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PMID: 6776228 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

IgA proteases of two distinct specificities are released by Neisseria meningitidis.

The Journal of experimental medicine ·Vol. 152 ·No. 5 ·1980-11-01 ·Pages 1442-7

Mulks MH, Plaut AG, Feldman HA, Frangione B

Abstract

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.

MeSH Terms
Amino Acid Sequence Electrophoresis, Polyacrylamide Gel Humans Immunoglobulin A/metabolism Neisseria meningitidis/enzymology Peptide Hydrolases/metabolism
Chemicals
Immunoglobulin A Peptide Hydrolases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Mulks M H
Plaut A G
Feldman H A
Frangione B
References (19)
19 references, click to expand
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
DOI
10.1084/jem.152.5.1442
Published
1980-11-01
Pages
1442-7
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2185987
Subset
IM
Grants
NIAID NIH HHS · AI14648 · United States
NIADDK NIH HHS · AM02594+ · United States
NIADDK NIH HHS · AM17194 · United States
External Links
PubMed source DOI: 10.1084/jem.152.5.1442 PMC Full Text View journal details
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