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Titolo:
The surface coat of procyclic Trypanosoma brucei: Programmed expression and proteolytic cleavage of procyclin in the tsetse fly
Autore:
Acosta-Serrano, A; Vassella, E; Liniger, M; Renggli, CK; Brun, R; Roditi, I; 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 Univ Bern, Inst Zellbiol, CH-3012 Bern, Switzerland Univ Bern Bern Switzerland CH-3012 t Zellbiol, CH-3012 Bern, Switzerland Swiss Trop Inst, CH-4002 Basel, Switzerland Swiss Trop Inst Basel Switzerland CH-4002 st, CH-4002 Basel, Switzerland
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 4, volume: 98, anno: 2001,
pagine: 1513 - 1518
SICI:
0027-8424(20010213)98:4<1513:TSCOPT>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLOOD-STREAM FORMS; AFRICAN TRYPANOSOMES; REPETITIVE PROTEIN; STRUCTURAL CHARACTERIZATION; CULTURE FORMS; DIFFERENTIATION; INVITRO; ANTIGEN; GENE; TRANSFORMATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
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., "The surface coat of procyclic Trypanosoma brucei: Programmed expression and proteolytic cleavage of procyclin in the tsetse fly", P NAS US, 98(4), 2001, pp. 1513-1518

Abstract

Trypanosoma brucei, the protozoan parasite causing sleeping sickness, is transmitted by a tsetse fly vector. When the tsetse takes a blood meal from an infected human, it ingests bloodstream form trypanosomes that quickly differentiate into procyclic forms within the fly's midgut, During this process, the parasite loses the 10(7) molecules of variant surface glycoprotein that formed its surface coat, and it develops a new coat composed of several million procyclin molecules. Procyclins, the products of a small multigene family, are glycosyl phosphatidylinositol-anchored proteins containing characteristic amino acid repeats at the C terminus [either EP (EP procyclin,a form of procyclin rich in Glu-Pro repeats) or GPEET (GPEET procyclin, a form of procyclin rich in Glu-Pro-Glu-Glu-Thr repeats)], We have used a sensitive and accurate mass spectrometry method to analyze the appearance of different procyclins during the establishment of midgut infections in tsetseflies. We found that different procyclin gene products are expressed in anorderly manner. Early in the infection (day 3), GPEET2 is the only procyclin detected. By day 7, however, GPEET1 disappears and is replaced by several isoforms of glycosylated EP, but not the unglycosylated isoform EP2. Unexpectedly, we discovered that the N-terminal domains of all procyclins are quantitatively removed by proteolysis in the fly, but not in culture. These findings suggest that one function of the protease-resistant C-terminal domain, containing the amino acid repeats, is to protect the parasite surface from digestive enzymes in the tsetse fly gut.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 23:44:25