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Titolo:
Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion
Autore:
Melikyan, GB; Lin, SS; Roth, MG; Cohen, FS;
Indirizzi:
Rush Med Coll, Dept Physiol & Mol Biophys, Chicago, IL 60612 USA Rush Med Coll Chicago IL USA 60612 l & Mol Biophys, Chicago, IL 60612 USA Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75235 USA Univ Texas Dallas TX USA 75235 ed Ctr, Dept Biochem, Dallas, TX 75235 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 6, volume: 10, anno: 1999,
pagine: 1821 - 1836
SICI:
1059-1524(199906)10:6<1821:AASROT>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
VIRAL ENVELOPE PROTEIN; GPI-ANCHORED PROTEINS; CELL-CELL FUSION; CAPACITANCE MEASUREMENTS; INTRACELLULAR-TRANSPORT; SPANNING DOMAIN; SNARE COMPLEX; HOST-RANGE; GLYCOPROTEIN; HEMIFUSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Cohen, FS Rush Med Coll, Dept Physiol & Mol Biophys, Chicago, IL 60612 USARush Med Coll Chicago IL USA 60612 ophys, Chicago, IL 60612 USA
Citazione:
G.B. Melikyan et al., "Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion", MOL BIOL CE, 10(6), 1999, pp. 1821-1836

Abstract

The amino acid sequence requirements of the transmembrane (TM) domain and cytoplasmic tail (CT) of the hemagglutinin (HA) of influenza virus in membrane fusion have been investigated. Fusion properties of wild-type HA were compared with those of chimeras consisting of the ectodomain of HA and the TM domain and/or CT of polyimmunoglobulin receptor, a nonviral integral membrane protein. The presence of a CT was not required for fusion. But when a TM domain and CT were present, fusion activity was greater when they were derived from the same protein than derived from different proteins. In fact,the chimera with a TM domain of HA and truncated CT of polyimmunoglobulin receptor did not support full fusion, indicating that the two regions are not functionally independent. Despite the fact that there is wide latitude in the sequence of the TM domain that supports fusion, a point mutation of asemiconserved residue within the TM domain of HA inhibited fusion. The ability of a foreign TM domain to support fusion contradicts the hypothesis that a pore is composed solely of fusion proteins and supports the theory that the TM domain creates fusion pores after a stage of hemifusion has been achieved.

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Documento generato il 09/07/20 alle ore 20:53:23