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A more recent version of this article appeared on April 1, 2003
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Submitted on October 30, 2002
Revised on November 22, 2002
Accepted on December 4, 2002
1 Institut für Zellbiologie, Universität Bern, Baltzerstrasse 4, CH-3012 Bern, Switzerland
2 Institut für Biochemie und Molekularbiologie, Bühlstrasse 28, CH-3012 Bern, Switzerland
3 Department Biologie I, Genetik, Ludwig-Maximilians-Universität, Maria-Ward-Str. 1a, 80368 München, Germany
* Corresponding author. E-mail address: isabel.roditi{at}izb.unibe.ch.
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 two months in culture they proliferated at the same rate as wild type trypanosomes. Analysis of these culture-adaptated 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 to 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 as they partition in a solvent fraction (chloroform/water/methanol) that is normally discarded when GPI-anchored proteins are purified.
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