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Updated: Jun 25, 2026

Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes
Published on: September 19, 2013
IgA-specific proteins of pathogenic bacteria
1Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia.
Abstract:
Data on structure and specificity of bacterial IgA receptors (IgA-binding M-like proteins Arp4 and Sir22 from hemolytic streptococci of serogroup A, beta-antigen from hemolytic streptococci of serogroup B, and SSL family proteins from Staphylococcus aureus) are surveyed in this review. The principal conclusion derived from comparison is the fact that all bacterial receptors bind the same site in the IgA molecule overlapping with the binding site of endogenous human IgA receptor CD89. We assume that this site, consisting of spatially close amino acid strands Leu257-Gly259 in domain Calpha2 and Pro440-Phe443 in domain Calpha3, is subject to conformational rearrangement induced by the binding of antigen in the IgA active site.
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