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Clinical and Diagnostic Laboratory Immunology, Jul 1995, 478-483, Vol 2, No. 4
R Raeder and MD Boyle
Analysis of immunoglobulin G (IgG)-binding-protein expression by invasive
group A streptococcal isolates of the M1 serotype collected as part of a
Centers for Disease Control and Prevention surveillance study revealed two
distinct phenotypes. One group of type M1 isolates expressed a surface
protein reactive with all four human IgG subclasses (type IIo), while a
second group expressed a surface protein demonstrating significant
reactivity only with human IgG3 (type IIb). The functional forms of
IgG-binding protein were antigenically related, and both were recognized by
a rabbit polyclonal antiserum to serotype M1 but not by normal rabbit
serum. While the quantities of antigenic M1 protein present in the extracts
of representative isolates displaying each phenotype differed, the
functional differences were found to be qualitative and not solely
quantitative. The IgG-binding properties of these antigenically related M1
proteins could be readily distinguished from those of another IgG-binding
protein, protein H. Type M1 isolates of the IIb phenotype differed from
those of the IIo phenotype by secreting larger amounts of a
casein-hydrolyzing protease into culture supernatants.
Copyright © 1995 by the American Society for Microbiology. All rights reserved.
Distinct profiles of immunoglobulin G-binding-protein expression by invasive serotype M1 isolates of Streptococcus pyogenes
Department of Microbiology, Medical College of Ohio, Toledo 43699-0008, USA.
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