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Vol. 14, Issue 4, 1308-1318, April 2003
and
*Institut für Zellbiologie, Universität Bern,
CH-3012 Bern, Switzerland; Procyclins are abundant, glycosylphosphatidylinositol
(GPI)-anchored proteins on the surface of procyclic (insect) form
trypanosomes. To investigate whether trypanosomes are able to survive
without a procyclin coat, all four procyclin genes were deleted
sequentially. Bloodstream forms of the null mutant exhibited no
detectable phenotype and were able to differentiate to procyclic forms.
Initially, differentiated null mutant cells were barely able to grow,
but after an adaptation period of 2 mo in culture they proliferated at
the same rate as wild-type trypanosomes. Analysis of these culture-adapted null mutants revealed that they were covered by free
GPIs. These were closely related to the mature procyclin anchor in
structure and were expressed on the surface in numbers comparable with
that of procyclin in wild-type cells. However, free GPIs were smaller
than the procyclin anchor, indicative of a lower number of
poly-N-acetyllactosamine repeats, and a proportion contained diacylphosphatidic acid. Free GPIs are also expressed by
wild-type cells, although to a lesser extent. These have been overlooked in the past because they partition in a solvent fraction (chloroform/water/methanol) that is normally discarded when
GPI-anchored proteins are purified.
Institut für
Biochemie und Molekularbiologie, CH-3012 Bern, Switzerland; and
Department Biologie I, Genetik,
Ludwig-Maximilians-Universität, 80368 München, Germany
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