Biochemistry (Moscow)

, Volume 74, Issue 1, pp 12–21 | Cite as

IgA-specific proteins of pathogenic bacteria

  • T. N. Kazeeva
  • A. B. ShevelevEmail author


Data on structure and specificity of bacterial IgA receptors (IgA-binding M-like proteins Arp4 and Sir22 from hemolytic streptococci of serogroup A, β-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 Cα2 and Pro440-Phe443 in domain Cα3, is subject to conformational rearrangement induced by the binding of antigen in the IgA active site.

Key words

IgA IgA-binding proteins CD89 


CHα (Cα)

constant domain of heavy (α) chain of IgA


variable antigen-binding superdomain of Ig


constant superdomain of Ig


receptor specific for Fc-superdomain of IgA


group A and B streptococci, respectively

IgA, IgG, and IgM

immunoglobulins A, G, and M, respectively


3-nitro-4-hydroxy-5-iodophenylacetate (hapten)


secretory form of IgA


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Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  1. 1.Bach Institute of BiochemistryRussian Academy of SciencesMoscowRussia
  2. 2.Chumakov Institute of Poliomyelitis and Viral EncephalitisRussian Academy of Medical Sciences, Leninsky DistrictMoscow RegionRussia

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