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Role of Small Hydrophobic Protein of J Paramyxovirus in Virulence.
- Source :
-
Journal of virology [J Virol] 2018 Sep 26; Vol. 92 (20). Date of Electronic Publication: 2018 Sep 26 (Print Publication: 2018). - Publication Year :
- 2018
-
Abstract
- J paramyxovirus (JPV) was first isolated from moribund mice with hemorrhagic lung lesions in Australia in 1972. It is a paramyxovirus classified under the newly proposed genus Jeilongvirus JPV has a genome of 18,954 nucleotides, consisting of eight genes in the order 3'-N-P/V/C-M-F-SH-TM-G-L-5'. JPV causes little cytopathic effect (CPE) in tissue culture cells but severe disease in mice. The small hydrophobic (SH) protein is an integral membrane protein encoded by many paramyxoviruses, such as mumps virus (MuV) and respiratory syncytial virus (RSV). However, the function of SH has not been defined in a suitable animal model. In this work, the functions of SH of JPV, MuV, and RSV have been examined by generating recombinant JPV lacking the SH protein (rJPV-ΔSH) or replacing SH of JPV with MuV SH (rJPV-MuVSH) or RSV SH (rJPV-RSVSH). rJPV-ΔSH, rJPV-MuVSH, and rJPV-RSVSH were viable and had no growth defect in tissue culture cells. However, more tumor necrosis factor alpha (TNF-α) was produced during rJPV-ΔSH infection, confirming the role of SH in inhibiting TNF-α production. rJPV-ΔSH induced more apoptosis in tissue culture cells than rJPV, rJPV-MuVSH, and rJPV-RSVSH, suggesting that SH plays a role in blocking apoptosis. Furthermore, rJPV-ΔSH was attenuated in mice compared to rJPV, rJPV-MuVSH, and rJPV-RSVSH, indicating that the SH protein plays an essential role in virulence. The results indicate that the functions of MuV SH and RSV SH are similar to that of JPV SH even though they have no sequence homology. IMPORTANCE Paramyxoviruses are associated with many devastating diseases in animals and humans. J paramyxovirus (JPV) was isolated from moribund mice in Australia in 1972. Newly isolated viruses, such as Beilong virus (BeiPV) and Tailam virus (TlmPV), have genome structures similar to that of JPV. A new paramyxovirus genus, Jeilongvirus , which contains JPV, BeiPV, and TlmPV, has been proposed. Small hydrophobic (SH) protein is present in many paramyxoviruses. Our present study investigates the role of SH protein of JPV in pathogenesis in its natural host. Understanding the pathogenic mechanism of Jeilongvirus is important to control and prevent potential diseases that may emerge from this group of viruses.<br /> (Copyright © 2018 American Society for Microbiology.)
- Subjects :
- Animals
Cell Line
Chlorocebus aethiops
Disease Models, Animal
Gene Deletion
Genetic Complementation Test
Humans
Mice
Microbial Viability
Mumps virus genetics
Mumps virus physiology
Paramyxoviridae Infections virology
Respiratory Syncytial Viruses genetics
Respiratory Syncytial Viruses physiology
Retroviridae Proteins, Oncogenic genetics
Virulence
Virulence Factors genetics
Apoptosis Regulatory Proteins metabolism
Paramyxoviridae growth & development
Paramyxoviridae Infections pathology
Retroviridae Proteins, Oncogenic metabolism
Tumor Necrosis Factor-alpha antagonists & inhibitors
Virulence Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5514
- Volume :
- 92
- Issue :
- 20
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 30068647
- Full Text :
- https://doi.org/10.1128/JVI.00653-18