AI Article Synopsis
- IgG binding proteins on the surface of Streptococcus suis were detected using nitrocellulose membranes and human IgG treatment, revealing that two specific isolates (S. suis P43 and P143) exhibited strong binding activities.
- Heat treatment at acidic pH and mutanolysin treatment were effective in solubilizing these binding proteins, and Western blot analysis identified multiple IgG binding bands.
- Additionally, a microfiltration assay showed that 51 out of 75 S. suis isolates released IgG binding proteins into the culture supernatant, with P43 and P143 also binding several human proteins, indicating a relationship to streptococcal protein G.
Article Abstract
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.
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| http://dx.doi.org/10.1111/j.1439-0450.1996.tb00346.x | DOI Listing |
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