This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hanley, J Articles by Hofmann, T Search for Related Content PubMed PubMed Citation Articles by Hanley, J Articles by Hofmann, T

 Previous Article  |  Next Article 

Infect Immun. 1985 September; 49(3): 581-586

Immunochemical characterization of P pili from invasive Escherichia coli.

ABSTRACT

P pili (or fimbriae) are present on most pyelonephritogenic Escherichia coli strains, and they mediate binding to erythrocytes and epithelial cells. To determine the antigenic diversity of P pili, we purified the pili from 14 bacteremic E. coli strains which caused mannose-resistant hemagglutination. Pilus preparations consisted of one to three bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and ranged in molecular weight from 14,000 to 19,500. There was no single band common to all the strains. An enzyme-linked immunosorbent inhibition assay detected 20 ng of pilus antigen. When four different rabbit antisera were used, only two or fewer heterologous strains could inhibit the enzyme-linked immunosorbent assay. Immunoblots yielded the same results. Protein sequences of four P pili had identical N termini. These results show that despite having identical amino-terminal sequences, P pili are antigenically heterogeneous. The receptor-binding domains which are likely to be identical in all strains must be immunorecessive.

This article has been cited by other articles:

• Arora, S. K., Dasgupta, N., Lory, S., Ramphal, R. (2000). Identification of Two Distinct Types of Flagellar Cap Proteins, FliD, in Pseudomonas aeruginosa. Infect. Immun. 68: 1474-1479 [Abstract] [Full Text]