Group A streptococcal immunoglobulin-binding proteins: adhesins, molecular mimicry or sensory proteins?
Pathogenic streptococci express multiple immunoglobulin-binding proteins (IGPs) on their surface that are similar in sequence and structure to the antiphagocytic M proteins. Both are evolutionary products of a duplicated ancestral gene and are components of the Vir gene cluster. Except for M proteins, there is little direct experimental evidence to implicate IGPs in pathogenesis. Several functions of IGPs are postulated and discussed.
Dept of Microbiology, University of Minnesota, Minneapolis 55455.
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Cleary
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Retnoningrum
D000818:Animals; D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism*; D013297:Streptococcus pyogenes / Q000276:immunology*
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007136:Immunoglobulins; C014689:streptococcal M protein