Modulation of IgG effector functions by a monovalent fragment of staphylococcal protein A.
Mol Immunol
; 23(4): 377-84, 1986 Apr.
Article
em En
| MEDLINE
| ID: mdl-3724757
ABSTRACT
The monovalent V-1 fragment of protein A (fSpA) with a mol. wt of 13,000 obtained from an u.v. mutant of Staphylococcus aureus Cowan I strain was proved to be able to modulate significantly some of the effector functions of IgG, such as complement fixation, catabolism, attachment to Fc receptors and antibody-dependent cell-mediated cytotoxicity. Moreover fSpA-like protein A obtained from the A676 strain is mitogenic and enhances NK activity of human peripheral lymphocytes. The efficiency of fSpA was found to be lower than that of protein A with regard to its ability to inhibit complement fixation, EA rosette formation and antibody-dependent cell-mediated cytotoxicity. Both protein A and fSpA had the same efficiency in activation of the complement system after reaction with human or guinea pig IgG, and in increasing the IgG catabolism. Unlike fSpA the monovalent B fragment of protein A (with mol. wt of 7000) was not able to inhibit EA rosette formation and antibody-dependent cell-mediated cytotoxicity. The results recommend fSpA, substituting for protein A, as a molecular probe for the investigation of IgG antibody and lymphocyte effector functions.
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Base de dados:
MEDLINE
Assunto principal:
Proteína Estafilocócica A
/
Imunoglobulina G
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
1986
Tipo de documento:
Article