Assembly of infectious Kaposi’s sarcoma-associated herpesvirus progeny requires formation of a pORF19 pentamer

Autor: Peter Naniima, Eleonora Naimo, Sandra Koch, Ute Curth, Khaled R. Alkharsah, Luisa J. Ströh, Anne Binz, Jan-Marc Beneke, Benjamin Vollmer, Heike Böning, Eva Maria Borst, Prashant Desai, Jens Bohne, Martin Messerle, Rudolf Bauerfeind, Pierre Legrand, Beate Sodeik, Thomas F. Schulz, Thomas Krey
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: PLoS Biology, Vol 19, Iss 11 (2021)
Druh dokumentu: article
ISSN: 1544-9173
1545-7885
Popis: Herpesviruses cause severe diseases particularly in immunocompromised patients. Both genome packaging and release from the capsid require a unique portal channel occupying one of the 12 capsid vertices. Here, we report the 2.6 Å crystal structure of the pentameric pORF19 of the γ-herpesvirus Kaposi’s sarcoma-associated herpesvirus (KSHV) resembling the portal cap that seals this portal channel. We also present the structure of its β-herpesviral ortholog, revealing a striking structural similarity to its α- and γ-herpesviral counterparts despite apparent differences in capsid association. We demonstrate pORF19 pentamer formation in solution and provide insights into how pentamerization is triggered in infected cells. Mutagenesis in its lateral interfaces blocked pORF19 pentamerization and severely affected KSHV capsid assembly and production of infectious progeny. Our results pave the way to better understand the role of pORF19 in capsid assembly and identify a potential novel drug target for the treatment of herpesvirus-induced diseases. In herpesviruses, genome packaging and release from the capsid require a unique portal channel. Here, the authors have resolved the crystal structure of a pentameric KSHV pORF19 assembly and find that it resembles the herpesviral portal cap and provides insights how the viral genome is retained within the capsid.
Databáze: Directory of Open Access Journals
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