Assembly of a chemically synthesized peptide of Escherichia coli type 1 fimbriae into fimbria-like antigenic structures.
Published
Journal Article
Escherichia coli type 1 fimbriae are composed of subunits, each of which comprises 158 amino acids. We synthesized a copy of a 13-residue peptide, located near the NH2 terminus of the fimbrial subunit, that assumed some of the properties of type 1 fimbriae. At pH 5.5 the synthetic peptide autoassembled into fibrillar structures that resembled type 1 fimbriae except that they appeared less rigid and rodlike. A quaternary structure-specific monoclonal antibody against type 1 fimbriae recognized the synthetic peptide in the assembled but not the unassembled state. Furthermore, when the synthetic peptide was injected in its fimbrial conformation into rabbits, it evoked antibodies that reacted with type 1 fimbriae isolated from E. coli.
Full Text
Duke Authors
Cited Authors
- Abraham, SN; Beachey, EH
Published Date
- June 1, 1987
Published In
Volume / Issue
- 169 / 6
Start / End Page
- 2460 - 2465
PubMed ID
- 2884209
Pubmed Central ID
- 2884209
International Standard Serial Number (ISSN)
- 0021-9193
Digital Object Identifier (DOI)
- 10.1128/jb.169.6.2460-2465.1987
Language
- eng
Conference Location
- United States