Lomholt J A, Kilian M
Department of Medical Microbiology and Immunology, University of Aarhus, DK-8000 Aarhus C, Denmark.
J Clin Microbiol. 2000 Jul;38(7):2760-2. doi: 10.1128/JCM.38.7.2760-2762.2000.
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 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.
本研究的目的是确定孪生球菌属及相关分类群成员中免疫球蛋白A1(IgA1)蛋白酶活性的发生情况和性质。在总共22株属于溶血孪生球菌、麻疹孪生球菌、血孪生球菌和伯氏孪生球菌这四个物种的孪生球菌菌株,以及昆氏孪生球菌、人孪生球菌和血球形菌这三个物种的四株参考菌株中,IgA1蛋白酶活性是溶血孪生球菌所有九株分离株的独有特征。溶血孪生球菌的IgA1蛋白酶似乎是一种金属型IgA1蛋白酶,它像几种链球菌属物种的蛋白酶一样,在α1链的铰链区切割Pro(227)-Thr(228)肽键。对分离株的表型特征分析表明,筛选IgA1蛋白酶活性为该组细菌的物种鉴别提供了一种有价值的方法。