title: Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen.
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.
authors.affiliation: Department of Pathology and Laboratory Medicine, School of Medicine, Indiana University, Indianapolis, USA.
authors.forename: Jingping
authors.initials: J
authors.lastname: Ge
authors.forename: Diana M
authors.initials: DM
authors.lastname: Catt
authors.forename: Richard L
authors.initials: RL
authors.lastname: Gregory
mesh_terms: D015153:Blotting, Western; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D009077:Mucins / Q000378:metabolism*; D010751:Phosphopyruvate Hydratase / Q000737:chemistry / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism*; D012471:Salivary Proteins and Peptides / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013295:Streptococcus mutans / Q000201:enzymology*
chemical_list: C083238:MUC7 protein, human; D009077:Mucins; D012471:Salivary Proteins and Peptides; D010958:Plasminogen; D010751:Phosphopyruvate Hydratase