Disease relevance of UL25

• Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1 [1].
• The distribution of UL17 and UL25 on B capsids was examined using immunogold labeling [2].
• Evolutionary trace analysis of UL25 and its homologues in other herpesviruses was used to locate potentially important amino acids on the surface of the protein, leading to the identification of four putative docking regions for protein partners [1].
• The UL25 packaging protein, which is also present in virions, was not found in significant amounts in L particles, indicating that it is associated only with the capsid [3].
• The rabbit antiserum raised against HSV-1 UL25 protein immunoprecipitated a UL25-homologue of identical size from HSV-2-infected cells [4].

High impact information on UL25

• Herpes simplex virus type 1 DNA-packaging protein UL17 is required for efficient binding of UL25 to capsids [2].
• The herpes simplex virus type 1 UL25 protein is incorporated into the capsid during DNA packaging, and previous studies of a null mutant have demonstrated that its function is essential at the late stages of the head-filling process, either to allow packaging to proceed to completion or for retention of the viral genome within the capsid [1].
• To clarify the functional role of UL25 we analyzed the homologous protein of the alphaherpesvirus pseudorabies virus (PrV) [5].
• Furthermore, this analysis, together with guanidine HCl extraction analysis of purified capsids, indicates that UL6, UL25, and UL28 are able to associate with B capsids in the absence of other DNA cleavage and packaging proteins [6].
• Consistent with previous studies showing that UL6 and UL25 are minor protein constituents of the capsids, we detected these proteins in both B and C capsids [6].

Biological context of UL25

• The herpes simplex virus type 1 (HSV-1) UL25 gene contains a 580-amino-acid open reading frame that codes for an essential protein [7].
• Vero cells were transformed with plasmid DNA that encoded ORF UL25 through UL28 and screened for their ability to support the growth of a mutant virus with a null mutation in UL27 (K082) [8].
• Nucleotide sequence and transcriptional analysis of a portion of the bovine herpesvirus genome encoding genes homologous to HSV-1, UL25, UL26 and UL26.5 [9].

Other interactions of UL25

• In the absence of UL17, the levels of UL25 in the mutant capsids were much lower than those in wt B capsids [2].
• RESULTS: We found that the HSV-1 UL21 gene product, a capsid-associated tegument protein with an apparent molecular mass of 62 kDa, promotes the outgrowth of long cellular processes when it is over-expressed in non-neural cells [10].

Analytical, diagnostic and therapeutic context of UL25

• By immunoelectron microscopy, we detected UL25-specific label on DNA-containing C capsids but not on other intranuclear immature or defective capsid forms [5].

References