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Titolo:
Protein glycosylation mutants of procyclic Trypanosoma brucei: defects in the asparagine-glycosylation pathway
Autore:
Hwa, KY; Acosta-Serrano, A; Khoo, KH; Pearson, TW; Englund, PT;
Indirizzi:
Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA JohnsHopkins Univ Baltimore MD USA 21205 l Chem, Baltimore, MD 21205 USA Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan Acad Sinica Taipei Taiwan 115 Sinica, Inst Biol Chem, Taipei 115, Taiwan Univ Victoria, Dept Biochem & Microbiol, Victoria, BC V8W 3P6, Canada UnivVictoria Victoria BC Canada V8W 3P6 ol, Victoria, BC V8W 3P6, Canada
Titolo Testata:
GLYCOBIOLOGY
fascicolo: 2, volume: 9, anno: 1999,
pagine: 181 - 190
SICI:
0959-6658(199902)9:2<181:PGMOPT>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
VARIANT SURFACE GLYCOPROTEIN; ACIDIC REPETITIVE PROTEINS; CULTURE FORMS; STAGE; EXPRESSION; ANCHOR; LIPOPHOSPHOGLYCAN; IDENTIFICATION; PURIFICATION; BIOSYNTHESIS;
Keywords:
concanavalin A; glycosylation mutant; glycoprotein; Trypanosoma brucei;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Englund, PT Johns21205ins Univ, Sch Med, Dept Biol Chem, 725 N Wolfe ST, Baltimore, MD Johns Hopkins Univ 725 N Wolfe ST Baltimore MD USA 21205 e, MD
Citazione:
K.Y. Hwa et al., "Protein glycosylation mutants of procyclic Trypanosoma brucei: defects in the asparagine-glycosylation pathway", GLYCOBIOLOG, 9(2), 1999, pp. 181-190

Abstract

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 phenotype, 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 proteinstreated with PNGase F. This finding suggested that the mutants had alteredasparagine-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 Man(5)GlcNAc(2) 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 00:32:51