A Temperature-sensitive Mutant of Newcastle Disease Virus Defective in Intracellular Processing of Fusion Protein

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1990 Mar 1

PMID 2304149

Citations 2

Authors

H Matsumura

Y Futaesaku

S Kohno

A Sugiura

M Kohase

Affiliations

Soon will be listed here.

Abstract

A temperature-sensitive mutant (ts3) of Newcastle disease virus was physiologically characterized. All major viral structural proteins were synthesized at the permissive (37 degrees C) and nonpermissive (42 degrees C) temperatures, but the fusion (F) glycoprotein was not cleaved at 42 degrees C. In immunocytochemical electron microscopy, the F protein was abundant in the rough endoplasmic reticulum but not in cytoplasmic membrane at 42 degrees C. Noninfectious hemagglutinating virus particles containing all major structural proteins except the F protein were released at 42 degrees C from infected cells. We concluded that the defect in ts3 resides in the intracellular processing of the F protein.

Citing Articles

Virus maturation by budding.

Garoff H, Hewson R, Opstelten D Microbiol Mol Biol Rev. 1998; 62(4):1171-90.

PMID: 9841669 PMC: 98943. DOI: 10.1128/MMBR.62.4.1171-1190.1998.

Intracellular processing of the paramyxovirus F protein: critical role of the predicted amphipathic alpha helix adjacent to the fusion domain.

Wang C, Raghu G, Morrison T, Peeples M J Virol. 1992; 66(7):4161-9.

PMID: 1602539 PMC: 241219. DOI: 10.1128/JVI.66.7.4161-4169.1992.

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