v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | During primary envelopment Human herpesvirus 1 (HHV-1, HSV-1) nucleocapsids translocate from the nucleus to the cytoplasm. Lining the inside of the INM is the nuclear lamina, which is composed of a meshwork of proteins with spaces too small for the capsid to move through without some disruption of the lamina. The lamina is mainly made up of lamin A/C and lamin B proteins, with smaller amounts of other proteins also present; this lamina must be disrupted before the nucleocapsids can egress. UL31, nuclear egress protein 2 (also known as UL34) and US3 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids and successful egress of the nucleocapsids [ ]. Although UL34 has been shown to interact directly with lamin A it cannot disrupt lamin structure by itself. Its interaction with UL31 and US3 appears to be crucial for lamin disruption, though the mechanism is not yet clear [, ].This entry includes Herpesvirus UL31 protein, also known as nuclear egress protein 1 (NEC1). Within the host nucleus, NEC1 interacts with the newly formed capsid and directs it to the inner nuclear membrane by associating with nuclear egress protein 2 (UL34 or NEC2) [ , ]. The NEC1/NEC2 complex, known as the nuclear egress complex (NEC), induces the budding of the capsid at the inner nuclear membrane and its envelopment into the perinuclear space, where the complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm []. |
| Short Name | Herpes_UL31 |