Apr 6, 2018 · Our structure of the HSV-1 capsid with capsid-associated tegument proteins provides mechanistic insights into multiple aspects of the viral life cycle, including capsid assembly, nuclear egress, acquisition of tegument and envelope, and …

The capsid shell of HSV-1 is built from four structural proteins: a major capsid protein, VP5, which forms the capsomers (hexons and pentons), the triplex consisting of VP19C and VP23 found between the capsomers, and VP26 which binds to VP5 on hexons but not pentons.

Initial studies of herpes simplex virus (HSV-1) capsid structure were carried out with capsids isolated from the infected cell nucleus. Three types of capsids, A, B and C capsids, were isolated and all were found to have the same shell structure.

Aug 25, 2022 · Herpes simplex virus 1 (HSV-1). Structure, Genome, Epidemiology, Transmission, Replication, Pathogenesis, Clinical Manifestation, Lab Diagnosis, Treatment.

Aug 28, 2023 · Herpes simplex virus type 1 (HSV-1) is a member of the Alphaherpesviridae subfamily. Its structure is composed of linear dsDNA, an icosahedral capsid that is 100 to 110 nm in diameter, with a spikey envelope.

Feb 2, 2003 · Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid. The major capsid protein, VP5 (149 kDa), makes up both types of capsomere, pentons and hexons.

Apr 6, 2018 · Here we report cryo-electron microscopy structures of the HSV-1 capsid with CATC up to 3.5-angstrom resolution and atomic models of multiple conformers of capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36.

rt of their genome-containing capsids between sites of infection and neuronal cell bodies. Here we report cryo–electron microscopy structures of the HSV-1 capsid with CATC up to 3.5-angstrom resolution and atomic models of multiple conformers o.

Dec 15, 2021 · It has been shown that capsid vertex-specific component (CVSC) proteins, which are located at the twelve vertices of the human herpes simplex virus type 1 (HSV-1) capsid, interact with nucleoporins (Nups) of NPCs.

Our structure of the HSV-1 capsid with capsid-associated tegument proteins provides mechanistic insights into multiple aspects of the viral life cycle, including capsid assembly, nuclear egress, acquisition of tegument and envelope, and axonal transport in neuronal cells.