Effect of SpeB and EndoS from Streptococcus pyogenes on Human Immunoglobulins
AUTOR(ES)
Collin, Mattias
FONTE
American Society for Microbiology
RESUMO
Streptococcus pyogenes secretes a specific immunoglobulin G (IgG)-protease, SpeB, as well as the IgG glycan-hydrolyzing enzyme EndoS. Here we show that SpeB also degrades IgA, IgM, IgD, and IgE. We also show that EndoS only hydrolyzes the glycan moiety on native but not denatured IgG. Thus, SpeB has a broad immunoglobulin-degrading activity, while EndoS is highly specific for IgG.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=100124Documentos Relacionados
- EndoS and SpeB from Streptococcus pyogenes Inhibit Immunoglobulin-Mediated Opsonophagocytosis
- EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
- Role of RopB in Growth Phase Expression of the SpeB Cysteine Protease of Streptococcus pyogenes
- Inactivation of the streptococcal erythrogenic toxin B gene (speB) in Streptococcus pyogenes.
- Role for Serine Protease HtrA (DegP) of Streptococcus pyogenes in the Biogenesis of Virulence Factors SpeB and the Hemolysin Streptolysin S