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* Department of Biochemistry, Cambridge University, Cambridge CB2 1QW, United Kingdom; In the mammalian host, the cell surface of
Trypanosoma brucei is protected by a variant surface
glycoprotein that is anchored in the plasma membrane
through covalent attachment of the COOH terminus to
a glycosylphosphatidylinositol. The trypanosome also contains a phospholipase C (GPI-PLC) that cleaves this
anchor and could thus potentially enable the trypanosome to shed the surface coat of VSG. Indeed, release
of the surface VSG can be observed within a few minutes on lysis of trypanosomes in vitro. To investigate
whether the ability to cleave the membrane anchor of
the VSG is an essential function of the enzyme in vivo,
a GPI-PLC null mutant trypanosome has been generated by targeted gene deletion. The mutant trypanosomes are fully viable; they can go through an entire
life cycle and maintain a persistent infection in mice. Thus the GPI-PLC is not an essential activity and is not
necessary for antigenic variation. However, mice infected with the mutant trypanosomes have a reduced
parasitemia and survive longer than those infected with
control trypanosomes. This phenotype is partially alleviated when the null mutant is modified to express low
levels of GPI-PLC.
Laboratory of Molecular
Parasitology, University of Brussels, 1460 Rhode St Genese, Belgium; § Laboratory of Entomology, Institute for Tropical
Medicine, B2000 Antwerpen, Belgium; and Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G11
6NU, Scotland
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