Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen.
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.
Ge
Jingping
J
Department of Pathology and Laboratory Medicine, School of Medicine, Indiana University, Indianapolis, USA.
Catt
Diana M
DM
Gregory
Richard L
RL
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*
C083238:MUC7 protein, human; D009077:Mucins; D012471:Salivary Proteins and Peptides; D010958:Plasminogen; D010751:Phosphopyruvate Hydratase