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Titolo:
Critical roles of glycosylphosphatidylinositol for Trypanosoma brucei
Autore:
Nagamune, K; Nozaki, T; Maeda, Y; Ohishi, K; Fukuma, T; Hara, T; Schwarz, RT; Sutterlin, C; Brun, R; Riezman, H; Kinoshita, T;
Indirizzi:
Osaka Univ, Microbial Dis Res Inst, Dept Immunoregulat, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 regulat, Suita, Osaka 5650871, Japan Natl Inst Infect Dis, Dept Parasitol, Shinjuku Ku, Tokyo 1628640, Japan Natl Inst Infect Dis Tokyo Japan 1628640 injuku Ku, Tokyo 1628640, Japan Kurume Univ, Sch Med, Dept Parasitol, Kurume, Fukuoka 8300011, Japan Kurume Univ Kurume Fukuoka Japan 8300011 , Kurume, Fukuoka 8300011, Japan Univ Marburg, Med Ctr Hyg & Med Microbiol, D-35011 Marburg, Germany Univ Marburg Marburg Germany D-35011 Microbiol, D-35011 Marburg, Germany Univ Basel, Biozentrum, CH-4056 Basel, Switzerland Univ Basel Basel Switzerland CH-4056 zentrum, CH-4056 Basel, Switzerland Schweizer Tropeninst, CH-4002 Basel, Switzerland Schweizer Tropeninst Basel Switzerland CH-4002 H-4002 Basel, Switzerland
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 19, volume: 97, anno: 2000,
pagine: 10336 - 10341
SICI:
0027-8424(20000912)97:19<10336:CROGFT>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACIDIC REPETITIVE PROTEIN; PROCYCLIC CULTURE FORMS; GPI-ANCHOR SYNTHESIS; SURFACE GLYCOPROTEIN; DEVELOPMENTAL REGULATION; ENDOPLASMIC-RETICULUM; AFRICAN TRYPANOSOMES; MEMBRANE ANCHORS; PIG-B; BIOSYNTHESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Kinoshita, T Osaka Univ, Microbial Dis Res Inst, Dept Immunoregulat, 3-1 Yamada-oka, Suita, Osaka 5650871, Japan Osaka Univ 3-1 Yamada-oka Suita Osaka Japan 5650871 71, Japan
Citazione:
K. Nagamune et al., "Critical roles of glycosylphosphatidylinositol for Trypanosoma brucei", P NAS US, 97(19), 2000, pp. 10336-10341

Abstract

Trypanosoma brucei, the protozoan parasite responsible for sleeping sickness, evades the immune response of mammalian hosts and digestion in the gut of the insect vector by means of its coat proteins tethered to the cell surface via glycosylphosphatidyl inositol (GPI) anchors. To evaluate the importance of CPI for parasite survival, we cloned and disrupted a trypanosomal gene, TbGPI10, involved in biosynthesis of GPI. TbGPI10 encodes a protein of 558 amino acids having 25% and 23% sequence identity to human PIC-B and Saccharomyces cerevisiae Gpi10p, respectively. TbGPI10 restored biosynthesisof GPI in a mouse mutant cell line defective in mouse Pig-b gene. TbGPI10 also rescued the inviability of GPI10-disrupted S. cerevisiae, indicating that TbGPI10 is the orthologue of PIG-B/GPI10 that is involved in the transfer of the third mannose to GPI. The bloodstream form of T. brucei could notlose TbGPI10; therefore, GPI synthesis is essential for growth of mammalian stage parasites. Procyclic form cells (insect stage parasites) lacking the surface coat proteins because of disruption of TbGPI10 are viable and grow slower than normal, provided that they are cultured in nonadherent flasks. In regular flasks, they adhered to the plastic surface and died. Infectivity to tsetse flies is partially impaired, particularly in the early stage. Therefore, parasite-specific inhibition of GPI biosynthesis should be an effective chemotherapy target against African trypanosomiasis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 02:39:20