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dc.contributor.authorBorrelli, S
dc.contributor.authorHossany, RB
dc.contributor.authorPinto, BM
dc.date.accessioned2020-06-29T10:14:30Z
dc.date.available2020-06-29T10:14:30Z
dc.date.issued2008
dc.identifier.issn1556-6811
dc.identifier.doi10.1128/CVI.00050-08
dc.identifier.urihttp://hdl.handle.net/10072/395008
dc.description.abstractAn approach to vaccine design is the use of molecules that mimic the immunogenic element of interest. In this context, the interaction of MDWNMHAA, a peptide mimic of the Shigella flexneri Y O polysaccharide (PS), with an anti-carbohydrate monoclonal antibody, as studied previously by X-ray crystallography, suggested the presence of functional rather than structural mimicry and a bound peptide conformation that was not represented significantly in the free-ligand ensemble. The antibody response elicited by an MDWNMHAA-carrier protein (tetanus toxoid [TT]) conjugate has now been investigated in BALB/c mice. The mice were immunized following a homologous prime/boost strategy using MDWNMHAA-TT as the immunogen. The mice showed anti-peptide antibody (immunoglobulin G [IgG]) titers that increased after being boosted. High anti-lipopolysaccharide (LPS) (IgG) titers were observed after the last boost. A faster immune response, with cross-reactive titers, was observed with a peptide conjugate with 30% more copies of the peptide. The binding of anti-peptide polyclonal antibodies to LPS could be inhibited by LPS, PS, MDWNMHAA, and MDWNMHAA-bovine serum albumin, as assessed by inhibition enzyme-linked immunosorbent assay. Conversely, mice immunized with PS-TT showed IgG anti-peptide titers. These data demonstrate the cross-reactivity of the antibody response and support the hypothesis that functional, as opposed to structural, mimicry of the S. flexneri Y O PS by MDWNMHAA or the underrepresentation of the bound ligand conformation in the free-ligand ensemble does not compromise immunological cross-reactivity. Prime/boost strategies were performed with a heterologous boost of PS-TT or MDWNMHAA-TT. They led to high anti-LPS titers after only three injections, suggesting alternatives to improve the immunogenicity of the carbohydrate-mimetic peptide and confirming the antigenic mimicry.
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Society for Microbiology
dc.relation.ispartofpagefrom1106
dc.relation.ispartofpageto1114
dc.relation.ispartofissue7
dc.relation.ispartofjournalClinical and Vaccine Immunology
dc.relation.ispartofvolume15
dc.subject.fieldofresearchImmunology
dc.subject.fieldofresearchcode1107
dc.titleImmunological evidence for functional rather than structural mimicry by a Shigella flexneri Y polysaccharide-mimetic peptide
dc.typeJournal article
dcterms.bibliographicCitationBorrelli, S; Hossany, RB; Pinto, BM, Immunological evidence for functional rather than structural mimicry by a Shigella flexneri Y polysaccharide-mimetic peptide, Clinical and Vaccine Immunology, 2008, 15 (7), pp. 1106-1114
dc.date.updated2020-06-29T10:11:03Z
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 2018 American Society for Microbiology. The attached file is reproduced here in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
gro.hasfulltextFull Text
gro.griffith.authorPinto, Mario M.


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