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Gene disruption identifies a 290 kDa cell‐surface polypeptide conferring hydrophobicity and coaggregation properties in Streptococcus gordonii
Author(s) -
McNab R.,
Jenkinson H. F.
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb01753.x
Subject(s) - streptococcus gordonii , biology , mutant , gene , actinomyces , bacteria , coding region , microbiology and biotechnology , biochemistry , streptococcaceae , genetics
Summary The C ‐terminal coding region of the gene (denoted csh A ) 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