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Infect. Immun., 11 1997, 4452-4459, Vol 65, No. 11
J Reinholdt and M Kilian
Immunoglobulin A1 (IgA1) proteases cleaving human IgA1 in the hinge region
are produced constitutively by a number of pathogens, including Haemophilus
influenzae, Neisseria meningitidis, Neisseria gonorrhoeae, and
Streptococcus pneumoniae, as well as by some members of the resident
oropharyngeal flora. Whereas IgA1 proteases have been shown to interfere
with the functions of IgA antibodies in vitro, the exact role of these
enzymes in the relationship of bacteria to a human host capable of
responding with enzyme-neutralizing antibodies is not clear. Conceivably,
the role of IgA1 proteases may depend on the quantity of IgA1 protease
generated as well as on the balance between secreted and cell-associated
forms of the enzyme. Therefore, we have compared levels of IgA1 protease
activity in cultures of 38 bacterial strains representing different genera
and species as well as strains of different pathogenic potential. Wide
variation in activity generation rate was found overall and within some
species. High activity was not an exclusive property of bacteria with
documented pathogenicity. Almost all activity of H. influenzae, N.
meningitidis, and N. gonorrhoeae strains was present in the supernatant. In
contrast, large proportions of the activity in Streptococcus, Prevotella,
and Capnocytophaga species was cell associated at early stationary phase,
suggesting that the enzyme may play the role of a surface antigen. Partial
release of cell-associated activity occurred during stationary phase.
Within some taxa, the degree of activity variation correlated with degree
of antigenic diversity of the enzyme as determined previously. This finding
may indicate that the variation observed is of biological significance.
Copyright © 1997, American Society for Microbiology
Comparative analysis of immunoglobulin A1 protease activity among bacteria representing different genera, species, and strains
Department of Oral Biology, Royal Dental College, University of Aarhus, Aarhus C, Denmark. mikrjr@svfcd.aau.dk
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