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PMID: 3312162 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Role of phenylalanine 150 in the receptor-binding domain of the K88 fibrillar subunit.

Journal of bacteriology ·Vol. 169 ·No. 11 ·1987-11-00 ·Pages 4907-11

Jacobs AA, Roosendaal B, van Breemen JF, de Graaf FK

Abstract

Recently, we reported the isolation of three peptides, Ile-83-Ala-Phe-85, Ser-148-Leu-Phe-150, and Ala-156-Ile-Phe-158, derived from the K88 fibrillar subunit and found to inhibit the binding of K88 fibrillae to cavia erythrocytes or pig intestinal epithelial cells (A. A. C. Jacobs, J. Venema, R. Leeven, H. van Pelt-Heerschap, and F. K. de Graaf, J. Bacteriol. 169:735-741, 1987). The gene encoding the K88 fibrillar adhesin was modified by oligonucleotide-directed site-specific mutagenesis such that each of the phenylalanine residues at positions 85, 150, and 158 were replaced by serine. Replacement of phenylalanine 85 or 158 had no apparent effect on the biosynthesis of the fibrillae or on their adhesive capacity. In contrast, substitution of phenylalanine 150 with serine resulted in a dramatic decrease in adhesive capacity of the K88 fibrillae. Apparently, phenylalanine 150 plays an essential role in the interaction of the adhesin with receptor molecules present on eucaryotic cells.

MeSH Terms
Animals Antigens, Bacterial Antigens, Surface/genetics,isolation & purification,metabolism Bacterial Adhesion Binding Sites Escherichia coli/genetics,metabolism Escherichia coli Proteins Fimbriae Proteins Hemagglutination Molecular Weight Mutation Phenylalanine Plasmids Protein Binding
Chemicals
Antigens, Bacterial Antigens, Surface Escherichia coli Proteins K88 antigen, E coli Fimbriae Proteins Phenylalanine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Jacobs A A
Department of Microbiology, Vrije Universiteit, Amsterdam, The Netherlands.
Roosendaal B
van Breemen J F
de Graaf F K
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.169.11.4907-4911.1987
Published
1987-11-00
Pages
4907-11
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC213884
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.169.11.4907-4911.1987 PMC Full Text View journal details
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