Residues F593 and E596 of HSV-1 tegument protein pUL36 (VP1/2) mediate binding of tegument protein pUL37

The interaction of HSV-1 tegument proteins pUL36 and pUL37: a novel target for antivirals that inhibit viral assembly

Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1.

Studies with herpes simplex virus type 1 (HSV-1) have shown that secondary envelopment and virus release are blocked in mutants deleted for the tegument protein gene UL36 or UL37, leading to the accumulation of DNA-containing capsids in the cytoplasm of infected cells. The failure to assemble infectious virions has meant that the roles of these genes in the initial stages of infection could not...

Intercellular Trafficking of VP22, a Herpes Simplex Virus Type 1 Tegument Protein

The herpes simplex virus type 1 (HSV-1) tegument protein, VP22 has been reported to have the property of intercellular transport. The previous studies have shown that following expression of a fusion protein containing VP22 it spreads to every cell in a monolayer and concentrates in the nucleus. In spite of these reports, some studies have shown that VP22 trafficking and its nucleus accumulatio...

The Large Tegument Protein pUL36 Is Essential for Formation of the Capsid Vertex-Specific Component at the Capsid-Tegument Interface of Herpes Simplex Virus 1

UNLABELLED Herpesviruses have a characteristic particle structure comprising an icosahedral capsid, which contains the DNA genome and is, in turn, surrounded by a proteinaceous tegument layer and a lipid envelope. In herpes simplex virus, the interaction between the capsid and tegument is limited to the capsid vertices and involves two minor capsid proteins, pUL17 and pUL25, and the large inner...

The tegument protein UL94 of human cytomegalovirus as a binding partner for tegument protein pp28 identified by intracellular imaging.

The tegument protein pp28 of human cytomegalovirus (HCMV) is essential for the assembly of infectious HCMV virions, but how it functions during the process of HCMV tegumentation and envelopment remains unclear. By using live cell fluorescence resonance energy transfer (FRET) microscopy and yeast two-hybrid assays, we found that another HCMV tegument protein, UL94, was a specific binding partner...