Toward a better understanding of the basis of the molecular mimicry of polysaccharide antigens by peptides: the example of Shigella flexneri 5a.

Title:

Toward a better understanding of the basis of the molecular mimicry of polysaccharide antigens by peptides: the example of Shigella flexneri 5a.

identifier:	1244652
description:	epitope description:beta-D-GlcpNAc-(1->2)-alpha-L-Rhap-(1->2)-[alpha-D-Glcp-(1->3)]-alpha-L-Rhap-(1->3)-alpha-L-Rhap antigen name:lipopolysaccharide host organism:Mus musculus antibody name:I3, C5
aggregation:	instance of dataset
availability:	available
primaryPublications:	16251186

study type:	b cell assays
subject species:	Shigella flexneri 5a

fullName:	Marie-Jeanne Clé ment Antoine Fortuné Armelle Phalipon Vé ronique Marcel-Peyre Catherine Simenel Anne Imberty Muriel Delepierre Laurence A Mulard

method:	antigen inhibition

name:	Toward a better understanding of the basis of the molecular mimicry of polysaccharide antigens by peptides: the example of Shigella flexneri 5a.
description:	Two protective IgA mAbs raised against S.flexneri, specific for the O-antigen (O-Ag) part of LPS, are tested for the inhibition of LPS recognition by this pentasaccharide. For both a similar IC50 value of 25mM (due to the multivalency of LPS and the dimeric nature of IgAs this is not a true measurement of affinity). Structural definition of the complexed (with C5 or I3) and free form of this oligosaccharide by NMR experiments allowed for the definition of glucose E as a key element in mAb recognition. Also the methyl group of the B sugar give strong NMR signals enhancements.

name:	iedb
homePage:	http://www.iedb.org

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