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Article: DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV

TitleDNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV
Authors
Keywordscryo-EM
virology
tegument
portal
microscopy
Kaposi's sarcoma-associated herpesvirus
herpesvirus
genome
gammaherpesvirus
capsid
Issue Date2019
Citation
Cell, 2019, v. 178, n. 6, p. 1329-1343.e12 How to Cite?
Abstract© 2019 Elsevier Inc. 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.
Persistent Identifierhttp://hdl.handle.net/10722/285843
ISSN
2023 Impact Factor: 45.5
2023 SCImago Journal Rankings: 24.342
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorGong, Danyang-
dc.contributor.authorDai, Xinghong-
dc.contributor.authorJih, Jonathan-
dc.contributor.authorLiu, Yun Tao-
dc.contributor.authorBi, Guo Qiang-
dc.contributor.authorSun, Ren-
dc.contributor.authorZhou, Z. Hong-
dc.date.accessioned2020-08-18T04:56:47Z-
dc.date.available2020-08-18T04:56:47Z-
dc.date.issued2019-
dc.identifier.citationCell, 2019, v. 178, n. 6, p. 1329-1343.e12-
dc.identifier.issn0092-8674-
dc.identifier.urihttp://hdl.handle.net/10722/285843-
dc.description.abstract© 2019 Elsevier Inc. 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.-
dc.languageeng-
dc.relation.ispartofCell-
dc.subjectcryo-EM-
dc.subjectvirology-
dc.subjecttegument-
dc.subjectportal-
dc.subjectmicroscopy-
dc.subjectKaposi's sarcoma-associated herpesvirus-
dc.subjectherpesvirus-
dc.subjectgenome-
dc.subjectgammaherpesvirus-
dc.subjectcapsid-
dc.titleDNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/j.cell.2019.07.035-
dc.identifier.pmid31447177-
dc.identifier.pmcidPMC6753055-
dc.identifier.scopuseid_2-s2.0-85071615985-
dc.identifier.volume178-
dc.identifier.issue6-
dc.identifier.spage1329-
dc.identifier.epage1343.e12-
dc.identifier.eissn1097-4172-
dc.identifier.isiWOS:000483983000010-
dc.identifier.issnl0092-8674-

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