Location of the complement factor H binding site on streptococcal M6 protein
نویسندگان
چکیده
منابع مشابه
cloning, expression and purification of the factor h binding protein and its interaction with factor h
background and objective: neisseria meningitidis is a leading cause of meningitis and sepsis worldwide. the factor h binding protein (fhbp) is a key virulence factor of neisseria meningitidis that is able to selectively bind to human factor h, the key regulator of the alternative complement pathway, which it has important implications for meningococcal pathogene- sis and vaccine design. the aim...
متن کاملStreptococcal M6 protein expressed in Escherichia coli. Localization, purification, and comparison with streptococcal-derived M protein
Type 6 streptococcal M protein produced by E. coli bearing plasmid pJRS42.13 (ColiM6) accumulates in the periplasmic space of this new host. No immunoreactive M protein was found either on the surface of the organism or in the culture medium. The ColiM6 protein was purified from the periplasm and the final preparation consisted of three protein bands of apparent molecular weight 55,000, 57,000,...
متن کاملEffect of complement-protein-C3b density on the binding of complement factor H to surface-bound C3b.
Various amounts of the activation fragment C3b of the complement (C) protein C3 were coupled to Sepharose 4B by catalysis with the C3 convertase of the alternative pathway of C. The binding of radioactively labelled C proteins B and H (= factor H) to the C3b-carrying particles was assayed. It was found that the relative binding of H, but not of B, fell rapidly with decreasing densities of solid...
متن کاملWest Nile virus nonstructural protein NS1 inhibits complement activation by binding the regulatory protein factor H.
The complement system, by virtue of its dual effector and priming functions, is a major host defense against pathogens. Flavivirus nonstructural protein (NS)-1 has been speculated to have immune evasion activity, because it is a secreted glycoprotein, binds back to cell surfaces, and accumulates to high levels in the serum of infected patients. Herein, we demonstrate an immunomodulatory functio...
متن کاملThe importance of the location of antibody binding on the M6 protein for opsonization and phagocytosis of group A M6 streptococci
One of 19 mAbs against the native group A streptococcal M6 protein proved opsonic for type 6 organisms in a bactericidal assay. The opsonic and three nonopsonic antibodies were selected for isotype and complement fixation studies based on previous knowledge of their epitope site on the M6 molecule. While mAb 3B8 (IgG3), whose epitope is in the NH2-terminal hypervariable region of the molecule (...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1995
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.63.1.149-153.1995