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Vol. 11, Issue 4, 1183-1195, April 2000
and
*Wellcome Centre for Molecular Parasitology, University of Glasgow,
The Anderson College, Glasgow G11 6NU, Scotland, United Kingdom;
The major surface proteins of the parasitic protozoon
Leishmania mexicana are anchored to the plasma membrane
by glycosylphosphatidylinositol (GPI) anchors. We have cloned
the L. mexicana GPI8 gene that encodes the catalytic
component of the GPI:protein transamidase complex that adds GPI
anchors to nascent cell surface proteins in the endoplasmic reticulum.
Mutants lacking GPI8 (Department of Biochemistry and Molecular Biology,
University of Melbourne, Parkville, Victoria 3052, Australia; and
Division of Infection and Immunity, University of
Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom
GPI8) do not
express detectable levels of GPI-anchored proteins and accumulate two putative protein-anchor precursors. However, the synthesis and cellular levels of other non-protein-linked GPIs, including
lipophosphoglycan and a major class of free GPIs, are not affected in
the GPI8 mutant. Significantly, the
GPI8 mutant displays normal growth in liquid culture,
is capable of differentiating into replicating amastigotes within
macrophages in vitro, and is infective to mice. These data suggest that
GPI-anchored surface proteins are not essential to L.
mexicana for its entry into and survival within mammalian host
cells in vitro or in vivo and provide further support for the notion
that free GPIs are essential for parasite growth.
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