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

Jingping Ge, Diana M. Catt, Richard L. Gregory

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

Matrix-assisted laser desorption ionization-time of flight mass spectrometry analysis identified enolase as a cell surface component of Streptococcus mutons, 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.

Original languageEnglish (US)
Pages (from-to)6748-6752
Number of pages5
JournalInfection and immunity
Volume72
Issue number11
DOIs
StatePublished - Nov 2004

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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