Disease relevance of UL19

• 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 [1].
• The glycoproteins gC and gE are largely type-specific; whereas gB and gD as well as ICP35, ICP8 and the major capsid protein represent well conserved proteins of the simplexviruses [2].
• We have asked whether the promoter for the gene encoding the major capsid protein (VP5) of herpes simplex virus functions in uninfected mouse cells [3].
• The purpose of this investigation was to identify and characterize the regulatory elements involved in the transcriptional activation of the beta gamma (leaky-late or gamma 1) genes of herpes simplex virus type 1 (HSV-1) by using the major capsid protein (VP5 or ICP5) gene as model [4].
• Herpes simplex virus type 1 (HSV-1) capsids have an icosahedral structure with capsomers formed by the major capsid protein, VP5, linked in groups of three by distinctive structures called triplexes [5].

High impact information on UL19

• The hexameric and pentameric capsomers are composed of the major capsid protein (MCP) encoded by open reading frame 25 [6].
• CD4 T-cell responses to herpes simplex virus type 2 major capsid protein VP5: comparison with responses to tegument and envelope glycoproteins [7].
• Comparison of 8MA and 8MA/DeltaSma with respect to viral DNA accumulation and encapsidation and accumulation of the major capsid protein, VP5, revealed that the 8MA lethal phenotype is only partially due to uncontrolled vhs activity, indicating that VP16 is required in HSV-1 virion formation [8].
• We used CD4 lymphocyte clones from herpes simplex virus type 2 (HSV-2) lesions or the cervix and molecular libraries of HSV-2 DNA to define HSV-2 major capsid protein VP5 and glycoprotein E (gE) as T-cell antigens [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 [9].

Chemical compound and disease context of UL19

• Hexon-only binding of VP26 reflects differences between the hexon and penton conformations of VP5, the major capsid protein of herpes simplex virus [10].
• Several HSV-1 proteins including the major capsid protein (VP5), two minor capsid proteins (VP11-12 and VP18.8), the alkaline nuclease and glycoprotein gH have been reported to be encoded by the left-most one-third of HSV-1 UL DNA [11].

Biological context of UL19

• Two herpes simplex virus proteins, the major capsid protein and the major DNA binding protein, are specifically localized to the nucleus of infected cells [12].
• Transactivation of the major capsid protein gene of herpes simplex virus type 1 requires a cellular transcription factor [4].
• However, VP26 is not present on pentons, indicating that the conformational differences between the hexon and penton states of the major capsid protein, VP5, extend to the VP26 binding site [13].
• Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics [14].
• We examined the kinetics and the nature of the association of two herpes simplex virus proteins, the major DNA-binding protein (ICP8) and the major capsid protein (ICP5), with the nuclei of infected cells [15].

Anatomical context of UL19

• The major capsid protein showed some similar stages of association with the cell nucleus but the initial association with the nucleus followed a lag period [15].
• They appeared to be associated with an enrichment of the 155K major capsid protein in the nuclear membrane subfractions as compared with the protein composition of nuclei and plasma membrane fractions [16].
• Indirect immunofluorescence assays with monoclonal antibodies revealed that ICP5, the major capsid protein, accumulated on the nuclear matrix while ICP8, the major viral DNA binding protein, accumulates in the chromatin fraction that can be separated from the nuclear matrix by extraction with DNase and salt [17].

Associations of UL19 with chemical compounds

• Treatment of HSV-infected BHK-21 cells with 5-10 mM of beta-hydroxynorvaline (Hnv), an analog of threonine which blocked attachment of oligosaccharides at the Asn-X-Thr sites, markedly inhibited the synthesis of all viral glycoproteins as well as the major capsid protein [18].

Analytical, diagnostic and therapeutic context of UL19

• Immunoblotting of individual gradient fractions indicated that ICP10 cosediments with the major capsid protein and the highest virus titers [19].
• A monospecific antiserum raised against the fusion protein close to the N terminus of the MCP, as well as a monoclonal antibody and a monospecific rabbit antiserum directed against the viral MCP, cross-reacted with the VP5 as shown by immunoblotting and immunofluorescence [20].
• Polymerase chain reaction (PCR) was used to detect herpesvirus DNA and HCMV cDNA of major capsid protein transcripts, indicative of viral activation [21].

References