Streptococcus mutans surface α-enolase binds salivary mucin MG2 and human plasminogen

被引：79

作者：

Ge, JP

Catt, DM

Gregory, RL

机构：

[1] Indiana Univ, Sch Dent, Dept Oral Biol, Indianapolis, IN 46202 USA

[2] Indiana Univ, Sch Med, Dept Pathol & Lab Med, Indianapolis, IN 46202 USA

来源：

INFECTION AND IMMUNITY | 2004年 / 72卷 / 11期

关键词：

D O I：

10.1128/IAI.72.11.6748-6752.2004

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

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.

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页码：6748 / 6752

页数：5

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