Inhibition of microbial IgA proteases by human secretory IgA and serum.
Mol Immunol
; 20(9): 1039-49, 1983 Sep.
Article
em En
| MEDLINE
| ID: mdl-6417473
ABSTRACT
Microbial IgA proteases cleave human serum IgA1 immunoglobulin, but human secretory IgA is resistant to hydrolysis. We have found this resistance to be due to an inhibition of protease activity that is mediated by the Fab region of secretory IgA. The IgA proteases of the genus Neisseria are more sensitive to inhibition than is the protease of Streptococcus sanguis. There is also a serum inhibitor of Neisseria proteases that co-chromatographs with IgG. Monoclonal (myeloma) human IgG proteins and plasma protease inhibitors such as alpha-1-antitrypsin and alpha-2-macroglobulin do not inhibit. Human sera do not contain inhibitor to S. sanguis protease activity. We conclude that microbial IgA proteases are subject to inhibition by IgA in secretions and IgG in serum, and this activity is most consistent with being an anti-enzyme antibody. The insensitivity of S. sanguis IgA protease to inhibition is unexplained but provides further evidence that the IgA proteases are structurally diverse.
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Base de dados:
MEDLINE
Assunto principal:
Inibidores de Proteases
/
Streptococcus sanguis
/
Imunoglobulina A Secretora
/
Serina Endopeptidases
/
Neisseria gonorrhoeae
/
Neisseria meningitidis
Limite:
Humans
Idioma:
En
Ano de publicação:
1983
Tipo de documento:
Article