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Journal of Virology, March 2008, p. 2150-2160, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.01969-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Vaccinia Virus A34 Glycoprotein Determines the Protein Composition of the Extracellular Virus Envelope{triangledown}

Beatriz Perdiguero ,{dagger},{ddagger} María M. Lorenzo,{dagger} and Rafael Blasco*

Departamento de Biotecnología, INIA, Ctra. La Coruña km 7.5, 28040 Madrid, Spain

Received 7 September 2007/ Accepted 3 December 2007

The outer envelope of the extracellular form of vaccinia virus contains five virus-encoded proteins, F13, A33, A34, A56, and B5, that, with the exception of A56, are implicated in virus egress or infectivity. A34, a type II transmembrane glycoprotein, is involved in the induction of actin tails, the release of enveloped virus from the surfaces of infected cells, and the disruption of the virus envelope after ligand binding prior to virus entry. To investigate interactions between A34 and other envelope proteins, a recombinant vaccinia virus (vA34RHA) expressing an epitope-tagged version of A34 (A34HA) was constructed by appending an epitope from influenza virus hemagglutinin to the C terminus of A34. Complexes of A34HA with B5 and A36, but not with A33 or F13, were detected in vA34RHA-infected cells. A series of vaccinia viruses expressing mutated versions of the B5 protein was used to investigate the domain(s) of B5 required for interaction with A34. Both the cytoplasmic and the transmembrane domains of B5 were dispensable for binding to A34. Most of the extracellular domain of B5, which contains four short consensus repeats homologous to complement control proteins, was sufficient for A34 interaction, indicating that both proteins interact through their ectodomains. Immunofluorescence experiments on cells infected with A34-deficient virus indicated that A34 is required for efficient targeting of B5, A36, and A33 into wrapped virions. Consistent with this observation, the envelope of A34-deficient virus contained normal amounts of F13 but decreased amounts of A33 and B5 with respect to the parental WR virus. These results point to A34 as a major determinant in the protein composition of the vaccinia virus envelope.

* Corresponding author. Mailing address: Dpto. Biotecnología, INIA, Ctra. La Coruña km 7.5, 28040 Madrid, Spain. Phone: 34-91-347 39 13. Fax: 34-91-357 22 93. E-mail: blasco{at}inia.es

{triangledown} Published ahead of print on 19 December 2007.

{dagger} B.P. and M.M.L. contributed equally to this work.

{ddagger} Present address: Departamento de Biología Molecular y Celular, Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma, 28049 Madrid, Spain.

Journal of Virology, March 2008, p. 2150-2160, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.01969-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Roberts, K. L., Breiman, A., Carter, G. C., Ewles, H. A., Hollinshead, M., Law, M., Smith, G. L. (2009). Acidic residues in the membrane-proximal stalk region of vaccinia virus protein B5 are required for glycosaminoglycan-mediated disruption of the extracellular enveloped virus outer membrane. J. Gen. Virol. 90: 1582-1591 [Abstract] [Full Text]  


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