prikaz prve stranice dokumenta The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity
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Scientific paper - Original scientific paper
The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity
Journal of Biological Chemistry, 298 (2022), 3; 101625. https://doi.org/10.1016/j.jbc.2022.101625
Schweininger, Johannes; Kriegel, Mark; Häge, Sigrun; Conrad, Marcus; Alkhashrom, Sewar; Lösing, Josephine; Weiler, Sigrid; Tillmanns, Julia; Egerer-Sieber, Claudia; Decker, Andrea; Lenac Roviš, Tihana; Eichler, Jutta; Sticht, Heinrich; Marschall, Manfred; Muller, Yves A. More authors...

Institutional repository: Repository of the University of Rijeka, Faculty of Medicine

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Schweininger, J., Kriegel, M., Häge, S., Conrad, M., Alkhashrom, S., Lösing, J. ... Muller, Y. A. (2022). The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity. Journal of Biological Chemistry, 298. (3). doi: 10.1016/j.jbc.2022.101625

Schweininger, Johannes, et al. "The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity." Journal of Biological Chemistry, vol. 298, no. 3, 2022. https://doi.org/10.1016/j.jbc.2022.101625

Schweininger, Johannes, Mark Kriegel, Sigrun Häge, Marcus Conrad, Sewar Alkhashrom, Josephine Lösing, Sigrid Weiler, et al. "The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity." Journal of Biological Chemistry 298, no. 3 (2022). https://doi.org/10.1016/j.jbc.2022.101625

Schweininger, J., et al. (2022) 'The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity', Journal of Biological Chemistry, 298(3). doi: 10.1016/j.jbc.2022.101625

Schweininger J, Kriegel M, Häge S, Conrad M, Alkhashrom S, Lösing J, and sur.. The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity. Journal of Biological Chemistry [Internet]. 2022 March [cited 2024 November 09];298(3). doi: 10.1016/j.jbc.2022.101625

J. Schweininger, et al., "The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity", Journal of Biological Chemistry, vol. 298, no. 3, March 2022. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:184:243588. [Accessed: 09 November 2024]

Metadata
Title (english)The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity
AuthorJohannes Schweininger
AuthorMark Kriegel
AuthorSigrun Häge
AuthorMarcus Conrad
AuthorSewar Alkhashrom
AuthorJosephine Lösing
AuthorSigrid Weiler
AuthorJulia Tillmanns
AuthorClaudia Egerer-Sieber
AuthorAndrea Decker
AuthorTihana Lenac Roviš
AuthorJutta Eichler
AuthorHeinrich Sticht
AuthorManfred Marschall
AuthorYves A. Muller
Author's institutionUniversity of Rijeka
Faculty of Medicine
(Center for Proteomics)
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract (english)
Abstract Varicella-zoster virus (VZV) is a human pathogen from the α-subfamily of herpesviruses. The VZV Orf24-Orf27 complex represents the essential viral core nuclear egress complex (NEC) that orchestrates the egress of the preassembled virus capsids from the nucleus. While previous studies have primarily emphasized that the architecture of core NEC complexes is highly conserved among herpesviruses, the present report focuses on subfamily-specific structural and functional features that help explain the differences in the autologous versus nonautologous interaction patterns observed for NEC formation across herpesviruses. Here, we describe the crystal structure of the Orf24-Orf27 complex at 2.1 Å resolution. Coimmunoprecipitation and confocal imaging data show that Orf24-Orf27 complex formation displays some promiscuity in a herpesvirus subfamily-restricted manner. At the same time, analysis of thermodynamic parameters of NEC formation of three prototypical α-, β-, and γ herpesviruses, i.e., VZV, human cytomegalovirus (HCMV), and Epstein-Barr virus (EBV), revealed highly similar binding affinities for the autologous interaction with specific differences in enthalpy and entropy. Computational alanine scanning, structural comparisons, and mutational data highlight intermolecular interactions shared among α-herpesviruses that are clearly distinct from those seen in β- and γ-herpesviruses, including a salt bridge formed between Orf24-Arg167 and Orf27-Asp126. This interaction is located outside of the hook-into-groove interface and contributes significantly to the free energy of complex formation. Combined, these data explain distinct properties of specificity and permissivity so far observed in herpesviral NEC interactions. These findings will prove valuable in attempting to target multiple herpesvirus core NECs with selective or broad-acting drug candidates.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titleJournal of Biological Chemistry
Numberingvol. 298, no. 3, 101625
p-ISSN0021-9258
DOIhttps://doi.org/10.1016/j.jbc.2022.101625
URN:NBNurn:nbn:hr:184:243588
Publication2022-03
Document URLhttps://linkinghub.elsevier.com/retrieve/pii/S0021925822000655
Type of resourceText
Access conditionsOpen access
Terms of useLicence Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) icon
Created on2022-04-26 11:30:22