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Journal of Virology, January 2006, p. 306-313, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.306-313.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Characterization of the Vaccinia Virus A35R Protein and Its Role in Virulence

Rachel L. Roper*

East Carolina University, Brody Medical School, Microbiology & Immunology Department, Greenville, North Carolina 27834

Received 23 June 2005/ Accepted 4 October 2005

The vaccinia virus A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. Western blotting with anti-A35R peptide antibodies indicated that the protein is expressed early in infection and resolved as a single sharp band of ~23 kDa, slightly higher than the 20 kDa predicted from its sequence. The protein band appeared to be the same molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whether expressed in an in vitro transcription/translation system without microsomes or expressed in infected cells, suggesting that it was not glycosylated. A mutant virus with the A35R gene deleted (vA35{Delta}) formed wild-type-sized plaques on all cell lines tested (human, monkey, mouse, and rabbit); thus, A35R is not required for replication and does not appear to be a host range gene. Although the A35R protein is hydrophobic, it is unlikely to be an integral membrane protein, as it partitioned to the aqueous phase during TX-114 partitioning. The protein could not be detected in virus-infected cell supernatants. A35R localized intracellularly to the virus factories, where the first stages of morphogenesis occur. The vA35{Delta} mutant formed near-normal levels of the various morphogenic stages of infectious virus particles and supported normal acid-induced fusion of virus-infected cells. Despite normal growth and morphogenesis in vitro, the vA35{Delta} mutant virus was attenuated in intranasal challenge of mice compared to wild-type and A35R rescue virus. Thus, the intracellular A35R protein plays a role in virulence. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence mechanism.

* Mailing address: East Carolina University, Brody School of Medicine, 600 Moye Blvd., 5E106A, Department of Microbiology & Immunology, Greenville, NC 27834. Phone: (252) 744-2708. Fax: (252) 744-3104. E-mail: roperr{at}ecu.edu.

Journal of Virology, January 2006, p. 306-313, Vol. 80, No. 1
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.1.306-313.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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