Binding of native alpha 2-macroglobulin to human group G streptococci.

Infection and Immunity
H P Müller, L K Rantamäki

Abstract

Binding of human alpha 2-macroglobulin (alpha 2M) to group G streptococci and to their immunoglobulin G (IgG)-binding proteins (protein G) was investigated. Native alpha 2M bound specifically to strain G-148 with an apparent dissociation constant of (2.2 +/- 1.5) x 10(-9) M. Proteinase-complexed alpha 2M did not compete for the binding sites, and 125I-labelled proteinase-complexed alpha 2M did not bind to the bacteria. Binding of native alpha 2M to the cells was not affected by IgG or protein G consisting of only IgG-binding domains. 125I-labelled recombinant protein G did not bind to native or proteinase-complexed alpha 2M. However, a lysate of G-148 cells inhibited binding of alpha 2M to the bacteria, and immobilized wild-type protein G bound alpha 2M directly from fresh human plasma. In 13 group G streptococcal isolates, IgG-binding proteins were immunologically identified as protein G. In 11 isolates, these molecules reacted also with alpha 2M and human serum albumin (HSA). Western blots (immunoblots) of two wild-type protein G variants revealed identical bands reactive with goat IgG, HSA, and native alpha 2M. Digestion of wild-type protein G with clostripain destroyed in both variants the binding sites for alpha 2M but not...Continue Reading

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Citations

Oct 23, 2012·Journal of Cellular Physiology·Ahmed A RehmanFahim H Khan
May 1, 1997·Zentralblatt für Veterinärmedizin. Reihe B. Journal of veterinary medicine. Series B·H Ding, C Lämmler
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Mar 16, 2019·Microbiology Spectrum·Horst Malke
May 22, 2019·Microbiology Spectrum·Claire E TurnerAndroulla Efstratiou

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