Further studies on immunoglobulin G- and albumin-binding properties of streptococci of serological group L.
In this study, all 88 streptococci of serological group L isolated from cows, pigs, poultry and humans bound 125I-immunoglobulin G, and, in addition, 22 cultures interacted with 125I-albumin. IgG- and albumin-binding sites were solubilized from the streptococcal surface by heat extraction at an acid pH and also by mutanolysin treatment of the bacteria. Western blot analysis of these binding proteins revealed that almost identical protein bands were responsible for 125I-IgG and -albumin binding. Certain protein fractions of the cultures interacted exclusively with 125I-IgG, indicating that there are two groups of IgG receptors among streptococci of this serogroup.
Sippel
K
K
Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität Giessen, Germany.
Lämmler
C
C
D000418:Albumins / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002418:Cattle Diseases / Q000382:microbiology; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D011200:Poultry; D011201:Poultry Diseases / Q000382:microbiology; D013290:Streptococcal Infections / Q000382:microbiology / Q000662:veterinary*; D013291:Streptococcus / Q000145:classification / Q000276:immunology / Q000378:metabolism*; D013552:Swine; D013553:Swine Diseases / Q000382:microbiology
D000418:Albumins; D007074:Immunoglobulin G