Binding properties of Streptococcus suis for immunoglobulin G and other plasma proteins.
Immunoglobulin G (IgG) binding proteins on the surface of Streptococcus suis could be readily detected by direct cultivation of the bacteria on nitrocellulose membranes and subsequent treatment of the membranes with human IgG. Among the 75 S. suis isolates tested two cultures (S. suis P43, S. suis P143) caused a blue colouration of the membranes indicating IgG binding activities. The IgG binding proteins could be solubilized by heat treatment of the bacteria at an acid pH and also by mutanolysin treatment. Western blot analysis revealed numerous protein bands with IgG binding activities. The IgG binding proteins were also released into the culture supernatant of the bacteria. This could be detected for 51 of the 75 S. suis using a microfiltration assay. In binding studies with 125I-IgG S. suis P43 and S. suis P143 but none of the other S. suis isolates showed a significant binding of the protein. These two cultures additionally bound 125I-albumin, 125I-alpha 2-macroglobulin and 125I-fibrinogen all from humans but not 125I-chicken IgG or 125I-human haptoglobin 2-1. The binding profiles of the two S. suis cultures tested indicate a close relation of these binding proteins with streptococcal protein G.
Salasia
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Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität Giessen, Germany.
Lämmler
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D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D015153:Blotting, Western / Q000662:veterinary; D002645:Chickens; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000378:metabolism*; D007457:Iodine Radioisotopes; D012709:Serum Albumin / Q000378:metabolism; D017011:Streptococcus suis / Q000378:metabolism*; D000511:alpha-Macroglobulins / Q000378:metabolism
D001798:Blood Proteins; D007074:Immunoglobulin G; D007457:Iodine Radioisotopes; D012709:Serum Albumin; D000511:alpha-Macroglobulins; D005340:Fibrinogen