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Invasive isolates of Neisseria meningitidis possess enhanced immunoglobulin A1 protease activity compared to colonizing strains

Invasive isolates of Neisseria meningitidis possess enhanced immunoglobulin A1 protease activity compared to colonizing strains
Invasive isolates of Neisseria meningitidis possess enhanced immunoglobulin A1 protease activity compared to colonizing strains

Neisseria meningitidis, Haemophilus influenzae, and Streptococcus pneumoniae possess the ability to cleave human IgA1 antibodies, and all successfully colonize and occasionally invade the human upper respiratory tract. N. meningitidis invades the bloodstream after a period of nasopharyngeal colonization. We directly compared levels of IgA1 protease activity in strains (n=52) derived from the cerebrospinal fluid or blood of patients with meningococcal disease with strains of N. meningitidis obtained from asymptomatic carriers (n=25). IgA1 protease activity was determined by a sensitive semiquantitative ELISA assay. Levels of IgA1 protease activity were significantly higher (P<0.0001) in strains associated with invasive meningococcal disease (98% with detectable activity, mean = 580 mU) than with those obtained from asymptomatic carriers (76% with detectable activity, mean = 280 mU). Despite marked variation in enzyme activity, almost all strains (96%) possessed the gene for IgA1 protease. Given the panmictic population structure of the bacterial isolates investigated, these data, obtained from two groups infected with N. meningitidis, but with markedly different clinical outcomes, provide the first quantitative evidence that IgA1 protease activity is a virulence determinant that contributes to the pathogenic phenotype, and suggest IgA1 protease as a potential target for prophylaxis.

Biomarkers, Humans, Immunoglobulin A, Meningitis, Meningococcal, Neisseria meningitidis, Serine Endopeptidases, Virulence, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
0892-6638
331-337
Vitovski, S.
5d8f8fff-cffe-44f0-b9c2-a43e269b4ee2
Read, R.C.
b5caca7b-0063-438a-b703-7ecbb6fc2b51
Sayers, J.R.
fdf8b8bf-4771-4253-a02d-69b051780cea
Vitovski, S.
5d8f8fff-cffe-44f0-b9c2-a43e269b4ee2
Read, R.C.
b5caca7b-0063-438a-b703-7ecbb6fc2b51
Sayers, J.R.
fdf8b8bf-4771-4253-a02d-69b051780cea

Vitovski, S., Read, R.C. and Sayers, J.R. (1999) Invasive isolates of Neisseria meningitidis possess enhanced immunoglobulin A1 protease activity compared to colonizing strains. The FASEB Journal, 13 (2), 331-337.

Record type: Article

Abstract

Neisseria meningitidis, Haemophilus influenzae, and Streptococcus pneumoniae possess the ability to cleave human IgA1 antibodies, and all successfully colonize and occasionally invade the human upper respiratory tract. N. meningitidis invades the bloodstream after a period of nasopharyngeal colonization. We directly compared levels of IgA1 protease activity in strains (n=52) derived from the cerebrospinal fluid or blood of patients with meningococcal disease with strains of N. meningitidis obtained from asymptomatic carriers (n=25). IgA1 protease activity was determined by a sensitive semiquantitative ELISA assay. Levels of IgA1 protease activity were significantly higher (P<0.0001) in strains associated with invasive meningococcal disease (98% with detectable activity, mean = 580 mU) than with those obtained from asymptomatic carriers (76% with detectable activity, mean = 280 mU). Despite marked variation in enzyme activity, almost all strains (96%) possessed the gene for IgA1 protease. Given the panmictic population structure of the bacterial isolates investigated, these data, obtained from two groups infected with N. meningitidis, but with markedly different clinical outcomes, provide the first quantitative evidence that IgA1 protease activity is a virulence determinant that contributes to the pathogenic phenotype, and suggest IgA1 protease as a potential target for prophylaxis.

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More information

Published date: February 1999
Keywords: Biomarkers, Humans, Immunoglobulin A, Meningitis, Meningococcal, Neisseria meningitidis, Serine Endopeptidases, Virulence, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't

Identifiers

Local EPrints ID: 416968
URI: http://eprints.soton.ac.uk/id/eprint/416968
ISSN: 0892-6638
PURE UUID: 4a328124-6051-408b-b934-398b79279e57
ORCID for R.C. Read: ORCID iD orcid.org/0000-0002-4297-6728

Catalogue record

Date deposited: 15 Jan 2018 17:31
Last modified: 10 Nov 2021 03:30

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Contributors

Author: S. Vitovski
Author: R.C. Read ORCID iD
Author: J.R. Sayers

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