Journal article

Function of the small hydrophobic protein of J paramyxovirus

Z Li, J Xu, J Patel, S Fuentes, Y Lin, D Anderson, K Sakamoto, LF Wang, B He

Journal of Virology | AMER SOC MICROBIOLOGY | Published : 2011

Abstract

At 18,954 nucleotides, the J paramyxovirus (JPV) genome is one of the largest in the family Paramyxoviridae, consisting of eight genes in the order 3′-N-P/V/C-M-F-SH-TM-G-L-5′. To study the function of novel paramyxovirus genes in JPV, a plasmid containing a full-length cDNA clone of the genome of JPV was constructed. In this study, the function of the small hydrophobic (SH) protein of JPV was examined by generating a recombinant JPV lacking the coding sequence of the SH protein (rJPVΔSH). rJPVΔSH was viable and had no growth defect in tissue culture cells. However, more tumor necrosis factor alpha (TNF-α) was produced during rJPVΔSH infection, suggesting that SH plays a role in inhibiting T..

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University of Melbourne Researchers

Grants

Awarded by National Institute of Allergy and Infectious Diseases


Funding Acknowledgements

The work was supported by grants from the National Institute of Allergy and Infectious Diseases and Georgia Research Alliance to B. H. (grant numbers AI070847 and K02 AI65795).