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. 2000 Jul;38(7):2760-2.
doi: 10.1128/JCM.38.7.2760-2762.2000.

Immunoglobulin A1 protease activity in Gemella haemolysans

J A Lomholt  1 , M Kilian
Affiliations

Immunoglobulin A1 protease activity in Gemella haemolysans

J A Lomholt et al. J Clin Microbiol. 2000 Jul.

Abstract

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 Pro(227)-Thr(228) peptide bond in the hinge region of the alpha1 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. VSports手机版.

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FIG. 1
FIG. 1
SDS-polyacrylamide gel electrophoresis of human IgA1 and IgA2 myeloma proteins before and after incubation for 24 h with G. haemolysans or reference IgA1 proteases. Lane 1, molecular weight standards (in thousands); lane 2, intact IgA1 control; lane 3, IgA1 incubated with G. haemolysans cells; lane 4, PBS incubated with G. haemolysans cells; lane 5, IgA1 incubated with S. pneumoniae cells; lane 6, PBS incubated with S. pneumoniae cells; lane 7, IgA1 incubated with S. sanguis cells; lane 8, IgA1 incubated with cleavage type 1 IgA1 protease from H. influenzae HK393; lane 9, IgA1 incubated with cleavage type 2 IgA1 protease from H. influenzae HK224; lane 10, IgA1 incubated with G. haemolysans cells in the presence of 100 mM EDTA; lane 11, IgA1 incubated with S. pneumoniae cells in the presence of 100 mM EDTA; lane 12, IgA2 incubated with G. haemolysans cells; lane 13, IgA2 incubated with S. pneumoniae cells and 100 mM EDTA; lane 14, intact IgA2; lane 15, molecular weight standards. Lane 3 demonstrates that G. haemolysans cleaves IgA1 to yield Fc and Fd fragments identical in size to those released by S. sanguis (lane 7) and distinct from those released by S. pneumoniae (lane 5) and the two cleavage types of H. influenzae (lanes 8 and 9). Note that Fd fragments released by the protease activity of G. haemolysans and S. sanguis are close to the size of IgA1 light chains (L chain). The activity is inhibited by EDTA (lane 10). The distinct size of Fc fragments released from IgA1 by S. pneumoniae (lane 5), although cleaving the same peptide bond as S. sanguis, is due to glycosidase activities releasing carbohydrate side chains of the heavy chain (8). None of the bacteria cleave IgA2 (lanes 12 and 13).
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