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© The Rockefeller University Press, 0021-9525/1997//103 $5.00
The Journal of Cell Biology, Volume 139, Number 1, , 1997 103-114

Article

The GPI-Phospholipase C of Trypanosoma brucei Is Nonessential But Influences Parasitemia in Mice



Helena Webb*, Nicola Carnall*, Luc Vanhamme{ddagger}, Sylvie Rolin{ddagger}, Jakke Van Den Abbeele§, Sue Welburn||, Etienne Pays{ddagger}, and Mark Carrington*

* Department of Biochemistry, Cambridge University, Cambridge CB2 1QW, United Kingdom; {ddagger} 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

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.

Abbreviations used in this paper: CRD, cross-reacting determinant; GPI, glycosylphosphatidylinositol; mf, hydrophobic membrane form; PI, phosphatidylinositol; PLC, phospholipase C; VSG, variant surface glycoprotein.

Address all correspondence to M. Carrington, Department of Biochemistry, Tennis Court Road, Cambridge CB2 1QW, United Kingdom. Tel: (44) 1223 333 683. Fax: (44) 1223 333345. e-mail: mc115{at}mole.bio.cam.ac.uk

This work was funded by the Medical Research Council and the Wellcome Trust.


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