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Titolo:
Killing of Trypanosoma brucei by concanavalin A: Structural basis of resistance in glycosylation mutants
Autore:
Acosta-Serrano, A; Cole, RN; 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
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 4, volume: 304, anno: 2000,
pagine: 633 - 644
SICI:
0022-2836(200012)304:4<633:KOTBBC>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACIDIC REPETITIVE PROTEIN; PROCYCLIC CULTURE FORMS; AFRICAN TRYPANOSOMES; SURFACE PROTEIN; TRANS-SIALIDASE; EXPRESSION; IDENTIFICATION; GLYCOPROTEIN; INSECT; PARP;
Keywords:
trypanosome; procyclin; mass spectrometry; N-glycosylation; glycosyl phosphatidylinositol;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Englund, PT Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 imore, MD 21205 USA
Citazione:
A. Acosta-Serrano et al., "Killing of Trypanosoma brucei by concanavalin A: Structural basis of resistance in glycosylation mutants", J MOL BIOL, 304(4), 2000, pp. 633-644

Abstract

Concanavalin A (Con A) kills procyclic (insect) forms of Trypanosoma brucei by binding to N-glycans on EP-procyclin, a major surface glycosyl phosphatidylinositol (GPI)-anchored protein which is rich in Glu-Pro repeats. We have previously isolated and studied two procyclic mutants (ConA 1-1 and ConA 4-1) that are more resistant than wild-type (WT) to Con A killing. Although both mutants express the same altered oligosaccharides compared to WT cells, ConA 4-1 is considerably more resistant to lectin killing than is ConA1-1. Thus, we looked for other alterations to account for the differences in sensitivity. Using mass spectrometry, together with chemical and enzymatic treatments, we found that both mutants express types of EP-procyclin that are either poorly expressed or not found at all in WT cells. ConA 1-1 expresses mainly EP1-3, a novel procyclin that contains 18 EP repeats, is partially N-glycosylated, and bears hybrid-type glycans. On the other hand, ConA 4-1 cells express almost exclusively EP2-3, a navel non-glycosylated procyclin isoform with 23 EP repeats and no site for glycosylation. The predominance of EP2-3 in ConA 4-1 cells explains their high resistance to ConA killing. Thus, switching the procyclin repertoire, a process that could be relevant to parasite development in the insect vector, modulates the sensitivity of trypanosomes to cytotoxic lectins. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 21:34:52