Demonstration of human immunoglobulin G Fc-binding activity in oral bacteria.
AUTOR(ES)
Grenier, D
RESUMO
Nonimmune binding of immunoglobulins via the Fc fragment may reduce opsonization and phagocytosis of bacteria and is thus considered a virulence factor. The aim of this study was to investigate a wide range of oral bacterial strains for the presence of human immunoglobulin G (IgG) Fc-binding activity. A total of 132 strains representing 40 different gram-positive and gram negative bacterial species were tested for IgG Fc-binding activity by using a fast and simple dot blot procedure with horseradish peroxidase-conjugated Fc fragments from human IgG. Neither the human nor animal biotype of Porphyromonas gingivalis possessed IgG Fc-binding activity. The strongest positive reaction of gram-negative species with the IgG Fc fragments were obtained with strains of Prevotella intermedia and Fusobacterium nucleatum. Among the gram-positive bacteria tested, Peptostreptococcus micros, Lactobacillus spp., and several species of streptococci possessed IgG Fc-binding activity. In the present investigation, the ability of several oral bacterial species to bind IgG Fc fragments was demonstrated. This factor represents a potential virulence determinant as it may help pathogenic oral bacteria escape host defense mechanisms.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=368238Documentos Relacionados
- Characterization of the human immunoglobulin G Fc-binding activity in Prevotella intermedia.
- Human Cytomegalovirus Open Reading Frame TRL11/IRL11 Encodes an Immunoglobulin G Fc-Binding Protein
- Membrane proteins specified by herpes simplex viruses. V. Identification of an Fc-binding glycoprotein.
- Glycoprotein gE of herpes simplex virus type 1: effects of anti-gE on virion infectivity and on virus-induced fc-binding receptors.
- Similarities and differences in the Fc-binding glycoprotein (gE) of herpes simplex virus types 1 and 2 and tentative mapping of the viral gene for this glycoprotein.
