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An Update of the Virion Proteome of Kaposi Sarcoma-Associated Herpesvirus
Article

The Portal Vertex of KSHV Promotes Docking of Capsids at the Nuclear Pores

1
The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat Gan 5290002, Israel
2
Department of Chemistry, Bar-Ilan University, Ramat Gan 5290002, Israel
3
Advanced Materials and Nanotechnology Institute, Bar-Ilan University, Ramat Gan 5290002, Israel
*
Author to whom correspondence should be addressed.
Academic Editor: Jennifer Corcoran
Viruses 2021, 13(4), 597; https://doi.org/10.3390/v13040597
Received: 21 March 2021 / Accepted: 29 March 2021 / Published: 31 March 2021
(This article belongs to the Special Issue New Advances in Kaposi's Sarcoma-Associated Herpesvirus Research)
Kaposi’s sarcoma-associated herpesvirus (KSHV) is a cancer-related herpesvirus. Like other herpesviruses, the KSHV icosahedral capsid includes a portal vertex, composed of 12 protein subunits encoded by open reading frame (ORF) 43, which enables packaging and release of the viral genome into the nucleus through the nuclear pore complex (NPC). Capsid vertex-specific component (CVSC) tegument proteins, which directly mediate docking at the NPCs, are organized on the capsid vertices and are enriched on the portal vertex. Whether and how the portal vertex is selected for docking at the NPC is unknown. Here, we investigated the docking of incoming ORF43-null KSHV capsids at the NPCs, and describe a significantly lower fraction of capsids attached to the nuclear envelope compared to wild-type (WT) capsids. Like WT capsids, nuclear envelope-associated ORF43-null capsids co-localized with different nucleoporins (Nups) and did not detach upon salt treatment. Inhibition of nuclear export did not alter WT capsid docking. As ORF43-null capsids exhibit lower extent of association with the NPCs, we conclude that although not essential, the portal has a role in mediating the interaction of the CVSC proteins with Nups, and suggest a model whereby WT capsids can dock at the nuclear envelope through a non-portal penton vertex, resulting in an infection ‘dead end’. View Full-Text
Keywords: Kaposi’s sarcoma-associated herpesvirus (KSHV); open reading frame 43 (ORF43); portal; nuclear pore complex (NPC); capsid vertex-specific component (CVSC) Kaposi’s sarcoma-associated herpesvirus (KSHV); open reading frame 43 (ORF43); portal; nuclear pore complex (NPC); capsid vertex-specific component (CVSC)
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MDPI and ACS Style

Dünn-Kittenplon, D.; Ashkenazy-Titelman, A.; Kalt, I.; Lellouche, J.-P.; Shav-Tal, Y.; Sarid, R. The Portal Vertex of KSHV Promotes Docking of Capsids at the Nuclear Pores. Viruses 2021, 13, 597. https://doi.org/10.3390/v13040597

AMA Style

Dünn-Kittenplon D, Ashkenazy-Titelman A, Kalt I, Lellouche J-P, Shav-Tal Y, Sarid R. The Portal Vertex of KSHV Promotes Docking of Capsids at the Nuclear Pores. Viruses. 2021; 13(4):597. https://doi.org/10.3390/v13040597

Chicago/Turabian Style

Dünn-Kittenplon, Daniela, Asaf Ashkenazy-Titelman, Inna Kalt, Jean-Paul Lellouche, Yaron Shav-Tal, and Ronit Sarid. 2021. "The Portal Vertex of KSHV Promotes Docking of Capsids at the Nuclear Pores" Viruses 13, no. 4: 597. https://doi.org/10.3390/v13040597

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