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Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada
The GTPase superfamily includes a diversity of molecules whose
functions are regulated through the binding and hydrolysis of GTP. This
superfamily can be segregated into families of functionally related
molecules that typically share amino acid sequence similarity within
and around the nucleotide-binding domains. A new family of putative
GTPases, including IRG-47, LRG-47, IGTP, and TGTP/Mg21, has recently
emerged that share significant sequence identity (25–40%). Expression
of these molecules has been shown to be selectively induced by IFN-
and in some cases by IFN-
ß or bacterial LPS. This induction
pattern implicates these putative GTPases as part of the innate defense
of cells to infection, but their role in such defense has not yet been
defined. We have previously described the cloning of TGTP and now
confirm its intrinsic activity as a GTPase. We found that TGTP is
strongly induced by endogenous IFN-ß produced in response to
standard lipofection of plasmid DNA or polyinosinic polycytidilic acid.
The ability of endogenously produced IFN-ß to efficiently induce
expression of TGTP under these conditions suggested that TGTP might
participate in defense against viral infection. This proposal was borne
out when TGTP-transfected L cells displayed relative resistance to
plaque formation by vesicular stomatitis virus but not herpes simplex
virus. This observation places TGTP among a small family of innate
antiviral agents and has implications for the functions of other
members of this family of GTPases.
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