A comparative study of the properties of Vibrio cholerae O139, O1 and other non-O1 strains. 1995

R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
Department of Microbiology, Bose Institute, Calcutta, India.

Vibrio cholerae O139 organisms isolated from different parts of India and from Bangladesh were characterised with respect to their haemagglutination (HA) activity, plasmid content, cholera toxin (CT) production, cell surface protein and lipopolysaccharide (LPS) profiles, and antigenic properties. Of 28 V. cholerae O139 isolates tested, 14 (50%) were shown to agglutinate chicken erythrocytes; the HA activity was sensitive to D-mannose 0.1%. In parallel experiments, 12 (92.3%) of 13 V. cholerae O1 (El Tor) and 12 (75%) of 16 non-O1, non-O139 strains agglutinated chicken erythrocytes. Plasmid analysis of 32 O139 isolates showed that 12 (37.5%) carried one or more plasmids of 35.8-2.6 MDa. Plasmids were not detected in any of the V. cholerae O1 strains, although plasmids were demonstrable in 35% of the non-O1, non-O139 strains tested. V. cholerae O139 isolates showed an ability to produce CT that depended on media composition and other cultural conditions. A comparison of envelope and outer-membrane protein profiles between O1 and O139 isolates failed to show any significant differences. LPS analysis of O139 isolates revealed that these organisms were devoid of long "O" side-chain polysaccharides. Some of the non-O1, non-O139 strains also showed similar LPS profiles whereas others showed the presence of long repetitive "O" side-chain polysaccharides similar to those seen in O1 organisms. An antiserum raised against V. cholerae O1 strain O395 did not show any significant reactivity towards O139 and non-O1, non-O139 strains although it reacted with other O1 strains. Furthermore, the anti-O1 serum induced marked protection against challenge with an O1 strain but not with an O139 strain in passive protection experiments.(ABSTRACT TRUNCATED AT 250 WORDS)

UI MeSH Term Description Entries
D007106 Immune Sera Serum that contains antibodies. It is obtained from an animal that has been immunized either by ANTIGEN injection or infection with microorganisms containing the antigen. Antisera,Immune Serums,Sera, Immune,Serums, Immune
D007194 India A country in southern Asia, bordering the Arabian Sea and the Bay of Bengal, between Burma and Pakistan. The capitol is New Delhi. Republic of India
D008070 Lipopolysaccharides Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed) Lipopolysaccharide,Lipoglycans
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D002771 Cholera An acute diarrheal disease endemic in India and Southeast Asia whose causative agent is VIBRIO CHOLERAE. This condition can lead to severe dehydration in a matter of hours unless quickly treated. Vibrio cholerae Infection,Choleras,Infection, Vibrio cholerae,Infections, Vibrio cholerae,Vibrio cholerae Infections
D002772 Cholera Toxin An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. Cholera Toxin A,Cholera Toxin B,Cholera Toxin Protomer A,Cholera Toxin Protomer B,Cholera Toxin Subunit A,Cholera Toxin Subunit B,Choleragen,Choleragenoid,Cholera Enterotoxin CT,Cholera Exotoxin,Cholera Toxin A Subunit,Cholera Toxin B Subunit,Procholeragenoid,Enterotoxin CT, Cholera,Exotoxin, Cholera,Toxin A, Cholera,Toxin B, Cholera,Toxin, Cholera
D004196 Disease Outbreaks Sudden increase in the incidence of a disease. The concept includes EPIDEMICS and PANDEMICS. Outbreaks,Infectious Disease Outbreaks,Disease Outbreak,Disease Outbreak, Infectious,Disease Outbreaks, Infectious,Infectious Disease Outbreak,Outbreak, Disease,Outbreak, Infectious Disease,Outbreaks, Disease,Outbreaks, Infectious Disease
D004269 DNA, Bacterial Deoxyribonucleic acid that makes up the genetic material of bacteria. Bacterial DNA
D004587 Electrophoresis, Agar Gel Electrophoresis in which agar or agarose gel is used as the diffusion medium. Electrophoresis, Agarose Gel,Agar Gel Electrophoresis,Agarose Gel Electrophoresis,Gel Electrophoresis, Agar,Gel Electrophoresis, Agarose
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked

Related Publications

R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
October 1999, FEMS microbiology letters,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
February 2001, Applied and environmental microbiology,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
November 2008, The Southeast Asian journal of tropical medicine and public health,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
April 2004, Emerging infectious diseases,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
April 1996, Journal of clinical microbiology,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
December 2007, Molecular microbiology,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
April 2001, Presse medicale (Paris, France : 1983),
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
October 2010, Journal of medical microbiology,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
August 2019, Medecine et maladies infectieuses,
R K Nandy, and T K Sengupta, and S Mukhopadhyay, and A C Ghose
April 1995, FEMS immunology and medical microbiology,
Copied contents to your clipboard!