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Titolo:
Reversible interruption of Giardia lamblia cyst wall protein transport in a novel regulated secretory pathway
Autore:
Reiner, DS; McCaffery, JM; Gillin, FD;
Indirizzi:
Univ Calif San Diego, Sch Med, Dept Pathol, Div Infect Dis, San Diego, CA 92103 USA Univ Calif San Diego San Diego CA USA 92103 Dis, San Diego, CA 92103 USA Univ Calif San Diego, Sch Med, Ctr Mol Genet, San Diego, CA 92103 USA UnivCalif San Diego San Diego CA USA 92103 enet, San Diego, CA 92103 USA Univ Calif San Diego, Sch Med, Dept Cellular & Mol Med, San Diego, CA 92103 USA Univ Calif San Diego San Diego CA USA 92103 Med, San Diego, CA 92103 USA
Titolo Testata:
CELLULAR MICROBIOLOGY
fascicolo: 7, volume: 3, anno: 2001,
pagine: 459 - 472
SICI:
1462-5814(200107)3:7<459:RIOGLC>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIELD-EMISSION SEM; ENDOPLASMIC-RETICULUM; PRIMITIVE EUKARYOTE; SURFACE PROTEIN; ANTIGENIC VARIATION; IDENTIFICATION; EXCYSTATION; EXPRESSION; INVITRO; ENCYSTATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Gillin, FD Univ Calif San Diego, Sch Med, Dept Pathol, Div Infect Dis, SanDiego, CA 92103 USA Univ Calif San Diego San Diego CA USA 92103 iego, CA 92103 USA
Citazione:
D.S. Reiner et al., "Reversible interruption of Giardia lamblia cyst wall protein transport in a novel regulated secretory pathway", CELL MICROB, 3(7), 2001, pp. 459-472

Abstract

To survive in the environment and infect a new host, Giardia lamblia secretes an extracellular cyst wall using a poorly understood pathway. The two cyst wall proteins (CWPs) form disulphide-bonded heterodimers and are exported via novel encystation-specific secretory vesicles (ESVs). Exposure of eukaryotic cells to dithiothreitol (DTT) blocks the formation of disulphide bonds in nascent proteins that accumulate in the endoplasmic reticulum (ER) and induces an unfolded protein response (UPR). Proteins that have exited the ER are not susceptible. Exposure to DTT inhibits ESV formation by > 85%. Addition of DTT to encysting cells causes rapid (t(1/2) < 10 min), reversible disappearance of ESVs, correlated with reduction of CWPs to monomers and reformation of CWP oligomers upon removal of DTT. Neither CWPs nor ESVs are affected by mercaptoethanesulphonic acid, a strong reducing agent that does not penetrate cells. DTT does not inhibit the overall protein secretorypathway, and recovery does not require new protein synthesis. We found evidence of protein disulphide isomerases in the ESV and the surface of encysting cells, in which they may catalyse initial CWP folding and recovery fromDTT. This is the first suggestion of non-CWP proteins in ESVs and of enzymes on the giardial surface. DTT treatment did not stimulate a UPR, suggesting that Giardia may have diverged before the advent of this conserved form of ER quality control.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 18:44:30