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Journal of Virology, February 2006, p. 1700-1709, Vol. 80, No. 4
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.4.1700-1709.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Function of Small Hydrophobic Proteins of Paramyxovirus

Rebecca L. Wilson,1 Sandra M. Fuentes,2 Ping Wang,3 Erica C. Taddeo,1 Alicia Klatt,2 Andrew J. Henderson,1,2,3,4,5 and Biao He1,2,3,4,5*

Department of Veterinary and Biomedical Sciences,1 Graduate Program in Pathobiology,2 Intercollege Graduate Program in Genetics,3 Integrated Biosciences Graduate Program, The Huck Institutes of Life Sciences,4 Center of Molecular Immunology and Infectious Disease, Pennsylvania State University, University Park, Pennsylvania 168025

Received 22 July 2005/ Accepted 15 November 2005

Mumps virus (MuV), a rubulavirus of the paramyxovirus family, causes acute infections in humans. MuV has seven genes including a small hydrophobic (SH) gene, which encodes a type I membrane protein of 57 amino acid residues. The function of the SH protein is not clear, although its expression is not necessary for growth of MuV in tissue culture cells. It is speculated that MuV SH plays a role in viral pathogenesis. Simian virus 5 (SV5), a closely related rubulavirus, encodes a 44-amino-acid-residue SH protein. Recombinant SV5 lacking the SH gene (rSV5{Delta}SH) is viable and has no growth defect in tissue culture cells. However, rSV5{Delta}SH induces apoptosis in tissue culture cells and is attenuated in vivo. Neutralizing antibodies against tumor necrosis factor alpha (TNF-{alpha}) and TNF-{alpha} receptor 1 block rSV5{Delta}SH-induced apoptosis, suggesting that SV5 SH plays an essential role in blocking the TNF-{alpha}-mediated apoptosis pathway. Because MuV is closely related to SV5, we hypothesize that the SH protein of MuV has a function similar to that of SV5, even though there is no sequence homology between them. To test this hypothesis and to study the function of MuV SH, we have replaced the open reading frame (ORF) of SV5 SH with the ORF of MuV SH in a SV5 genome background. The recombinant SV5 (rSV5{Delta}SH+MuV-SH) was analyzed in comparison with SV5. It was found that rSV5{Delta}SH+MuV-SH was viable and behaved like wild-type SV5, suggesting that MuV SH has a function similar to that of SV5 SH. Furthermore, both ectopically expressed SV5 SH and MuV SH blocked activation of NF-{kappa}B by TNF-{alpha} in a reporter gene assay, suggesting that both SH proteins can inhibit TNF-{alpha} signaling.

* Corresponding author. Mailing address: Center of Molecular Immunology and Infectious Disease, Department of Veterinary and Biomedical Sciences, Pennsylvania State University, 115 Henning Bldg., University Park, PA 16802. Phone: (814) 863-8533. Fax: (814) 863-6140. E-mail: bxh40{at}psu.edu.

Journal of Virology, February 2006, p. 1700-1709, Vol. 80, No. 4
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.4.1700-1709.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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