Lipopolysaccharides of Vibrio cholerae: III. Biological functions

Chatterjee, Satadal; Chaudhuri, Keya

doi:10.1016/j.bbadis.2005.08.005

Cited by 37 publications

(35 citation statements)

References 152 publications

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“…cholerae LPS has been known to induce a protective immune response, and is used as a cholera vaccine. The serum antibodies against V. cholerae LPS are elevated following natural disease or oral vaccination, which correlates to a protective ability against cholera (8). OmpW, in contrast to V. cholerae LPS, has been studied less.…”

Section: Discussionmentioning

confidence: 99%

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Serum Anti-Vibrio cholerae Immunoglobulin Isotype in BALB/c Mice Immunized With ompW-Loaded Chitosan

Fasihi-Ramandi¹,

Ghobadi-Ghadikolaee²,

Ahmadi-Renani³

et al. 2016

Int J Enteric Pathog

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Section: Discussionmentioning

confidence: 99%

“…Therefore, these mechanisms interfere with the colonization process that is usually mediated by factors of pilus or non-pilus origin (7). The lipopolysaccharide (LPS) content of V. cholerae, in addition to the ompW protein, has been reported to induce a protective immunity in the host (8).…”

Section: Introductionmentioning

confidence: 99%

Serum Anti-Vibrio cholerae Immunoglobulin Isotype in BALB/c Mice Immunized With ompW-Loaded Chitosan

Fasihi-Ramandi¹,

Ghobadi-Ghadikolaee²,

Ahmadi-Renani³

et al. 2016

Int J Enteric Pathog

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“…This was compared to the vaccinees. LPS is considered as a major protective antigen for V. cholerae and thereby antibodies with high avidity directed against the LPS play a crucial role in protection [4]. In young children both LPS and to the antigenic component of the LPS, the O-specific polysaccharide (OSP), specific immune response is poor following natural infection.…”

Section: Short Communicationmentioning

confidence: 99%

Short Communication on: Study of Avidity of Antigen-Specific Antibody as a Means of Understanding Development of Long-Term Immunological Memory after Vibrio cholerae O1 Infection

Alam¹,

Bhuiyan²,

Qadri³

2017

J Vaccines Vaccin

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Short CommunicationInteraction between antigen and antibody modulates key biological processes in neutralizing and eliminating pathogenic microorganisms following infection. The strength of this interaction depends on the affinity, valency and three dimensional arrangements of the interacting epitopes and paratopes. The measure of the overall strength of this multimeric interaction is termed as ' Avidity' . Development of antibody with high avidity is a crucial feature of a secondary immune response followed by a low avidity antibody producing primary response [1,2]. Thus antibody avidity has been used as a marker for B cell maturation and is an important surrogate for determining long term immunological memory responses to pathogens. In our article entitled "Study of avidity of antigen-specific antibody as a means of understanding development of long-term immunological memory after Vibrio cholerae O1 infection" we showed that antibody avidity after infection and immunization is a good correlate of the development and maintenance of memory B cell responses to V. cholerae O1 antigens. To the best of our knowledge this is the first study that assesses antibody avidity following a non-invasive mucosal infection [3].V. cholerae infection still remains a significant threat for humans residing or travelling to the regions of the world with limited resources for clean water and adequate sanitation. Naturally occurring cholera infection is known to provide protection against the disease for several years, although the currently available licensed oral cholera vaccines fails to induce comparable protective immunity especially in young children. Therefore, understanding the mechanism of protection against cholera is crucial for the development of an effective vaccine.Our study showed that individuals immunized with a killed whole cell cholera vaccine (Dukoral) did not generate immune response comparable to the patients d following a severe cholera requiring hospitalization. Cholera patients showed a longer persistence of IgG and IgA antibodies of high avidity to both T cell dependent antigen, cholera toxin as well as the T cell independent antigen lipopolysaccharide (LPS). This was compared to the vaccinees. LPS is considered as a major protective antigen for V. cholerae and thereby antibodies with high avidity directed against the LPS play a crucial role in protection [4]. In young children both LPS and to the antigenic component of the LPS, the O-specific polysaccharide (OSP), specific immune response is poor following natural infection. High avidity antibodies to LPS can provide protection by inhibiting the motility of V. cholerae strains which can prevent a successful colonization.Generation and long term persistence of LPS specific antibodies with high avidity in patients infected with cholera may explain in part that protective mechanism develops in naturally occurring cholera. The lack of such responses in vaccinees thus can account for the lack of long term protection in these individuals. Similarly, longer persis...

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“…Systemic LPS leads to inflammation, multiple organ failure, shock, and potentially death (Chatterjee & Chaudhuri, 2006). The O-SP by itself is poorly immunogenic (Gupta et al, 1992(Gupta et al, , 1998.…”

Section: Introductionmentioning

confidence: 99%

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

2009

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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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Lipopolysaccharides of Vibrio cholerae: III. Biological functions

Cited by 37 publications

References 152 publications

Serum Anti-Vibrio cholerae Immunoglobulin Isotype in BALB/c Mice Immunized With ompW-Loaded Chitosan

Serum Anti-Vibrio cholerae Immunoglobulin Isotype in BALB/c Mice Immunized With ompW-Loaded Chitosan

Short Communication on: Study of Avidity of Antigen-Specific Antibody as a Means of Understanding Development of Long-Term Immunological Memory after Vibrio cholerae O1 Infection

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

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