Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-06078-4
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Funding
- Strategic Priority Research Program [XDB29010000, XDB08020200]
- Key Programs of the Chinese Academy [KJZD-SW-L05]
- National Key Research and Development Program [2014CB542800, 2017YFC0840300, 2017YFA0504701]
- National Science Foundation of China [813300237, 31570717, 91530321, 31570742, 81520108019]
- Technology Planning Project of Hunan Province [2017RS3033]
- Young Elite scientist sponsorship by CAST
- program C of One Hundred of Talented People of the Chinese Academy of Sciences
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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 angstrom 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.
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