Protein glycosylation mutants of procyclic Trypanosoma brucei: Defects in the asparagine-glycosglation pathway

Kuo Yuan Hwa, Alvaro Acosta-Serrano, Kay Hooi Khoo, Terry W. Pearson, Paul T. Englund

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


We employed a genetic approach to study protein glycosylation in the procyclic form of the parasite Trypanosoma brucei. Two different mutant parasites, ConA 1-1 and ConA 4-1, were isolated from mutagenized cultures by selecting cells which resisted killing or agglutination by concanavalin A. Both mutant cells show reduced concanavalin A binding. However, the mutants have different phenotypes, as indicated by the fact that ConA 1-1 binds to wheat germ agglutinin but ConA 4-1 and wild type do not. A blot probed with concanavalin A revealed that many proteins in both mutants lost the ability to bind this lectin, and the blots resembled one of wild type membrane proteins treated with PNGase F. This finding suggested that the mutants had altered asparagine-linked glycosylation. This conclusion was confirmed by studies on a flagellar protein (Fla1) and procyclic acidic repetitive protein (PARP). Structural analysis indicated that the N-glycan of wild type PARP is exclusively Man5GlcNAc2 whereas that in both mutants is predominantly a hybrid type with a terminal N-acetyllactosamine. The occupancy of the PARP glycosylation site in ConA 4-1 was much lower than that in ConA 1-1. These mutants will be useful for studying trypanosome glycosylation mechanisms and function.

Original languageEnglish (US)
Pages (from-to)181-190
Number of pages10
Issue number2
StatePublished - Feb 1999
Externally publishedYes


  • Concanavalin A
  • Glycoprotein
  • Glycosylation mutant
  • Trypanosoma brucei

ASJC Scopus subject areas

  • Biochemistry


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