title: Identification of a point mutation resulting in loss of cell wall anchoring activity of SrtA of Streptococcus mutans NG5.
abstract: Streptococcus mutans NG5 failed to anchor antigen P1 to the cell surface, and such a failure could be attributed to a defective SrtA, which was made defective by a point mutation within the srtA gene. Without a functional SrtA, S. mutans NG5 was not able to perform a number of cell surface-related activities, including saliva-mediated adherence and aggregation.
authors.affiliation: Department of Applied Oral Sciences, Faculty of Dentistry, Dalhousie University, Halifax, Nova Scotia, Canada B3H 3J5. Song.Lee@dal.ca
authors.forename: Song F
authors.initials: SF
authors.lastname: Lee
authors.forename: Mary K H
authors.initials: MK
authors.lastname: McGavin
mesh_terms: D000373:Agglutinins / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry; D019881:Aminoacyltransferases / Q000172:deficiency / Q000235:genetics* / Q000378:metabolism; D001422:Bacterial Adhesion / Q000502:physiology; D001426:Bacterial Proteins; D002473:Cell Wall / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003546:Cysteine Endopeptidases; D010457:Peptidoglycan / Q000737:chemistry; D017354:Point Mutation; D012463:Saliva / Q000378:metabolism; D013295:Streptococcus mutans / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
chemical_list: D000373:Agglutinins; D000596:Amino Acids; D001426:Bacterial Proteins; D010457:Peptidoglycan; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases