Disease relevance of UL19

• DNA sequence of the major capsid protein gene of herpes simplex virus type 1 [1].
• Comparisons of the amino acid sequence of this protein with those predicted from the published DNA sequences of two other herpesviruses, varicella-zoster virus and Epstein-Barr virus, resulted in the identification of the major capsid protein gene in each genome [1].
• We previously identified a minimal 12-amino-acid domain in the C terminus of the herpes simplex virus type 1 (HSV-1) scaffolding protein which is required for interaction with the HSV-1 major capsid protein [2].
• In cells infected with EHV-1 preparations rich in DI particles, the synthesis of major capsid protein 150000 was greatly reduced, whereas core protein 46000, a major component of I capsids, was overproduced as compared to standard virus infection [3].
• We have also used a monoclonal antibody (5C) specific for the hexon form of major capsid protein VP5 to study the distribution of capsids during infection [4].

High impact information on UL19

• The herpes simplex virus-1 (HSV-1) SCP was shown to be horn shaped and to specifically bind the upper domain of each major capsid protein in hexons but not in pentons [5].
• These data indicate that the precise timing of appearance of the major capsid protein plays a role in the pathogenesis of HSV infections and that changing the expression kinetics has different effects in different cell types and tissues [6].
• The hexameric and pentameric capsomers are composed of the major capsid protein (MCP) encoded by open reading frame 25 [7].
• The study showed that the glutathione S-transferase fusion containing 16 amino acids near the C-terminal end was sufficient to interact with the major capsid protein [2].
• When this region was converted so as to correspond to that of HSV-1, the CMV assembly protein domain lost its ability to interact with the CMV major capsid protein but gained full interaction with the HSV-1 major capsid protein [2].

Chemical compound and disease context of UL19

• The capsids formed in this system resembled native HSV-1 capsids in morphology as judged by electron microscopy, in sedimentation rate on sucrose density gradients, in protein composition, and in their ability to react with antibodies specific for the HSV-1 major capsid protein, VP5 [8].

Biological context of UL19

• We have recently reported that a cellular factor, the leaky-late binding factor (LBF), binds to sites in a number of leaky-late (beta gamma or gamma 1) genes of herpes simplex virus type 1 and that an LBF site is essential for maximum viral transactivation of the major capsid protein (VP5) gene [9].
• Mutational analysis of sequences downstream of the TATA box of the herpes simplex virus type 1 major capsid protein (VP5/UL19) promoter [10].
• Using confocal immunofluorescence microscopy, it was observed that in > 95% of HEp-2 cells fixed at late times after infection with wild-type HSV-1, capsids, major capsid proteins ICP5 and ICP35, and the UL6-encoded minor capsid protein localized in DNA replication compartments [11].

Anatomical context of UL19

• Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a [12].

Associations of UL19 with chemical compounds

• VP5, a 150 kDa major capsid protein that makes up both the penton and the bulk of the hexon subunits, has three domains: an upper diamond-shaped domain, a middle stem-like domain, and a lower anchoring domain [13].
• Two are early (beta) promoters, for alkaline exonuclease and deoxyuridine triphosphate nucleotidohydrolase; the third promoter controls the major capsid protein transcript and is late (beta gamma) [14].

Other interactions of UL19

• VP5, the major capsid protein of herpes simplex virus type 1 (HSV-1), interacts with the C-terminal residues of the scaffold molecules encoded by the overlapping UL26 and UL26.5 open reading frames [15].

References