IgA proteases of two distinct specificities are released by Neisseria meningitidis
| Autor: | Martha H. Mulks, Blas Frangione, Harry A. Feldman, Andrew G. Plaut |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
chemistry.chemical_classification
Proteases Protease medicine.medical_treatment Neisseria meningitidis Immunology Articles Biology medicine.disease_cause Immunoglobulin A Amino acid Enzyme chemistry Biochemistry Cleave medicine Humans Immunology and Allergy Peptide bond Electrophoresis Polyacrylamide Gel Amino Acid Sequence Peptide sequence Peptide Hydrolases |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| DOI: | 10.1084/jem.152.5.1442 |
| Popis: | Strains of Neisseria meningitidis produce two distinct extracellular IgA proteases that cleave the human IgA1 heavy chain at different points within the hinge region. Type 1 protease cleaves the prolyl-seryl peptide bond at position 237-238; type type 2 protease cleaves the prolyl-threonyl bond two residues amino terminal to that bond attacked by type 1 enzyme. Each meningococcal isolate elaborates only one of these two enzymes, and the type of protease produced correlates with certain serogroups: group A yielding only type 1, and groups X and Y only type 2 enzyme. In addition, analysis of amino acid sequences of human alpha-chain proteins reveals that the repeating octapeptide characteristic of the IgA1 hinge region is actually triplicated. |
| Databáze: | OpenAIRE |
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