Title |
The effect of the HRB linker of Newcastle disease virus fusion protein on the fusogenic activity |
Author |
Yaqing Liu1, Ying Liu2, Yanan Huang1, Hongling Wen1, Li Zhao1, Yanyan Song1, and Zhiyu Wang1* |
Address |
1Department of Virology, School of Public Health, Cheeloo College of Medicine, Shandong University, Jinan 250014, P. R. China, 2Jinan Central Hospital, Cheeloo College of Medicine, Shandong University, Jinan 250014, P. R. China |
Bibliography |
Journal of Microbiology, 59(5),513–521, 2021,
|
DOI |
10.1007/s12275-021-0539-4
|
Key Words |
Newcastle disease virus, fusion protein, mutation
analysis, fusogenic activity |
Abstract |
Newcastle disease, designated a class A disease of poultry by
the Office international des epizooties (OIE), is an acute infection
caused by Newcastle disease virus (NDV). The merging
of the envelope of NDV with the membrane of a target
host cell is the key step in the infection pathway, which is driven
by the concerted action of two glycoproteins: haemagglutinin-
neuraminidase (HN) and fusion (F) protein. When
the HN protein binds to the host cell surface receptor, the F
protein is activated to mediate fusion. The three-dimensional
structure of the F protein has been reported to have low
electron density between the DIII domain and the HRB domain,
and this electron-poor region is defined as the HRB
linker. To clarify the contributing role of the HRB linker in
the NDV F protein-mediated fusion process, 6 single amino
acid mutants were obtained by site-directed mutagenesis of
the HRB linker. The expression of the mutants and their abilities
to mediate fusion were analysed, and the key amino acids
in the HRB linker were identified as L436, E439, I450, and
S453, as they can modulate the fusion ability or expression
of the active form to a certain extent. The data shed light on
the crucial role of the F protein HRB linker in the acquisition
of a normal fusogenic phenotype. |