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Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen
Jingping Ge1, Diana M Catt, Richard L Gregory
1Department of Pathology and Laboratory Medicine, School of Medicine, Indiana University, Indianapolis, USA.
Infection and Immunity
|October 27, 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.