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J Biol Chem, Vol. 274, Issue 9, 5797-5809, February 26, 1999
Molecular Basis for the Enterocyte Tropism Exhibited by
Salmonella typhimurium Type 1 Fimbriae
Krishnan
Thankavel ,
Ankur H.
Shah¶,
Michael S.
Cohen ,
Teruo
Ikeda**,
Robin G.
Lorenz ,
Roy
Curtiss III¶, and
Soman N.
Abraham
From the Departments of Pathology and Microbiology,
Duke University Medical Center, Durham, North Carolina 27710, the
¶ Department of Biology, Washington University,
St. Louis, Missouri 63130, the ** Department of Veterinary
Microbiology, School of Veterinary Medicine, Azabu University,
Kanagawa 229, Japan, and the  Departments
of Pathology and Medicine, Washington University School of Medicine,
St. Louis, Missouri 63110
Salmonella typhimurium exhibits a
distinct tropism for mouse enterocytes that is linked to their
expression of type 1 fimbriae. The distinct binding traits of
Salmonella type 1 fimbriae is also reflected in their
binding to selected mannosylated proteins and in their ability to
promote secondary bacterial aggregation on enterocyte surfaces. The
determinant of binding in Salmonella type 1 fimbriae is a
35-kDa structurally distinct fimbrial subunit, FimHS,
because inactivation of fimHS abolished binding
activity in the resulting mutant without any apparent effect on
fimbrial expression. Surprisingly, when expressed in the absence of
other fimbrial components and as a translational fusion protein with MalE, FimHS failed to demonstrate any specific binding
tropism and bound equally to all cells and mannosylated proteins
tested. To determine if the binding specificity of
Salmonella type 1 fimbriae was determined by the fimbrial
shaft that is intimately associated with FimHS, we replaced
the amino-terminal half of FimHS with the corresponding
sequence from Escherichia coli FimH (FimHE) that contains the receptor binding domain of FimHE. The
resulting hybrid fimbriae bearing FimHES on a
Salmonella fimbrial shaft exhibited binding traits that
resembled that of Salmonella rather than E. coli fimbriae. Apparently, the quaternary constraints imposed by
the fimbrial shaft on the adhesin determine the distinct binding traits
of S. typhimurium type 1 fimbriae.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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