A family of stage-specific alanine-rich proteins on the surface of epimastigote forms of Trypanosoma brucei

Urwyler, Simon; Studer, Erwin; Renggli, Christina; Roditi, Isabel (2007). A family of stage-specific alanine-rich proteins on the surface of epimastigote forms of Trypanosoma brucei. Molecular microbiology, 63(1), pp. 218-28. Oxford: Blackwell Science 10.1111/j.1365-2958.2006.05492.x

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A 'two coat' model of the life cycle of Trypanosoma brucei has prevailed for more than 15 years. Metacyclic forms transmitted by infected tsetse flies and mammalian bloodstream forms are covered by variant surface glycoproteins. All other life cycle stages were believed to have a procyclin coat, until it was shown recently that epimastigote forms in tsetse salivary glands express procyclin mRNAs without translating them. As epimastigote forms cannot be cultured, a procedure was devised to compare the transcriptomes of parasites in different fly tissues. Transcripts encoding a family of glycosylphosphatidyl inositol-anchored proteins, BARPs (previously called bloodstream alanine-rich proteins), were 20-fold more abundant in salivary gland than midgut (procyclic) trypanosomes. Anti-BARP antisera reacted strongly and exclusively with salivary gland parasites and a BARP 3' flanking region directed epimastigote-specific expression of reporter genes in the fly, but inhibited expression in bloodstream and procyclic forms. In contrast to an earlier report, we could not detect BARPs in bloodstream forms. We propose that BARPs form a stage-specific coat for epimastigote forms and suggest renaming them brucei alanine-rich proteins.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Cell Biology

UniBE Contributor:

Roditi, Isabel

ISSN:

0950-382X

Publisher:

Blackwell Science

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:57

Last Modified:

06 Dec 2013 13:49

Publisher DOI:

10.1111/j.1365-2958.2006.05492.x

Web of Science ID:

000242906100019

URI:

https://boris.unibe.ch/id/eprint/24682 (FactScience: 52814)

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