变形链球菌表面α-烯醇化酶结合唾液粘蛋白MG2和人纤溶酶原。
Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen.
作者信息
Ge Jingping, Catt Diana M, Gregory Richard L
机构信息
Department of Pathology and Laboratory Medicine, School of Medicine, Indiana University, Indianapolis, USA.
出版信息
Infect Immun. 2004 Nov;72(11):6748-52. doi: 10.1128/IAI.72.11.6748-6752.2004.
Abstract
Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis identified enolase as a cell surface component of Streptococcus mutans, which was confirmed by enzyme-linked immunosorbent assay, Western blotting, and transmission electron microscopy. Surface enolase was demonstrated to bind to human plasminogen and salivary mucin MG2. The results suggested a role for enolase in S. mutans attachment, clearance, or breach of the bloodstream barrier.
摘要
基质辅助激光解吸电离飞行时间质谱分析确定烯醇化酶是变形链球菌的一种细胞表面成分，这通过酶联免疫吸附测定、蛋白质印迹法和透射电子显微镜得到了证实。表面烯醇化酶被证明能与人纤溶酶原和唾液粘蛋白MG2结合。结果表明烯醇化酶在变形链球菌附着、清除或突破血流屏障中发挥作用。
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