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Journal of Virology, September 2006, p. 8763-8777, Vol. 80, No. 17
0022-538X/06/$08.00+0     doi:10.1128/JVI.00598-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Interaction between Vaccinia Virus Extracellular Virus Envelope A33 and B5 Glycoproteins

Beatriz Perdiguero{dagger} and Rafael Blasco*

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

Received 24 March 2006/ Accepted 15 June 2006

The extracellular form of vaccinia virus acquires its outer envelope by wrapping with cytoplasmic membranes that contain at least seven virus-encoded proteins, of which four are glycoproteins. We searched for interactions between the vaccinia virus A33 glycoprotein and proteins A34, A36, B5, F12, and F13. First, when myc epitope-tagged A33 was expressed in combination with other envelope proteins, A33 colocalized with B5 and A36, suggesting that direct A33-B5 and A33-A36 interactions occur in the absence of infection. A recombinant vaccinia virus (vA33Rmyc) was constructed by introduction of the myc-tagged A33 version (A33myc) into A33-deficient vaccinia virus. A33myc partially restored plaque formation and colocalized with enveloped virions in infected cells. Coimmunoprecipitation experiments with extracts of vA33Rmyc-infected cells confirmed the existence of a physical association of A33 with A36 and B5. Of these, the A33-B5 interaction is a novel finding, whereas the interaction between A33 and A36 has been previously characterized. A collection of vaccinia viruses expressing mutated versions of the B5 protein was used to investigate the domain(s) of B5 required for interaction with A33. Both the cytoplasmic domain and most of the extracellular domain, but not the transmembrane domain, of the B5 protein were dispensable for binding to A33. Mutations in the extracellular portions of B5 and A33 that enhance extracellular virus release did not affect the interaction between the two. In contrast, substituting the B5 transmembrane domain with that of the vesicular stomatitis virus G glycoprotein prevented the association with A33. Immunofluorescence experiments on virus mutants indicated that B5 is required for efficient targeting of A33 into enveloped virions. These results point to the transmembrane domain of B5 as the major determinant of the A33-B5 interaction and demonstrate that protein-protein interactions are crucial in determining the composition of the 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.

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

Journal of Virology, September 2006, p. 8763-8777, Vol. 80, No. 17
0022-538X/06/$08.00+0     doi:10.1128/JVI.00598-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Earley, A. K., Chan, W. M., Ward, B. M. (2008). The Vaccinia Virus B5 Protein Requires A34 for Efficient Intracellular Trafficking from the Endoplasmic Reticulum to the Site of Wrapping and Incorporation into Progeny Virions. J. Virol. 82: 2161-2169 [Abstract] [Full Text]  
  • Perdiguero, B., Lorenzo, M. M., Blasco, R. (2008). Vaccinia Virus A34 Glycoprotein Determines the Protein Composition of the Extracellular Virus Envelope. J. Virol. 82: 2150-2160 [Abstract] [Full Text]  


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