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Efficient herpes simplex virus type 1 (HSV-1) capsid formation directed by the varicella-zoster virus scaffolding protein requires the carboxy-terminal sequences from the HSV-1 homologue

Preston, V.G., Kennard, J., Rixon, F.J., Logan, A.J., Mansfield, R.W., and McDougall, I.M. (1997) Efficient herpes simplex virus type 1 (HSV-1) capsid formation directed by the varicella-zoster virus scaffolding protein requires the carboxy-terminal sequences from the HSV-1 homologue. Journal of General Virology, 78 (7). pp. 1633-1646. ISSN 0022-1317

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Publisher's URL: http://vir.sgmjournals.org/content/78/7/1633.abstract

Abstract

The scaffolding protein and associated protease of the human herpesvirus varicella-zoster virus (VZV), encoded by genes 33.5 and 33 respectively, were synthesized in insect cells using a baculovirus expression system. The expressed 33.5 product formed numerous long, flexible, hollow rods, and in this respect different from the herpes simplex virus type 1 (HSV-1) homologue which forms large aggregates consisting mainly of fibrous material interspersed with scaffold-like particles. Removal of 27 amino acids from the carboxy terminus of the VZV scaffolding protein by the gene 33 protease or expression of the cleaved product did not result in any discernible change in the morphology of the scaffolding protein. Again, this was in marked contrast to the situation in HSV-1 where removal of the 25 carboxy-terminal amino acids from the scaffolding protein by the associated protease or expression of VP22a results in the formation of large numbers of scaffold-like particles. Despite these differences, when cells were multiply infected with baculoviruses expressing the HSV-1 capsid shell proteins and the VZV scaffolding protein complete capsids were observed, suggesting that the VZV protein could act as a scaffold for the assembly of the HSV-1 capsid shell. The efficiency of capsid assembly was increased substantially by exchanging the 23 carboxy-terminal amino acids of the VZV scaffolding protein for the corresponding 22 carboxy-terminal amino acids of the HSV-1 homologue, supporting previous work which showed that this region was critical for the formation of intact capsids.

Item Type:Article
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Rixon, Dr Frazer and Preston, Dr Valerie
Authors: Preston, V.G., Kennard, J., Rixon, F.J., Logan, A.J., Mansfield, R.W., and McDougall, I.M.
College/School:College of Medical Veterinary and Life Sciences > School of Life Sciences
College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation > Centre for Virus Research
Journal Name:Journal of General Virology
Journal Abbr.:J. Gen. Virol.
ISSN:0022-1317
ISSN (Online):1465-2099

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