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Effects of a streptococcal lipoteichoic acid on complement activation in vitro
Author(s) -
Monefeldt Kari,
Tollefsen Tore
Publication year - 1993
Publication title -
journal of clinical periodontology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.456
H-Index - 151
eISSN - 1600-051X
pISSN - 0303-6979
DOI - 10.1111/j.1600-051x.1993.tb00342.x
Subject(s) - lipoteichoic acid , alternative complement pathway , lipopolysaccharide , in vitro , chemistry , complement system , microbiology and biotechnology , complement factor b , activator (genetics) , bacteria , immunology , biochemistry , antibody , biology , staphylococcus aureus , receptor , genetics
This study describes activation of serum complement by lipoteichoic acid (LTA) from Streptococcus mutans OMZ 176, while in solution. Serum from 16 healthy students was taken. Test samples were incubated with increasing doses (1–5,000 μg/ml) of LTA or lipopolysaccharide (LPS) from Escherichia coli 0111:B4 for 1 h at 37°C; then assayed for degradation of C3, C4 or factor B by crossed immunoelectrophoresis. Each preparation caused a significant ( p <0.05) dose‐dependent conversion of C3. The response curves obtained were not statistically different. LPS was a stronger activator of the alternative pathway than LTA, as judged from analysis of C3 degradation in the presence of Mg 2+ /EGTA, and from their effects on factor B cleavage. LTA caused, however, pronounced alterations in the shape of C4 precipitations in the gels. Functional (hemolytic) assays showed that, when tested at 200 μg/ml, LTA and LPS triggered significant ( p <0.05) consumptions of both classical and alternative pathway proteins. LPS was a significantly ( p <0.05) stronger activator than LTA. Apparently, the C3 degradation found for this LTA involved the alternative pathway to a small extent; thus some other mechanism of fluid‐phase C3 cleavage seemed also to be operative.