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PMID: 1339408 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii associated with expression of cell surface lipoproteins.

Infection and immunity ·Vol. 60 ·No. 3 ·1992-03-00 ·Pages 1225-8

Jenkinson HF

Abstract

Streptococcus gordonii Challis incorporated exogenous [3H]palmitate into 13 polypeptides extractable from intact cells with sodium dodecyl sulfate. A 76-kDa surface-exposed polypeptide, implicated previously as a cell aggregation determinant, was shown to be one of these lipid-modified polypeptides. Differences in sodium dodecyl sulfate-polyacrylamide gel electrophoresis patterns of lipopolypeptides were detected with mutants of S. gordonii that were altered in adherence, aggregation, coaggregation, or hydrophobicity. Lipid-modified polypeptides, tightly associated with the cell membrane, may be involved in the expression of cell surface properties of S. gordonii important for colonization of the human oral cavity.

MeSH Terms
Amino Acid Sequence Bacterial Adhesion Bacterial Proteins/analysis Base Sequence Lipoproteins/analysis,physiology Molecular Sequence Data Mouth/microbiology Palmitic Acid Palmitic Acids/metabolism Streptococcus/chemistry,physiology
Chemicals
Bacterial Proteins Lipoproteins Palmitic Acids Palmitic Acid
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Jenkinson H F
Department of Oral Biology and Oral Pathology, University of Otago, Dunedin, New Zealand.
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.60.3.1225-1228.1992
Published
1992-03-00
Pages
1225-8
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC257617
Subset
IM
Databases
GENBANK
M63610, M63611, M63612, M63613, M63614, M63615, M63616, M63617, S56209, S85398
External Links
PubMed source DOI: 10.1128/iai.60.3.1225-1228.1992 PMC Full Text View journal details
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