5zz8

Publication Abstract from PubMed

Herpes simplex viruses (HSVs) cause human oral and genital ulcer diseases. Patients with HSV-2 have a higher risk of acquiring a human immunodeficiency virus infection. HSV-2 is a member of the alpha-herpesvirinae subfamily that together with the beta- and gamma-herpesvirinae subfamilies forms the Herpesviridae family. Here, we report the cryo-electron microscopy structure of the HSV-2 C-capsid with capsid-vertex-specific component (CVSC) that was determined at 3.75 A using a block-based reconstruction strategy. We present atomic models of multiple conformers for the capsid proteins (VP5, VP23, VP19C, and VP26) and CVSC. Comparison of the HSV-2 homologs yields information about structural similarities and differences between the three herpesviruses sub-families and we identify alpha-herpesvirus-specific structural features. The hetero-pentameric CVSC, consisting of a UL17 monomer, a UL25 dimer and a UL36 dimer, is bound tightly by a five-helix bundle that forms extensive networks of subunit contacts with surrounding capsid proteins, which reinforce capsid stability.

Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component.,Wang J, Yuan S, Zhu D, Tang H, Wang N, Chen W, Gao Q, Li Y, Wang J, Liu H, Zhang X, Rao Z, Wang X Nat Commun. 2018 Sep 10;9(1):3668. doi: 10.1038/s41467-018-06078-4. PMID:30201968^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.