Gene disruption identifies a 290 kDa cell-surface polypeptide conferring hydrophobicity and coaggregation properties in Streptococcus gordonii.
The C-terminal coding region of the gene (denoted cshA) encoding a high-molecular-mass (290 kDa) cell-surface polypeptide in the oral bacterium Streptococcus gordonii was cloned and sequenced. Insertion of ermAM into the S. gordonii chromosome at the 3' end of the coding region of cshA led to the production of isogenic mutants that secreted a truncated form (260 kDa) of the CshA polypeptide into the growth medium. Mutants had reduced cell-surface hydrophobicity and were impaired in their ability to coaggregate with oral actinomyces. The results identify a carboxyl terminus-anchored cell-surface protein determinant of hydrophobicity and coaggregation in S. gordonii.
McNab
R
R
Department of Oral Biology and Oral Pathology, University of Otago, Dunedin, New Zealand.
Jenkinson
H F
HF
D000190:Actinomyces / Q000502:physiology; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004352:Drug Resistance, Microbial; D004917:Erythromycin / Q000494:pharmacology; D005798:Genes, Bacterial / Q000235:genetics; D005819:Genetic Markers; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D009055:Mouth / Q000382:microbiology; D016254:Mutagenesis, Insertional; D013291:Streptococcus / Q000235:genetics* / Q000648:ultrastructure; D013499:Surface Properties
D001426:Bacterial Proteins; C079041:CshA protein, Streptococcus gordonii; D005819:Genetic Markers; D008565:Membrane Proteins; D004917:Erythromycin