosis factor-α. In conclusion, cecropin DH has potential as a therapeutic agent for both antibacterial and anti-inflammatory applications.

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2

Mills, David, and Freddi A. Hammerschlag. "THE EFFECT OF CECROPIN B ON CELLS AND PROTOPLASTS OF PEACH." HortScience 27, no. 6 (June 1992): 694d—694. http://dx.doi.org/10.21273/hortsci.27.6.694d.

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Pathogenic bacteria, such as Xanthomonas campestris pv. pruni, cause diseases of significant economical implications in the Prunus genus. Cecropins are naturally occurring bactericidal peptides found in the hemolymph of insects. Cecropins cause channel formation in membranes and lysis of bacterial cells. We are interested in engineering the gene for cecropin into peach (Prunus persica) and other fruit tree species. The objective of this study was to determine the effect of cecropin B on viability, using fluorescein diacetate staining, and on changes in transmembrane electrical potential (PD) using the fluorescing probe merocyanine-540. Protoplasts were isolated from shoot-tip cultures in a CPW13M (salts + 0.71M mannitol) solution containing 2% cellulase and 0.5% macerase, while cells were isolated in CPW15.4S (salts + 0.45M sucrose) containing 0.5% cellulase and 0.5% macerase. Cecropin B (1μM) had no effect on viability and changes in PD, while 10μM had a slight effect, and 100μM cecropin B caused significant depolarization and lysis of peach protoplasts. No effect on viability and change in PD were observed in cells when treated with 1-100μM cecropin B. These results suggest that cells and protoplasts of peach can resist cecropin B in the concentration range that causes lysis of plant pathogenic bacteria. The implication of using cecropin to increase microbial disease resistance will be discussed.

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3

Sallum, Ulysses W., and Thomas T. Chen. "Inducible Resistance of Fish Bacterial Pathogens to the Antimicrobial Peptide Cecropin B." Antimicrobial Agents and Chemotherapy 52, no. 9 (May 12, 2008): 3006–12. http://dx.doi.org/10.1128/aac.00023-08.

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ABSTRACT Cecropin B is a cationic antimicrobial peptide originally isolated from the diapausing pupae of the giant silk moth, Hylphora cecropia. Cecropin B elicits its antimicrobial effects through disruption of the anionic cell membranes of gram-negative bacteria. Previous work by our laboratory demonstrated that a constitutively expressed cecropin B transgene conferred enhanced resistance to bacterial infection in medaka. The development of antibiotic resistance by pathogenic bacteria is a growing problem. The potential for fish bacterial pathogens to develop resistance to cecropin B was addressed in this study. Four fish bacterial pathogens were selected for the study based on their importance in aquaculture. Vibrio anguillarum, Vibrio vulnificus, and Yersinia ruckeri all exhibited inducible resistance to cecropin B. The inducible resistance of these three pathogens was correlated with reversible changes in their ultrastructures, as observed by scanning electron microscopy. V. anguillarum was demonstrated to become more adhesive to a CHSE-214 cell monolayer and to cause increased cumulative mortality in medaka following exposure to cecropin B. This work demonstrates that the resistance of fish bacterial pathogens to cecropin B is inducible and suggests that resistance to other cationic antimicrobial peptides may occur through similar means. The observed changes in ultrastructure and infectivity suggest that resistance to antimicrobial peptides is an integral part of the pathogenesis of fish gram-negative bacterial pathogens.

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4

Ghandehari, Fereshte, and Mahnoosh Fatemi. "Study of anticancer activity of cecropin B on 7, 12-dimethylbenz (a) anthracene-induced breast cancer." Journal of Shahrekord University of Medical Sciences 22, no. 3 (June 29, 2020): 106–12. http://dx.doi.org/10.34172/jsums.2020.17.

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Background and aims: Antimicrobial peptides constitute a family of bioactive peptides that are involved in the body defense. Recently, their anti-cancer properties, especially by inducing apoptosis, have been proven in in vitro studies. Therefore, in this study, the effects of cecropin B as an antimicrobial peptide on breast cancer growth, hematological parameters, and histopathological changes in rats were evaluated. Methods: Twenty-four female rats were randomly divided into 4 groups. The cancer group, control group, cecropin B group, and cancer group treated with cecropin B. The tumor size was measured at the beginning and the completion of the treatment period. Blood samples were collected for assessment of the hematological parameters and Bax and Bcl2 levels. Tumor tissues were removed for histopathological analysis. Results: The tumor size had a significant increase in the cancer group and cancer group treated with cecropin at the end of the treatment. A significant decrease in mean cell volume, white blood cell count and Bcl2 level and a significant increase in hemoglobin and Bax levels were observed in the cancer group treated with cecropin B compared to cancer group. Changes in other parameters were not significant. Histopathological study showed the invasion of mitotic cells to stromal and muscular tissues of the breast in the cancer group, while focal destruction of tissue and cell death were observed in the cancer group treated with cecropin B. Conclusion: The results showed that cecropin B has been able to reduce tumor growth and have little side effects on hematologic factors probably through apoptosis.

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5

van Hofsten, P., I. Faye, K. Kockum, J. Y. Lee, K. G. Xanthopoulos, I. A. Boman, H. G. Boman, A. Engstrom, D. Andreu, and R. B. Merrifield. "Molecular cloning, cDNA sequencing, and chemical synthesis of cecropin B from Hyalophora cecropia." Proceedings of the National Academy of Sciences 82, no. 8 (April 1, 1985): 2240–43. http://dx.doi.org/10.1073/pnas.82.8.2240.

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6

Fernandez, R. C., and A. A. Weiss. "Susceptibilities of Bordetella pertussis strains to antimicrobial peptides." Antimicrobial Agents and Chemotherapy 40, no. 4 (April 1996): 1041–43. http://dx.doi.org/10.1128/aac.40.4.1041.

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We examined the susceptibilities of Bordetella pertussis strains to several antimicrobial peptides by determining the concentration required to inhibit or kill 50% of the bacterial population. The peptides are ranked in decreasing potency as follows: cecropin B > cecropin A > melittin > cecropin P1 > (ala8,13,18)-magainin II amide > mastoparan = defensin HNP1 > protamine > or = magainin II = magainin I. By using a radial diffusion assay to compare susceptibilities between strains, wild-type B. pertussis BP338 was more resistant than the avirulent bvg mutant strain BP347 and the brk mutant strain BPM2041 to killing by cecropin P1. In contrast, compared with the wild type, the avirulent BP347 strain was highly resistant to killing by protamine and defensin HNP1.

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7

XANTHOPOULOS, Kleanthis G., Jong-Youn LEE, Renbao GAN, Kerstin KOCKUM, Ingrid FAYE, and Hans G. BOMAN. "The structure of the gene for cecropin B, an antibacterial immune protein from Hyalophora cecropia." European Journal of Biochemistry 172, no. 2 (March 1988): 371–76. http://dx.doi.org/10.1111/j.1432-1033.1988.tb13896.x.

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8

Hongbiao, W., N. Baolong, H. Lihua, S. Weifeng, and M. Zhiqi. "Biological activities of cecropin B-thanatin hybrid peptides." Journal of Peptide Research 66, no. 6 (December 4, 2008): 382–86. http://dx.doi.org/10.1111/j.1399-3011.2005.00299.x.

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9

Chen, Hueih Min, Wei Wang, David Smith, and Siu Chiu Chan. "Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells." Biochimica et Biophysica Acta (BBA) - General Subjects 1336, no. 2 (August 1997): 171–79. http://dx.doi.org/10.1016/s0304-4165(97)00024-x.

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10

Wang, Chunmei, Fangzhou Chen, Han Hu, Wentao Li, Yang Wang, Pin Chen, Yingyu Liu, et al. "Gene Expression Profiling of Cecropin B-Resistant Haemophilus parasuis." Journal of Molecular Microbiology and Biotechnology 24, no. 2 (2014): 120–29. http://dx.doi.org/10.1159/000362277.

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11

Zhang, Jiao, Xiuxia Su, Dong Yang, and Chonglin Luan. "Label-free liquid crystal biosensor for cecropin B detection." Talanta 186 (August 2018): 60–64. http://dx.doi.org/10.1016/j.talanta.2018.04.004.

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12

Florack, Dion, Sjefke Allefs, Rik Bollen, Dirk Bosch, Bert Visser, and Willem Stiekema. "Expression of giant silkmoth cecropin B genes in tobacco." Transgenic Research 4, no. 2 (March 1995): 132–41. http://dx.doi.org/10.1007/bf01969415.

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13

Owens, Lowell D., and Thomas M. Heutte. "A Single Amino Acid Substitution in the Antimicrobial Defense Protein Cecropin B Is Associated with Diminished Degradation by Leaf Intercellular Fluid." Molecular Plant-Microbe Interactions® 10, no. 4 (May 1997): 525–28. http://dx.doi.org/10.1094/mpmi.1997.10.4.525.

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Degradation is one of several factors that may affect the level of accumulation of transgene products in plants. In plants engineered to secrete antimicrobial proteins to the intercellular compartment of leaves, the degradative activity of proteases residing in leaf intercellular fluid (IF) could be critical to achieving the expected transgene function. We synthesized a structural analogue (MB39) of the antibacterial protein cecropin B and compared the susceptibility of both proteins to degradation in vitro by IF extracted from leaves of various crops. The half-life of the two proteins in the various IF extracts ranged from 3 min to 25.5 h, with the analogue MB39 displaying the longer half-life in IF from nine of 10 species. Overall, the half-life of MB39 averaged 2.9 times greater than that of cecropin B. Analysis of the peptides produced by endopeptidase activity in potato IF indicated that the 5.7-fold lower degradation rate of MB39 was associated with the substitution of valine for methionine at residue 11 of cecropin B. These findings point to the possibility of tailoring antimicrobial protein genes to reduce the rate of protein degradation in a particular target crop.

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14

Chen, Fanjie, Han Hu, Zhonghua Li, Jiacheng Huang, Xuwang Cai, Chunmei Wang, Qigai He, and Jiyue Cao. "Deletion of HAPS_2096 Increases Sensitivity to Cecropin B in Haemophilus parasuis." Journal of Molecular Microbiology and Biotechnology 25, no. 4 (2015): 284–91. http://dx.doi.org/10.1159/000434752.

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Cecropin B (CB) is a very effective natural antimicrobial peptide that has shown great potential for future antimicrobial drug development. HAPS_2096 is a <i>Haemophilus parasuis</i> gene that encodes the periplasmic substrate-binding protein of an ATP-binding cassette-type amino acid transporter. In this research, we constructed and verified an HAPS_2096 deletion mutant and a complementary HAPS_2096 mutant of <i>H. parasuis</i> JS0135. A bactericidal assay revealed that the HAPS_2096 deletion mutant was significantly more sensitive than the wild-type strain to 0.25-0.5 µg/ml CB. However, the gene complementation alleviated the CB sensitivity of the mutant. Immunoelectron microscopy observation following a 30-min treatment with a sublethal concentration of CB (0.25 μg/ml) revealed more extensive morphological damage in the mutant strain than in the wild-type strain. Hence, our results suggest that the HAPS_2096 gene contributes to <i>H. parasuis</i> resistance to CB.

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15

Vaara, M., and T. Vaara. "Ability of cecropin B to penetrate the enterobacterial outer membrane." Antimicrobial Agents and Chemotherapy 38, no. 10 (October 1, 1994): 2498–501. http://dx.doi.org/10.1128/aac.38.10.2498.

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16

Sallum, Ulysses W., and Thomas T. Chen. "Molecular Cloning of Cecropin B Responsive Endonucleases in Yersinia ruckeri." Marine Biotechnology 13, no. 1 (March 30, 2010): 56–65. http://dx.doi.org/10.1007/s10126-010-9269-z.

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17

Mills, David, and Freddi A. Hammerschlag. "Effect of cecropin B on peach pathogens, protoplasts, and cells." Plant Science 93, no. 1-2 (January 1993): 143–50. http://dx.doi.org/10.1016/0168-9452(93)90043-y.

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18

Anghel, Radu, Daniela Jitaru, Laurentiu Badescu, Manuela Ciocoiu, and Magda Badescu. "The Cytotoxic Effect of Cecropin A and Cecropin B on the MDA-MB-231 and M14K Tumour Cell Lines." Journal of Biomedical Science and Engineering 07, no. 08 (2014): 504–15. http://dx.doi.org/10.4236/jbise.2014.78052.

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19

Hammerschlag, F. A. "In Vitro Inhibitory Activity of Antimicrobial Peptides Cecropin, α-Thionin DB4, and γ-Thionin RsAFP1 Against Several Pathogens of Strawberry and Highbush Blueberry." HortScience 39, no. 5 (August 2004): 1053–55. http://dx.doi.org/10.21273/hortsci.39.5.1053.

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As part of a program to develop transgenic highbush blueberry (Vaccinium corymbosum L.) and strawberry (Fragaria ×ananassa Duchesne) cultivars with increased levels of disease resistance, we have investigated the feasibility of introducing genes for the antimicrobial peptides cecropin B and MB39, α-thionin DB4 (DB4) and γ-thionin RsAFP1 (RsAFP1) by testing the effects of these peptides on several important pathogens of these two crop species. A thin-layer plate bioassay was conducted with these peptides and the pathogens Botrytis cinerea (Pers.ex. Fr.), Botryosphaeria dothidea (Mouq.ex. Fr.) Ces & de Not., Colletotrichum acutatum Simmonds, C. gloeosporioides (Penz.) Penz.et Sacc., C. fragariae Brooks, Monilinia vaccinii-corymbosi Reade (Honey), Phytophthora fragariae Hickman and Xanthomonas fragariae Kennedy and King. The minimum lethal concentration (μm) for cecropin ranged from 0.02 for X. fragariae strains 10 and 128 to 72.8 for C. gloeosporioides isolate Akp1. For DB4, the minimum inhibitory concentration (μm) ranged from 0.03 for X. fragariae strain 6 to 87.2 for B. cinerea isolate cc. For RsAFP1, the minimum inhibitory concentration (μm) ranged from 0.13 for X. fragariae strain 6 to 61.4 for M. vaccinii-corymbosi isolate 9423-x-45. These results indicate that introducing genes for either cecropin, DB4 or RsAFP1 into strawberry may be useful for controlling bacterial angular leaf spot disease caused by X. fragariae.

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20

Jan, Pey-Shynan, Hsu-Yuang Huang, and Hueih-Min Chen. "Expression of a Synthesized Gene Encoding Cationic Peptide Cecropin B in Transgenic Tomato Plants Protects against Bacterial Diseases." Applied and Environmental Microbiology 76, no. 3 (December 4, 2009): 769–75. http://dx.doi.org/10.1128/aem.00698-09.

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ABSTRACT The cationic lytic peptide cecropin B (CB), isolated from the giant silk moth (Hyalophora cecropia), has been shown to effectively eliminate Gram-negative and some Gram-positive bacteria. In this study, the effects of chemically synthesized CB on plant pathogens were investigated. The S50s (the peptide concentrations causing 50% survival of a pathogenic bacterium) of CB against two major pathogens of the tomato, Ralstonia solanacearum and Xanthomonas campestris pv. vesicatoria, were 529.6 μg/ml and 0.29 μg/ml, respectively. The CB gene was then fused to the secretory signal peptide (sp) sequence from the barley α-amylase gene, and the new construct, pBI121-spCB, was used for the transformation of tomato plants. Integration of the CB gene into the tomato genome was confirmed by PCR, and its expression was confirmed by Western blot analyses. In vivo studies of the transgenic tomato plant demonstrated significant resistance to bacterial wilt and bacterial spot. The levels of CB expressed in transgenic tomato plants (∼0.05 μg in 50 mg of leaves) were far lower than the S50 determined in vitro. CB transgenic tomatoes could therefore be a new mode of bioprotection against these two plant diseases with significant agricultural applications.

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21

Chakraborty, Sandeep, My Phu, Basuthkar J. Rao, Bjarni Asgeirsson, and Abhaya M. Dandekar. "The PDB database is a rich source of alpha-helical anti-microbial peptides to combat disease causing pathogens." F1000Research 3 (December 5, 2014): 295. http://dx.doi.org/10.12688/f1000research.5802.1.

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The therapeutic potential ofα-helical anti-microbial peptides (AH-AMP) to combat pathogens is fast gaining prominence. Based on recently published open access software for characterizingα-helical peptides (PAGAL), we elucidate a search methodology (SCALPEL) that leverages the massive structural data pre-existing in the PDB database to obtain AH-AMPs belonging to the host proteome. We providein vitrovalidation of SCALPEL on plant pathogens (Xylella fastidiosa,Xanthomonas arboricolaandLiberibacter crescens) by identifying AH-AMPs that mirror the function and properties of cecropin B, a well-studied AH-AMP. The identified peptides include a linear AH-AMP present within the existing structure of phosphoenolpyruvate carboxylase (PPC20), and an AH-AMP mimicing the properties of the twoα-helices of cecropin B from chitinase (CHITI25). The minimum inhibitory concentration of these peptides are comparable to that of cecropin B, while anionic peptides used as control failed to show any inhibitory effect on these pathogens. Substitute therapies in place of conventional chemotherapies using membrane permeabilizing peptides like these might also prove effective to target cancer cells. The use of native structures from the same organism largely ensures that administration of such peptides will be better tolerated and not elicit an adverse immune response. We suggest a similar approach to target Ebola epitopes, enumerated using PAGAL recently, by selecting suitable peptides from the human proteome, especially in wake of recent reports of cationic amphiphiles inhibiting virus entry and infection.

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22

Chakraborty, Sandeep, My Phu, Tâmara Prado de Morais, Rafael Nascimento, Luiz Ricardo Goulart, Basuthkar J. Rao, Bjarni Asgeirsson, and Abhaya M. Dandekar. "The PDB database is a rich source of alpha-helical anti-microbial peptides to combat disease causing pathogens." F1000Research 3 (June 16, 2015): 295. http://dx.doi.org/10.12688/f1000research.5802.2.

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The therapeutic potential ofα-helical anti-microbial peptides (AH-AMP) to combat pathogens is fast gaining prominence. Based on recently published open access software for characterizingα-helical peptides (PAGAL), we elucidate a search methodology (SCALPEL) that leverages the massive structural data pre-existing in the PDB database to obtain AH-AMPs belonging to the host proteome. We providein vitrovalidation of SCALPEL on plant pathogens (Xylella fastidiosa,Xanthomonas arboricolaandLiberibacter crescens) by identifying AH-AMPs that mirror the function and properties of cecropin B, a well-studied AH-AMP. The identified peptides include a linear AH-AMP present within the existing structure of phosphoenolpyruvate carboxylase (PPC20), and an AH-AMP mimicing the properties of the twoα-helices of cecropin B from chitinase (CHITI25). The minimum inhibitory concentration of these peptides are comparable to that of cecropin B, while anionic peptides used as control failed to show any inhibitory effect on these pathogens. Substitute therapies in place of conventional chemotherapies using membrane permeabilizing peptides like these might also prove effective to target cancer cells. The use of native structures from the same organism could possibly ensure that administration of such peptides will be better tolerated and not elicit an adverse immune response. We suggest a similar approach to target Ebola epitopes, enumerated using PAGAL recently, by selecting suitable peptides from the human proteome, especially in wake of recent reports of cationic amphiphiles inhibiting virus entry and infection.

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23

Moreno, Ana Beatriz, Álvaro Martínez del Pozo, Marisé Borja, and Blanca San Segundo. "Activity of the Antifungal Protein from Aspergillus giganteus Against Botrytis cinerea." Phytopathology® 93, no. 11 (November 2003): 1344–53. http://dx.doi.org/10.1094/phyto.2003.93.11.1344.

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Botrytis blight (gray mold), caused by Botrytis cinerea, is one of the most widely distributed diseases of ornamental plants. In geranium plants, gray mold is responsible for important losses in production. The mold Aspergillus giganteus is known to produce and secrete a basic low-molecular-weight protein, the antifungal protein (AFP). Here, the antifungal properties of the Aspergillus AFP against various B. cinerea isolates obtained from naturally infected geranium plants were investigated. AFP strongly inhibited mycelial growth as well as conidial germination of B. cinerea. Microscopic observations of fungal cultures treated with AFP revealed reduced hyphal elongation and swollen hyphal tips. Washout experiments in which B. cinerea was incubated with AFP for different periods of time and then washed away revealed a fungicidal activity of AFP. Application of AFP on geranium plants protected leaves against Botrytis infection. Cecropin A also was active against this pathogen. An additive effect against the fungus was observed when AFP was combined with cecropin A. These results are discussed in relation to the potential of the afp gene to enhance crop protection against B. cinerea diseases.

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Sarmasik, A. "Bactericidal activity of cecropin B and cecropin P1 expressed in fish cells (CHSE-214): application in controlling fish bacterial pathogens." Aquaculture 220, no. 1-4 (April 14, 2003): 183–94. http://dx.doi.org/10.1016/s0044-8486(02)00634-8.

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Borth, Wayne B., V. P. Jones, D. E. Ullman, and J. S. Hu. "Effects of Synthetic Cecropin Analogs on in Vitro Growth of Acholeplasma laidlawii." Antimicrobial Agents and Chemotherapy 45, no. 6 (June 1, 2001): 1894–95. http://dx.doi.org/10.1128/aac.45.6.1894-1895.2001.

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ABSTRACT Four synthetic peptides (Peptidyl MIMs; Demeter Biotechnologies, Inc.) were evaluated for their in vitro activity againstAcholeplasma laidlawii. Fifty percent effective concentration values ranged from 1 to 15 μM. Three of these compounds are more lethal than cecropin B against A. laidlawii.

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Liu, Zhongyuan, Qiangjun Zhou, Xinfang Mao, Xiangdong Zheng, Jiubiao Guo, Fuchun Zhang, Tingyi Wen, and Hai Pang. "Crystallization and preliminary X-ray analysis of cecropin B fromBombyx mori." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 7 (June 24, 2010): 851–53. http://dx.doi.org/10.1107/s1744309110020130.

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27

Banemann, Andreas, Heike Deppisch, and Roy Gross. "The Lipopolysaccharide of Bordetella bronchiseptica Acts as a Protective Shield against Antimicrobial Peptides." Infection and Immunity 66, no. 12 (December 1, 1998): 5607–12. http://dx.doi.org/10.1128/iai.66.12.5607-5612.1998.

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ABSTRACT Resistance profiles of the two Bordetella speciesB. bronchiseptica and B. pertussis against various antimicrobial peptides were determined in liquid survival and agar diffusion assays. B. bronchiseptica exhibited significantly higher resistance against all tested peptides thanB. pertussis. The most powerful agents acting on B. bronchiseptica were, in the order of their killing efficiencies, cecropin P > cecropin B > magainin-II-amide > protamine > melittin. Interestingly, for B. bronchiseptica, the resistance level was significantly affected by phase variation, as a bvgS deletion derivative showed an increased sensitivity to these peptides. Tn5-induced protamine-sensitive B. bronchiseptica mutants, which were found to be very susceptible to most of the cationic peptides, were isolated. In two of these mutants, the genetic loci inactivated by transposon insertion were identified as containing genes highly homologous to the wlbA and wlbL genes ofB. pertussis that are involved in the biosynthesis of lipopolysaccharide (LPS). In agreement with this finding, the two peptide-sensitive mutants revealed structural changes in the LPS, resulting in the loss of the O-specific side chains and the prevalence of the LPS core structure. This demonstrates that LPS plays a major role in the resistance of B. bronchiseptica against the action of antimicrobial peptides and suggests that B. pertussis is much more susceptible to these peptides due to the lack of the highly charged O-specific sugar side chains.

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WANG, XIUQING, MINGXING ZHU, GUIMAO YANG, CHUNXIA SU, AIJUN ZHANG, RUIBING CAO, and PUYAN CHEN. "Expression of cecropin B in Pichia pastoris and its bioactivity in vitro." Experimental and Therapeutic Medicine 2, no. 4 (2011): 655–60. http://dx.doi.org/10.3892/etm.2011.262.

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29

Lucca, A. J. De, J. M. Bland, C. B. Vigo, T. J. Jacks, J. Peter, and T. J. Walsh. "D-Cecropin B: proteolytic resistance, lethality for pathogenic fungi and binding properties." Medical Mycology 38, no. 4 (January 2000): 301–8. http://dx.doi.org/10.1080/mmy.38.4.301.308.

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De Lucca, A. J., J. M. Bland, C. B. Vigo, T. J. Jacks, J. Peter, and T. J. Walsh. "D-Cecropin B: proteolytic resistance, lethality for pathogenic fungi and binding properties." Medical Mycology 38, no. 4 (August 1, 2000): 301–8. http://dx.doi.org/10.1080/714030954.

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31

DE LUCCA, BLAND, JACKS, GRIMM, and WALSH. "Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin." Medical Mycology 36, no. 5 (October 1998): 291–98. http://dx.doi.org/10.1046/j.1365-280x.1998.00160.x.

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DE LUCCA, BLAND, JACKS, GRIMM, and WALSH. "Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin." Medical Mycology 36, no. 5 (July 25, 2008): 291–98. http://dx.doi.org/10.1111/j.1365-280x.1998.00160.x.

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De Lucca, A. J., J. M. Bland, T. J. Jacks, C. Grimm, and T. J. Walsh. "Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin." Medical Mycology 36, no. 5 (January 1998): 291–98. http://dx.doi.org/10.1080/02681219880000461.

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Imamura, Morikazu, Yuichi Nakahara, Toshio Kanda, Toshiki Tamura, and Kiyoko Taniai. "A transgenic silkworm expressing the immune-inducible cecropin B-GFP reporter gene." Insect Biochemistry and Molecular Biology 36, no. 5 (May 2006): 429–34. http://dx.doi.org/10.1016/j.ibmb.2006.03.002.

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35

Saugar, José María, Teresa Alarcón, Susana López-Hernández, Manuel López-Brea, David Andreu, and Luis Rivas. "Activities of Polymyxin B and Cecropin A-Melittin Peptide CA(1-8)M(1-18) against a Multiresistant Strain of Acinetobacter baumannii." Antimicrobial Agents and Chemotherapy 46, no. 3 (March 2002): 875–78. http://dx.doi.org/10.1128/aac.46.3.875-878.2002.

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ABSTRACT Polymyxin B (PXB) and the cecropin A-melittin hybrid CA(1-8)M(1-18) (KWKLFKKIGIGAVLKVLTTGLPALIS-NH2) were compared for antibiotic activity on reference and multiresistant Acinetobacter baumannii strains. Significant differences for both peptides were observed on their inner membrane interaction and inhibition by environmental factors, supporting the use of CA(1-8)M(1-18) as a potential alternative to PXB against Acinetobacter.

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Urban, Carl, Emerald Tay, Tomaz Koprivnjak, Jerrold Weiss, Noriel Mariano, James J. Rahal, and Conrado Ponio. "Polymyxin B-Resistant Acinetobacter baumanniiClinical Isolate Susceptible to Recombinant BPI21 and Cecropin P1." Antimicrobial Agents and Chemotherapy 45, no. 3 (March 1, 2001): 994–95. http://dx.doi.org/10.1128/aac.45.3.994-995.2001.

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37

Su, Xiuxia, Jia Xu, Jing Zhang, Dong Yang, Wenjing Huo, and Chen He. "Detection of Cecropin B by liquid-crystal biosensor based on AuNPs signal amplification." Liquid Crystals 47, no. 12 (March 2, 2020): 1794–802. http://dx.doi.org/10.1080/02678292.2020.1729425.

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38

Luo, Chao-chao, De-yun Yin, Xue-jun Gao, Qing-zhang Li, and Li Zhang. "Goat Mammary Gland Expression of Cecropin B to Inhibit Bacterial Pathogens Causing Mastitis." Animal Biotechnology 24, no. 1 (January 2013): 66–78. http://dx.doi.org/10.1080/10495398.2012.745417.

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39

Chen, Hueih Min, Shiu-Chiu Chan, Jao-Chang Lee, Chia-Ching Chang, Marudhamuthu Murugan, and Ralph W. Jack. "Transmission electron microscopic observations of membrane effects of antibiotic cecropin B onEscherichia coli." Microscopy Research and Technique 62, no. 5 (October 29, 2003): 423–30. http://dx.doi.org/10.1002/jemt.10406.

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40

Wu, Chunli, Xiaoping Geng, Shengyun Wan, Hui Hou, Fanzong Yu, Benli Jia, and Lei Wang. "Cecropin-P17, an analog of Cecropin B, inhibits human hepatocellular carcinoma cell HepG-2 proliferation via regulation of ROS, Caspase, Bax, and Bcl-2." Journal of Peptide Science 21, no. 8 (May 23, 2015): 661–68. http://dx.doi.org/10.1002/psc.2786.

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41

Wang, Qiang, Meijia Ren, Xiaoyong Liu, Hengchuan Xia, and Keping Chen. "Identification and characterization of novel short-type BmPGRP-S4 from the silkworm, Bombyx mori, involved in innate immunity." Zeitschrift für Naturforschung C 75, no. 1-2 (January 28, 2020): 13–21. http://dx.doi.org/10.1515/znc-2019-0093.

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AbstractPeptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that can recognize bacterial peptidoglycans and trigger the innate immune response of insects. Here, we identified and characterized a novel short-type Bombyx mori peptidoglycan recognition proteins short-4 (BmPGRP-S4) in a lepidopteran insect, Bombyx mori. BmPGRP-S4 exhibited a cDNA sequence length of 600 bp, encoding 199 aa with a protein molecular weight of 22 kDa. Multiple sequence alignment revealed that BmPGRP-S4 contains a conserved PGRP domain. Quantitative real-time polymerase chain reaction analysis showed that BmPGRP-S4 is highly expressed in the early developmental stages of silkworm larvae and presents tissue-specific expression in hemocytes. Interestingly, BmPGRP-S4 expression is significantly induced by bacterial infection in the midgut, fat body, and hemocytes. Furthermore, a dual luciferase reporter gene assay revealed that BmPGRP-S4 can activate the expression of the antimicrobial peptide genes lebocin, moricin, cecropin D, cecropin B, and attacin. Taken together, these results suggest that BmPGRP-S4 plays an important role in the innate immune response of silkworms.

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Taniai, Kiyoko, Yusuke Kato, Hirohiko Hirochika, and Minoru Yamakawa. "Isolation and nucleotide sequence of cecropin B cDNA clones from the silkworm, Bombyx mori." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1132, no. 2 (September 1992): 203–6. http://dx.doi.org/10.1016/0167-4781(92)90013-p.

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43

Shen, Xinkun, Fei Zhang, Ke Li, Chenhu Qin, Pingping Ma, Liangliang Dai, and Kaiyong Cai. "Cecropin B loaded TiO2 nanotubes coated with hyaluronidase sensitive multilayers for reducing bacterial adhesion." Materials & Design 92 (February 2016): 1007–17. http://dx.doi.org/10.1016/j.matdes.2015.12.126.

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44

Romoli, Ottavia, Shruti Mukherjee, Sk Abdul Mohid, Arkajyoti Dutta, Aurora Montali, Elisa Franzolin, Daniel Brady, et al. "Enhanced Silkworm Cecropin B Antimicrobial Activity against Pseudomonas aeruginosa from Single Amino Acid Variation." ACS Infectious Diseases 5, no. 7 (May 2, 2019): 1200–1213. http://dx.doi.org/10.1021/acsinfecdis.9b00042.

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45

Lee, P. H. A., S. M. Harris, L. Zhang, T. J. Falla, and R. L. Gallo. "143 HB?107, A Non?Antimicrobial Fragment of Cecropin B, Accelerates Murine Wound Repair." Wound Repair and Regeneration 12, no. 2 (March 2004): A37. http://dx.doi.org/10.1111/j.1067-1927.2004.0abstractel.x.

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Ghiselli, Roberto, Andrea Giacometti, Oscar Cirioni, Federico Mocchegiani, Fiorenza Orlando, Giuseppina DʼAmato, Valerio Sisti, Giorgio Scalise, and Vittorio Saba. "Cecropin B Enhances Betalactams Activities in Experimental Rat Models of Gram-Negative Septic Shock." Annals of Surgery 239, no. 2 (February 2004): 251–56. http://dx.doi.org/10.1097/01.sla.0000108673.25385.03.

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47

Nordeen, Russell O., Stephen L. Sinden, Jesse M. Jaynes, and Lowell D. Owens. "Activity of cecropin SB37 against protoplasts from several plant species and their bacterial pathogens." Plant Science 82, no. 1 (January 1992): 101–7. http://dx.doi.org/10.1016/0168-9452(92)90012-b.

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48

De-Simone, Salvatore G., Andre L. A. Souza, Jorge L. S. Pina, Ivan N. Junior, Maria C. Lourenço, and David W. Provance. "Bactericidal Activity of a Cationic Peptide on Neisseria meningitidis." Infectious Disorders - Drug Targets 19, no. 4 (December 23, 2019): 421–27. http://dx.doi.org/10.2174/1871526518666180816132414.

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Background: The increasing prevalence of antibiotic resistant bacteria has raised an urgent need for substitute remedies. Antimicrobial peptides (AMPs) are considered promising candidates to address infections by multidrug-resistant bacteria through new mechanisms of action that require a careful evaluation of their performance. Objective: Identification of effective AMPs against Neisseria meningitidis, which represents a pathogen of great public health importance worldwide that is intrinsically resistant to some AMPs, such as polymyxin B. Methods: A cationic 11-residue peptide (KLKLLLLLKLK), referred to as poly-Leu, was synthesized and its antimeningococcal activity was compared to cecropin A and poly-P (KLKPPPPPKLK) through a variety of assays. Flow cytometry was used to measure propidium iodide uptake by N. meningitidis serotype B as an indicator of the effectiveness of each peptide when added to cultures at different concentrations. Results: The addition of the poly-Leu peptide led to a 90.3% uptake of the dye with an EC50 value of 7.9 µg mL-1. In contrast, uptake was <10% in cells grown in the absence of peptides or with an identical concentration of cecropin and poly-Pro peptides. Electron micrographs indicated that the integrity of the cellular wall and internal membrane was impacted in relation to peptide concentrations, which was confirmed by the detection of released alkaline phosphatase from the periplasmic space due to disruption of the external membrane. Conclusion: Poly-Leu peptide demonstrated definitive antimicrobial activity against N. meningitidis.

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Thomas, Dyna Susan. "Expression of Silk Sericin-Cecropin B Fusion Protein in Pichia pastoris and Cell-Free System." Bioscience Biotechnology Research Communications 13, no. 2 (June 25, 2020): 981–84. http://dx.doi.org/10.21786/bbrc/13.2/88.

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50

Lee, Phillip H. A., Jennifer A. Rudisill, Kenneth H. Lin, Lijuan Zhang, Scott M. Harris, Timothy J. Falla, and Richard L. Gallo. "HB-107, a nonbacteriostatic fragment of the antimicrobial peptide cecropin B, accelerates murine wound repair." Wound Repair and Regeneration 12, no. 3 (June 2004): 351–58. http://dx.doi.org/10.1111/j.1067-1927.2004.012303.x.

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