Disease relevance of UL37

• Identification of nuclear export signal in UL37 protein of herpes simplex virus type 2 [1].
• In this study, we have generated a rabbit polyclonal antiserum against HSV-2 UL37 protein, and examined its intracellular localization by immunofluorescence study [1].
• Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid [2].
• Capsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites [3].
• In summary, our data indicate that the PrV UL17 protein is an internal nucleocapsid protein necessary for DNA cleavage and packaging but suggest that the protein is not a prominent part of the tegument [4].

High impact information on UL37

• Nuclear transport of the viral tegument protein VP16, transport of viral capsids to the nuclear pore, and downstream events (including expression of immediate-early genes and viral plaque formation) were substantially reduced in cells transfected with dominant-negative mutants of FAK or small interfering RNA designed to inhibit FAK expression [5].
• It is required, however, for RNA degradation activity of tegument-derived vhs and wild-type replication and virulence in mice [6].
• Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding [7].
• After contact of infectious virus with the cell plasma membrane, discernible changes of the envelope and tegument could be seen by electron microscopy [8].
• The MDV UL49 gene, which encodes the tegument viral protein 22 (VP22), has been expressed as a green fluorescent protein (GFP) fusion protein in chicken embryonic fibroblasts to examine its subcellular localization [9].

Chemical compound and disease context of UL37

• The protein kinase associated with purified herpes simplex virus 1 and 2 virions partitioned with the capsid-tegument structures and was not solubilized by non-ionic detergents and low, non-inhibitory concentrations of urea [10].
• The technique confirmed that L particles are composed of an outer envelope, i.e. a bilaminar membrane with protruding glycoprotein spikes, and a uniformly granular tegument, but lack any nucleocapsid [11].

Biological context of UL37

• Transfection assays of deletion mutants of UL37 protein suggested that the leucine rich region (LRR) containing amino acids 263-273 may be important for cytoplasmic localization [1].
• The agent has a broad host range and--besides the classical morphogenesis (budding at the internal nuclear membrane)--the virus gets enveloped at all cytoplasmic membranes including the plasma membrane; strikingly it carries a rather prominent tegument [12].
• To confirm more directly that NA induces apoptosis, the NA of clone 7a and A/Fiji was expressed fused to the Herpes simplex virus tegument coat protein VP22, transfected into HeLa cells and the level of apoptosis determined [13].

Anatomical context of UL37

• Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells [14].
• Immunolocalization studies on purified virions indicate that the antigen can be detected only in virions without membranes, and is located outside the capsid, most probably in the tegument [15].

Associations of UL37 with chemical compounds

• Deletion of the LRR or substitution of the leucine residues resulted in nuclear remaining of UL37 protein [1].

References