Abstract:
:The human oral bacterium Streptococcus gordonii expresses, on the cell surface, two antigenically related high-molecular-mass polypeptides denoted CshA and CshB, encoded by genes at separate chromosomal loci. The precursor form of CshA is composed of four distinct segments: (i) a 41-amino-acid residue leader peptide, (ii) N-terminal 42-878 residues, (iii) residues 879-2417 comprising 13 repeat blocks of 101 amino acid residues and three shorter blocks, and (iv) a C-terminal anchor domain similar to those present in some other Gram-positive bacterial cell-wall polypeptides. Insertional mutations within cshA reduced both cell-surface hydrophobicity and ability to adhere to oral Actinomyces naeslundii. Insertional mutations in cshB had less effect on hydrophobicity and coadherence. However, expression of both polypeptides was found to be necessary for streptococci to colonize the murine oral cavity.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
McNab R,Jenkinson HF,Loach DM,Tannock GWdoi
10.1111/j.1365-2958.1994.tb01311.xsubject
Has Abstractpub_date
1994-11-01 00:00:00pages
743-54issue
4eissn
0950-382Xissn
1365-2958journal_volume
14pub_type
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