National Institutes of Health/National Center for Research Resources (NIH/NCRR)
1S10RR23057
米国
Other government
2016YFA0400900
中国
National Science Foundation (NSF, United States)
DBI-1338135
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
1U24GM116792
米国
National Science Foundation (NSF, United States)
DMR-1548924
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM071940
米国
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE028583
米国
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE025567
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI094386
米国
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE027901
米国
National Institutes of Health/National Cancer Institute (NIH/NCI)
CA091791
米国
National Institutes of Health/National Cancer Institute (NIH/NCI)
CA177322
米国
Other government
2017YFA0505300
中国
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE023591
米国
引用
ジャーナル: Cell / 年: 2019 タイトル: DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV. 著者: Danyang Gong / Xinghong Dai / Jonathan Jih / Yun-Tao Liu / Guo-Qiang Bi / Ren Sun / Z Hong Zhou / 要旨: Assembly of Kaposi's sarcoma-associated herpesvirus (KSHV) begins at a bacteriophage-like portal complex that nucleates formation of an icosahedral capsid with capsid-associated tegument complexes ...Assembly of Kaposi's sarcoma-associated herpesvirus (KSHV) begins at a bacteriophage-like portal complex that nucleates formation of an icosahedral capsid with capsid-associated tegument complexes (CATCs) and facilitates translocation of an ∼150-kb dsDNA genome, followed by acquisition of a pleomorphic tegument and envelope. Because of deviation from icosahedral symmetry, KSHV portal and tegument structures have largely been obscured in previous studies. Using symmetry-relaxed cryo-EM, we determined the in situ structure of the KSHV portal and its interactions with surrounding capsid proteins, CATCs, and the terminal end of KSHV's dsDNA genome. Our atomic models of the portal and capsid/CATC, together with visualization of CATCs' variable occupancy and alternate orientation of CATC-interacting vertex triplexes, suggest a mechanism whereby the portal orchestrates procapsid formation and asymmetric long-range determination of CATC attachment during DNA packaging prior to pleomorphic tegumentation/envelopment. Structure-based mutageneses confirm that a triplex deep binding groove for CATCs is a hotspot that holds promise for antiviral development.