Faculty Opinions recommendation of Identification of the membrane penetrating domain of Vibrio cholerae cytolysin as a beta-barrel structure.

Background: Cholera triggered by Vibrio cholerae remains the main reason for morbidity and mortality all over the world. In addition, salmonellosis is regarded as an infectious disease that makes it essential for the identification and detection of Salmonella. With a beta-barrel structure consisting of eight non-parallel beta strands, OmpW family is widely distributed among gram-negative bacteria. Moreover, OmpW isolated from S. typhimurium and Vibrio cholerae can be used in vaccine design. Methods: Topology prediction was determined. T-cell and B-cell epitopes were selected from exposed areas, and sequence conservancy was evaluated. The remaining loops and inaccessible residues were removed to prepare OmpW-1. High antigenicity peptides were detected to replace inappropriate residues to obtain OmpW-2. Physicochemical properties were assessed, and antigenicity, hydrophobicity, flexibility, and accessibility were compared to the native Omp-W structure. Low score areas were removed from the designed structure for preparing the OmpW-3. To construct OmpW-4, TTFrC was used as T-CD4+ cell-stimulating factor and CTB as adjuvant to the end of the C-terminal of this sequence, which can increase the antigenicity and sequence density. The sequences were re-analyzed to delete the unfavorable residues. Besides, the solubility of the mature OmpW and the designed structure were predicted while overexpressed in E. coli. Results: The designed vaccine is a stable protein which has immune cells recognizing epitopes and is considered as an antigen. The construct can be overexpressed in a E. coli. Conclusion: The multi-epitope vaccine is a suitable stimulator for immune system and would be a candidate for experimental research. Recent patents describing numerous inventions related to the clinical facets of vaccine peptide against human infectious disease.

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Implication of Cholesterol in Regulating the Membrane-Interaction Mechanism of Vibrio cholerae Cytolysin, a Beta-Barrel Pore-Forming Toxin

Biophysical Journal ◽

10.1016/j.bpj.2018.11.1226 ◽

2019 ◽

Vol 116 (3) ◽

pp. 223a

Author(s):

Reema Kathuria ◽

Kausik Chattopadhyay

Keyword(s):

Vibrio Cholerae ◽

Interaction Mechanism ◽

Membrane Interaction ◽

Beta Barrel

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Revisiting the oligomerization mechanism of Vibrio cholerae cytolysin, a beta-barrel pore-forming toxin

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2016.05.006 ◽

2016 ◽

Vol 474 (3) ◽

pp. 421-427 ◽

Cited By ~ 1

Author(s):

Anand Kumar Rai ◽

Kausik Chattopadhyay

Keyword(s):

Vibrio Cholerae ◽

Beta Barrel

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Physicochemical constraints of elevated pH affect efficient membrane interaction and arrest an abortive membrane-bound oligomeric intermediate of the beta-barrel pore-forming toxin Vibrio cholerae cytolysin

Archives of Biochemistry and Biophysics ◽

10.1016/j.abb.2015.07.019 ◽

2015 ◽

Vol 583 ◽

pp. 9-17 ◽

Cited By ~ 3

Author(s):

Anand Kumar Rai ◽

Nidhi Kundu ◽

Kausik Chattopadhyay

Keyword(s):

Vibrio Cholerae ◽

Membrane Interaction ◽

Beta Barrel ◽

Membrane Bound

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In vivo Production of Soluble Inorganic Pyrophosphatases in Two Strains of Vibrio cholerae

Bangladesh Journal of Microbiology ◽

10.3329/bjm.v24i1.1235 ◽

1970 ◽

Vol 24 (1) ◽

pp. 38-41

Author(s):

Taslima Taher Lina ◽

Mohammad Ilias

Keyword(s):

Vibrio Cholerae ◽

Specific Activity ◽

Experimental Conditions ◽

Environmental Strain ◽

Cell Extracts ◽

Atcc Strain ◽

The Family ◽

Effects Of Ph ◽

Vibrio Cholerae O1

The in vivo production of soluble inorganic pyrophosphatases (PPases) was investigated in two strains, namely, Vibrio cholerae EM 004 (environmental strain) and Vibrio cholerae O1 757 (ATCC strain). V. cholerae is known to contain both family I and family II PPase coding sequences. The production of family I and family II PPases were determined by measuring the enzyme activity in cell extracts. The effects of pH, temperature, salinity of the growth medium on the production of soluble PPases were studied. In case of family I PPase, V. cholerae EM 004 gave the highest specific activity at pH 9.0, with 2% NaCl + 0.011% NaF and at 37°C. The strain V. cholerae O1 757 gave the highest specific activity at pH 9.0, with media containing 0% NaCl and at 37°C. On the other hand, under all the conditions family II PPase did not give any significant specific activity, suggesting that the family II PPase was not produced in vivo in either strains of V. cholerae under different experimental conditions. Keywords: Vibrio cholerae, Pyrophosphatases (PPases), Specific activityDOI: http://dx.doi.org/10.3329/bjm.v24i1.1235 Bangladesh J Microbiol, Volume 24, Number 1, June 2007, pp 38-41

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