1887

Abstract

SUMMARY

Virions prepared from a non-revertible temperature-sensitive () mutant (53) of Newcastle disease virus (NDV) grown at the permissive temperature (34 °C) possessed thermolabile haemagglutination and neuraminidase activities compared with parental ( ) virions. Purified haemagglutinin—neuraminidase (HN) protein from 53 virions was also more thermolabile than HN protein. SDS-PAGE analysis of [H]leucine pulse- and pulse/chase-labelled NDV proteins synthesized in chick embryo fibroblasts following infection with and 53 virus revealed that 53 matrix (M) protein was unstable and disappeared during chase incubations only at the non-permissive temperature (42 °C). The non-revertibility of the 53 mutant may indicate that it is a double mutant affected in both HN and M genes; alternatively this mutant may only be affected in the HN gene, the close physical association of the thermolabile HN with the M protein during virus maturation resulting in the lack of protection of the M protein from the action of cellular proteases at the non-permissive temperature.

Keyword(s): HN , M , maturation , NDV and ts mutants
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/content/journal/jgv/10.1099/0022-1317-64-12-2781
1983-12-01
2022-10-07
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