Expression of intimin γ from enterohemorrhagic Escherichia coli in Citrobacter rodentium

Elizabeth Louise Hartland, Veronika Huter, Lisa M Higgins, Nathalie S Goncalves, Gordon Dougan, Alan D Phillips, Thomas T MacDonald, Gad M Frankel

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24 Citations (Scopus)


The carboxy-terminal 280 amino acids (Int280) of the bacterial adhesion molecule intimin include the receptor-binding domain. At least five different types of Int280, designated α, β, γ, δ, and ε, have been described based on sequence variation in this region. Importantly, the intimin types are associated with different evolutionary branches and contribute to distinct tissue tropism of intimin-positive bacterial pathogens. In this study we engineered a strain of Citrobacter rodentium, which normally displays intimin β, to express intimin γ from enterohemorrhagic Escherichia coli. We show that intimin γ binds to the translocated intimin receptor (Tir) from C. rodentium and has the ability to produce attaching and effacing lesions on HEp-2 cells. However, C. rodentium expressing intimin γ could not colonize orally infected mice or induce mouse colonic hyperplasia. These results suggest that intimin may contribute to host specificity, possibly through its interaction with a receptor on the host cell surface.

Original languageEnglish
Pages (from-to)4637-4646
Number of pages10
JournalInfection and Immunity
Issue number8
Publication statusPublished - 12 Aug 2000
Externally publishedYes

Cite this

Hartland, E. L., Huter, V., Higgins, L. M., Goncalves, N. S., Dougan, G., Phillips, A. D., MacDonald, T. T., & Frankel, G. M. (2000). Expression of intimin γ from enterohemorrhagic Escherichia coli in Citrobacter rodentium. Infection and Immunity, 68(8), 4637-4646.