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Gene Review:

UL34 - type 2 membrane protein; interacts with...

Bovine herpesvirus 1

Schnee, M. et al., Antinone, S.E. et al., Asano, Y. et al., Haanes, E.J. et al., Ongkosuwito, J.V. et al.

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Disease relevance of UL34

We substituted the proteins encoded by the BHV-1 homologs of the UL26 and UL26.5 open reading frames, expressed in baculovirus, for the corresponding HSV-1 proteins in an in vitro HSV-1 capsid assembly system [1].
The proteins encoded by the UL34 and UL31 genes of herpes simplex virus are conserved among herpesviruses [2].
Starting with derivatives of pseudorabies virus that encode a fluorescent protein fused to a structural component of the virus, we have made a collection of 12 mutant viruses that lack either the VP26 capsid protein or an individual tegument protein [3].
RESULTS: Serum antibody titres to EBV capsid antigen proved to be significantly increased in HIV negative immunocompromised patients with uveitis (p < 0.01) compared with controls [4].

High impact information on UL34

A protein complementation assay (PCA) using the TEM-1 beta-lactamase fragments fused to UL31 and UL34 protein homologues was used to study protein-protein interactions in cells [2].
Here we show that the CR1 of all tested UL31 proteins contains the UL34 binding site, and chimeric proteins carrying the subfamily-specific CR1 rescued the ability to cross-complement in the PCA [2].
Under this experimental condition, virus-induced protein and glycoprotein began to appear 4 to 6 and 18 to 20 h after infection, respectively, and a capsid protein (MW 145,000) was prominent 18 h after injection [5].

References

The bovine herpesvirus 1 maturational proteinase and scaffold proteins can substitute for the homologous herpes simplex virus type 1 proteins in the formation of hybrid type B capsids. Haanes, E.J., Thomsen, D.R., Martin, S., Homa, F.L., Lowery, D.E. J. Virol. (1995) [Pubmed]
Common and Specific Properties of Herpesvirus UL34/UL31 Protein Family Members Revealed by Protein Complementation Assay. Schnee, M., Ruzsics, Z., Bubeck, A., Koszinowski, U.H. J. Virol. (2006) [Pubmed]
The Herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus. Antinone, S.E., Shubeita, G.T., Coller, K.E., Lee, J.I., Haverlock-Moyns, S., Gross, S.P., Smith, G.A. J. Virol. (2006) [Pubmed]
Increased presence of Epstein-Barr virus DNA in ocular fluid samples from HIV negative immunocompromised patients with uveitis. Ongkosuwito, J.V., Van der Lelij, A., Bruinenberg, M., Wienesen-van Doorn, M., Feron, E.J., Hoyng, C.B., de Keizer, R.J., Klok, A.M., Kijlstra, A. The British journal of ophthalmology. (1998) [Pubmed]
Studies on the polypeptides of varicella-zoster (V-Z) virus. II. Syntheses of viral polypeptides in infected cells. Asano, Y., Takahashi, M. Biken journal. (1980) [Pubmed]

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