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Distribution of presumptive pathogenicity factors among beta‐hemolytic streptococci isolated from Ethiopia
Author(s) -
TEWODROS WEZENET,
KRONVALL GÖRAN
Publication year - 1993
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1993.tb00114.x
Subject(s) - microbiology and biotechnology , streptococcus pyogenes , impetigo , tonsillitis , albumin , group a , fibrinogen , nephritis , streptococcus , immunology , medicine , biology , bacteria , staphylococcus aureus , genetics
Beta‐hemolytic streptococci are known to bind several mammalian proteins, which are presumed to be important in pathogenicity. The distribution of such binding structures was examined for mouse albumin, human serum IgA, human IgG, human fibrinogen, and human plasminogen. A total of 218 group A beta‐hemolytic streptococci (GAS) were studied: 5 isolates from children with acute rheumatic fever (ARF), 18 from acute post‐streptococcal glomerulonephritis (APSGN), 57 from tonsillitis, 52 from skin infections, and 86 from healthy carriers. Sixty‐eight Streptococcus equisimilis and 20 group G streptococci were also included. Most of the S. equisimilis (60/68) and group G (14/20) were obtained from apparently healthy carriers. The results were evaluated with respect to T type, serum opacity reaction (SOR), site of isolation, and disease type. No direct correlation was detected between the protein‐binding structures studied. There was no apparent correlation between any particular protein‐binding structure and specific T type. Albumin‐binding and IgA‐binding activities were inversely correlated among skin and nephritis GAS isolates. A strong correlation was demonstrated between IgA‐binding activity and SOR production, while albumin‐binding activity correlated with SOR‐negative strains. Albumin‐binding levels in isolates from ARF, APSGN and tonsillitis were significantly higher than in isolates from healthy carriers (P< 0.001). A higher albumin‐binding capacity was shown in skin isolates from APSGN than in isolates from impetigo (P< 0.001).