Characterization of FimH adhesins expressed by Salmonella enterica serovar Gallinarum biovars Gallinarum and Pullorum: reconstitution of mannose-binding properties by single amino acid substitution.

Abstract

Recombinant FimH adhesins of type 1 fimbriae from Salmonella enterica serovar Gallinarum biovars Gallinarum and Pullorum, in contrast to those of Salmonella enterica serovar Typhimurium, did not bind to high-mannose oligosaccharides or to human colon carcinoma HT-29 cells. However, mutated FimH proteins from biovar Gallinarum and biovar Pullorum, in which the isoleucine at position 78 was replaced by the threonine found in S. enterica serovar Typhimurium, bound well to glycoproteins carrying high-mannose oligosaccharides and colon carcinoma cells. The loss of sugar-binding properties by biovar Gallinarum and biovar Pullorum FimH adhesins, which are a part of the type 1 fimbriae, is most probably the result of a single T78I mutation, as was proven by site-directed mutagenesis of FimH proteins.

• Authors: Dagmara Kisiela, Anna Sapeta, Maciej Kuczkowski, Tadeusz Stefaniak, Alina Wieliczko, Maciej Ugorski
• Journal: Infection and immunity (Infect Immun) Vol. 73 Issue 9 Pg. 6187-90 (Sep 2005) ISSN: 0019-9567 [Print] United States
• PMID: 16113346 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Adhesins, Bacterial
• adhesin, Salmonella
• Mannose

Topics

• Adhesins, Bacterial (biosynthesis, genetics)
• Amino Acid Substitution (genetics)
• Blotting, Western
• Fimbriae, Bacterial (genetics, metabolism)
• Humans
• Mannose (metabolism)
• Molecular Sequence Data
• Mutation
• Protein Binding (genetics)
• Salmonella enterica (classification, genetics, metabolism)
• Structure-Activity Relationship