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金黄色葡萄球菌中可溶性溶菌转糖基酶同源物的亚细胞定位

Subcellular location of the soluble lytic transglycosylase homologue in Staphylococcus aureus.

作者信息

Sakata Noriaki, Terakubo Shigemi, Mukai Toshiji

机构信息

Department of Legal Medicine, St. Marianna University School of Medicine, Sugao 2-16-1, Miyamae-ku, Kawasaki, 216-8511, Japan.

出版信息

Curr Microbiol. 2005 Jan;50(1):47-51. doi: 10.1007/s00284-004-4381-9. Epub 2004 Dec 8.

Abstract

The immunodominant antigen A, IsaA, of Staphylococcus aureus was found to include a putative soluble lytic transglycosylase domain in its C-terminal region. Since the presence of this distinctive domain suggested that the protein might participate in peptidoglycan turnover, as indicated in Gram-negative bacteria, its cellular location was investigated. The protein was found not only in the culture supernatant but also in the cell wall fraction. To estimate its physiological role for the bacterium, its cell surface distribution was studied by immunoelectron microscopy. Protein A-gold particles binding to the immune complex were mainly located on the septal region of the bacterial cell surface. These data suggested that IsaA might be involved in bacterial cell separation through a preferential interaction with peptidoglycan chain.

摘要

金黄色葡萄球菌的免疫显性抗原A(IsaA)在其C端区域被发现包含一个假定的可溶性溶菌转糖基酶结构域。由于这一独特结构域的存在表明该蛋白可能如革兰氏阴性菌中所示参与肽聚糖周转,因此对其细胞定位进行了研究。该蛋白不仅存在于培养上清液中,也存在于细胞壁组分中。为评估其对细菌的生理作用,通过免疫电子显微镜研究了其细胞表面分布。与免疫复合物结合的蛋白A-金颗粒主要位于细菌细胞表面的隔膜区域。这些数据表明IsaA可能通过与肽聚糖链的优先相互作用参与细菌细胞分裂。

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