Isolation and characterization of a specific receptor for human albumin on a group L Streptococcus.
Certain group L streptococci demonstrate surface receptors for human albumin. Binding of 125I-albumin to group L streptococci could be inhibited by unlabelled albumin preparations from humans, dogs, mice and bovines, but not by albumin from rabbits. The albumin-binding proteins (ABP) could be solubilized from the streptococcal surface by hot acid treatment of the bacteria and isolated by affinity chromatography on human-albumin sepharose. ABP and specific antisera produced against ABP inhibited 125I-albumin binding to group L streptococci. The molecular weight of ABP determined by SDS-PAGE and Western blotting, was approximately 48,000 Dalton. ABP preparations of group G streptococci isolated from bovines and humans demonstrated cross reactivity with antiserum produced against group L streptococcal ABP.
Lämmler
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Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität Giessen, Federal Republic of Germany.
D000418:Albumins / Q000378:metabolism*; D000818:Animals; D001667:Binding, Competitive; D015153:Blotting, Western; D002417:Cattle; D002846:Chromatography, Affinity; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D051379:Mice; D008970:Molecular Weight; D011817:Rabbits; D017457:Receptors, Albumin; D011956:Receptors, Cell Surface / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D013291:Streptococcus / Q000378:metabolism*
D000418:Albumins; D017457:Receptors, Albumin; D011956:Receptors, Cell Surface