A simple procedure for isolation, identification and characterization of vibrio cholerae from clinical samples

2017 ◽  
Vol 8 (4) ◽  
Author(s):  
PARIMAL DUA ◽  
AMIT KARMAKAR ◽  
KUNAL DUTTA ◽  
CHANDRADIPA GHOSH
Keyword(s):  
Vibrio Cholerae ◽  
Simple Procedure ◽  
Clinical Samples ◽  
Identification And Characterization

scholarly journals Identification and Characterization of OscR, a Transcriptional Regulator Involved in Osmolarity Adaptation in Vibrio cholerae

2009 ◽  
Vol 191 (13) ◽  
pp. 4082-4096 ◽  
Author(s):  
Nicholas J. Shikuma ◽  
Fitnat H. Yildiz
Keyword(s):  
Vibrio Cholerae ◽  
Biofilm Formation ◽  
Transcriptional Regulator ◽  
Dependent Manner ◽  
Genome Wide ◽  
Low Salt ◽  
Adaptation Response ◽  
Matrix Production ◽  
Identification And Characterization

ABSTRACT Vibrio cholerae is a facultative human pathogen. In its aquatic habitat and as it passes through the digestive tract, V. cholerae must cope with fluctuations in salinity. We analyzed the genome-wide transcriptional profile of V. cholerae grown at different NaCl concentrations and determined that the expression of compatible solute biosynthesis and transporter genes, virulence genes, and genes involved in adhesion and biofilm formation is differentially regulated. We determined that salinity modulates biofilm formation, and this response was mediated through the transcriptional regulators VpsR and VpsT. Additionally, a transcriptional regulator controlling an osmolarity adaptation response was identified. This regulator, OscR (osmolarity controlled regulator), was found to modulate the transcription of genes involved in biofilm matrix production and motility in a salinity-dependent manner. oscR mutants were less motile and exhibited enhanced biofilm formation only under low-salt conditions.

Identification and Characterization of a New Class of (6–4) Photolyase from Vibrio cholerae

Biochemistry ◽  
2019 ◽  
Vol 58 (43) ◽  
pp. 4352-4360 ◽  
Author(s):  
Ugur Meric Dikbas ◽  
Mehmet Tardu ◽  
Asena Canturk ◽  
Seref Gul ◽  
Gozde Ozcelik ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
New Class ◽  
Identification And Characterization

scholarly journals Identification and Characterization of a Peptide Affinity Reagent for Detection of Noroviruses in Clinical Samples

2013 ◽  
Vol 51 (6) ◽  
pp. 1803-1808 ◽  
Author(s):  
J. D. Rogers ◽  
N. J. Ajami ◽  
B. G. Fryszczyn ◽  
M. K. Estes ◽  
R. L. Atmar ◽  
...  
Keyword(s):  
Clinical Samples ◽  
Affinity Reagent ◽  
Peptide Affinity ◽  
Identification And Characterization

Isolation, identification, and characterization of Vibrio cholerae from the Danube River in Slovakia

2012 ◽  
Vol 57 (3) ◽  
pp. 191-197 ◽  
Author(s):  
Milan Seman ◽  
Miloslava Prokšová ◽  
Jozef Rosinský ◽  
Peter Ferianc
Keyword(s):  
Vibrio Cholerae ◽  
Danube River ◽  
The Danube River ◽  
Identification And Characterization

scholarly journals Molecular Characterization of Vibrio cholerae Isolated From Clinical Samples in Kurdistan Province, Iran

2015 ◽  
Vol 8 (5) ◽  
Author(s):  
Rashid Ramazanzadeh ◽  
Samaneh Rouhi ◽  
Pegah Shakib ◽  
Babak Shahbazi ◽  
Farzam Bidarpour ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
Molecular Characterization ◽  
Clinical Samples

scholarly journals Characterization of a novel protective monoclonal antibody that recognizes an epitope common to Vibrio cholerae Ogawa and Inaba serotypes

Microbiology ◽  
2009 ◽  
Vol 155 (7) ◽  
pp. 2353-2364 ◽  
Author(s):  
Madushini N. Dharmasena ◽  
Shelly J. Krebs ◽  
Ronald K. Taylor
Keyword(s):  
Monoclonal Antibody ◽  
Phage Display ◽  
Vibrio Cholerae ◽  
Lipid A ◽  
Passive Immunization ◽  
Peptide Mimics ◽  
Peptide Mimic ◽  
Phage Display Libraries ◽  
Identification And Characterization

A novel protective monoclonal antibody (mAb) that recognizes a lipopolysaccharide (LPS) epitope common between serotypes Ogawa and Inaba of the O1 serogroup of Vibrio cholerae was characterized and the potential to develop peptide mimics of this protective LPS epitope was investigated. mAb 72.1 recognizes both Ogawa and Inaba LPS and it is vibriocidal and protective in passive immunization against infection by strains of both serotypes. The cDNA-derived amino acid sequence of mAb 72.1 is closely related to the previously characterized mAb ZAC-3, which is thought to recognize an epitope in the lipid A core region of O1 LPS. In an attempt to develop a peptide mimic-based vaccine against V. cholerae, phage display libraries were screened with mAb 72.1 and 11 peptide mimics were identified. Remarkably, all of the peptide sequences identified from linear phage display libraries contained two cysteine residues, suggesting that mAb 72.1 preferentially binds to peptides constrained with a disulphide bond. One of the peptide mimics was immunologically characterized. Although immunization of mice with this peptide mimic conjugated to KLH elicited antibodies against the peptide itself, these antibodies did not cross-react with Ogawa or Inaba LPS. Effectiveness of a peptide mimic as a vaccine may depend on how well the peptide can mimic the carbohydrate interactions when binding to the anti-carbohydrate antibody. Thus, investigating how peptides and LPS bind to mAb 72.1 may be useful in improving current peptide mimics or designing more effective peptide mimics. Identification and characterization of novel protective anti-LPS antibodies may be useful in studying protective epitopes of LPS, which may help develop LPS-based therapeutics against V. cholerae.

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