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Infection and Immunity, September 2005, p. 6187-6190, Vol. 73, No. 9
0019-9567/05/$08.00+0 doi:10.1128/IAI.73.9.6187-6190.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Department of Biochemistry, Pharmacology, and Toxicology,1 Department of Epizootiology and Veterinary Administration with Clinic,2 Department and Clinic of Obstetrics, Ruminant Diseases, and Animal Health, Faculty of Veterinary Medicine, Agricultural University of Wroclaw, 50-375 Wroclaw, Poland,3 Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, 53-114 Wroclaw, Poland4
Received 22 February 2005/ Returned for modification 4 April 2005/ Accepted 6 May 2005
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.
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