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PMID: 2886335 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The role of lysine-132 and arginine-136 in the receptor-binding domain of the K99 fibrillar subunit.

The EMBO journal ·Vol. 6 ·No. 6 ·1987-06-00 ·Pages 1805-8

Jacobs AA, Simons BH, de Graaf FK

Abstract

The gene encoding the K99 fibrillar adhesin of Escherichia coli has been modified by oligonucleotide-directed, site-specific, mutagenesis. The tryptophan-67, lysine-132, lysine-133 or arginine-136 were replaced by leucine, threonine, threonine and serine, respectively. The threonine-133 mutant fibrillae were indistinguishable from wild-type fibrillae. In contrast, replacement of lysine-132 or arginine-136 by threonine or serine, respectively, resulted in mutant fibrillae which had completely lost adhesive capacity, suggesting that the positive charges of these residues are essential for the interaction with the negatively charged sialic acid residue of the receptor molecules. After the replacement of tryptophan-67 with leucine neither fibrillae nor subunits were detectable, indicating that the mutant product is unstable and that tryptophan-67 has an essential structural role in the K99 subunit.

MeSH Terms
Adhesins, Escherichia coli Antigens, Surface/genetics,physiology Arginine Bacterial Adhesion Bacterial Proteins/genetics,physiology Bacterial Toxins Base Sequence Cloning, Molecular Codon Escherichia coli/genetics Genes Genes, Bacterial Lysine Mutation
Chemicals
Adhesins, Escherichia coli Antigens, Surface Bacterial Proteins Bacterial Toxins Codon K99 antigen Arginine Lysine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Jacobs A A
Simons B H
de Graaf F K
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21 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1987-06-00
Pages
1805-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC553558
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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