Affiliation:
1. Department of General Microbiology, University of Helsinki, SF-00280 Helsinki 28, Finland
2. Department of Medical Biochemistry, University of Göteborg, S-413 46 Göteborg, Sweden
3. Department of Clinical Immunology, University of Göteborg, S-413 46 Göteborg, Sweden
Abstract
The binding to mammalian cells of piliated enteric bacteria and the inhibition of the binding by antibodies to purified pili were studied. The target cells were epithelial cells from human bucca and human and rat urinary tracts, erythrocytes from various species, and
Saccharomyces cerevisiae
cells. The strains were selected to represent the two main agglutination patterns of enteric bacteria: mannose-resistant agglutination of human and other erythrocytes and mannose-sensitive agglutination of guinea pig and other erythrocytes.
Escherichia coli
3669 caused only mannose-resistant agglutination,
E. coli
6013 caused only mannose-sensitive agglutination, and
E. coli
3048 caused both types of agglutination simultaneously.
Salmonella typhimurium
SH6749 exhibited only mannose-sensitive hemagglutination and was included to allow comparison of its pili with those of
E. coli
strains. The range of epithelial cells to which the bacteria adhered was related to their agglutination patterns. All four strains attached to human buccal cells. Only
E. coli
strains 3669 and 3048, which caused mannose-resistant agglutination, adhered to human urinary tract epithelial cells, and only those strains that caused mannose-sensitive agglutination adhered to rat urinary tract epithelial cells. The binding of
S. typhimurium
SH6749, but not of the other strains with mannose-sensitive agglutination, was significantly inhibited by
d
-mannose. Globotetraosylceramide, a glycolipid present in the human urinary tract epithelium, inhibited attachment to human uroepithelial cells of the two strains with mannose-resistant hemagglutination. As tested by the enzyme-linked immunosorbent assay, cross-reactions between type 1 pili of the
E. coli
strains were strong, but those between
S. typhimurium
and
E. coli
mannose-sensitive pili were weak. The two pili that induced mannose-resistant hemagglutination on
E. coli
did not cross-react. Significant inhibition of adhesion of all four strains was obtained with the homologous anti-pilus antiserum. The binding of bacteria to mammalian cells may thus be mediated by several types of bacterial pili reacting with different receptors on mammalian cells.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Reference25 articles.
1. The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in gram negative bacteria;Brinton C. C.;Trans. N. Y. Acad. Sci.,1965
2. The function of bacterial fimbriae;Duguid J. P.;Arch. Immun. Ther. Exp.,1968
3. Antigens of the type-i fimbriae of Salmonellae and other enterobacteria;Duguid J. P.;J. Med. Microbiol.,1969
4. The fimbrial and non-fimbrial haemagglutinins of Escherichia coli;Duguid J. P.;J. Med. Microbiol.,1979
5. Enzyme-linked immunosorbent assay, ELISA. III. Quantitation of specific antibodies by enzyme-labelled anti-immunoglobulin in antigen-coated tubes;Engvall E.;J. Immunol.,1972
Cited by
85 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献