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Journal of Clinical Microbiology, July 2000, p. 2760-2762, Vol. 38, No. 7
0095-1137/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Immunoglobulin A1 Protease Activity in Gemella haemolysans

Jeanet A. Lomholt and Mogens Kilian*

Department of Medical Microbiology and Immunology, University of Aarhus, DK-8000 Aarhus C, Denmark

Received 29 February 2000/Returned for modification 31 March 2000/Accepted 25 April 2000

The purpose of this study was to determine the occurrence and nature of immunoglobulin A1 (IgA1) protease activity in members of the genus Gemella and related taxa. Among a total of 22 Gemella strains belonging to the four species Gemella haemolysans, Gemella morbillorum, Gemella sanguinis, and Gemella bergeriae and four reference strains of the species Helcococcus kunzii, Facklamia hominis, and Globicatella sanguinis, IgA1 protease activity was an exclusive character of all nine isolates of G. haemolysans. The IgA1 protease of G. haemolysans appears to be a metallo-type IgA1 protease that cleaves the Pro227-Thr228 peptide bond in the hinge region of the alpha 1 chain like that of several Streptococcus species. Phenotypic characterization of the isolates demonstrates that screening for IgA1 protease activity provides a valuable means for species differentiation in this group of bacteria.

* Corresponding author. Mailing address: Department of Medical Microbiology and Immunology, The Bartholin Building, University of Aarhus, DK-8000 Aarhus C, Denmark. Phone: 458942 1735. Fax: 458619 6128. E-mail: kilian{at}microbiology.au.dk.

Journal of Clinical Microbiology, July 2000, p. 2760-2762, Vol. 38, No. 7
0095-1137/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Takenouchi-Ohkubo, N., Mortensen, L. M., Drasbek, K. R., Kilian, M., Poulsen, K. (2006). Horizontal transfer of the immunoglobulin A1 protease gene (iga) from Streptococcus to Gemella haemolysans. Microbiology 152: 2171-2180 [Abstract] [Full Text]  


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