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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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. Više autora...

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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, br. 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, br. 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, i 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]. 03.2022. [pristupljeno 22.10.2024.];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, br. 3, Ožujak 2022. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:184:243588. [Citirano: 22.10.2024.]

Za citiranje koristite ovu mrežnu adresu: https://urn.nsk.hr/urn:nbn:hr:184:243588
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Naslov (engleski)The crystal structure of the varicella-zoster Orf24-Orf27 nuclear egress complex spotlights multiple determinants of herpesvirus subfamily specificity
AutorJohannes Schweininger
AutorMark Kriegel
AutorSigrun Häge
AutorMarcus Conrad
AutorSewar Alkhashrom
AutorJosephine Lösing
AutorSigrid Weiler
AutorJulia Tillmanns
AutorClaudia Egerer-Sieber
AutorAndrea Decker
AutorTihana Lenac Roviš
AutorJutta Eichler
AutorHeinrich Sticht
AutorManfred Marschall
AutorYves A. Muller
Autorova ustanovaSveučilište u Rijeci
Medicinski fakultet
(Centar za proteomiku)
Znanstveno / umjetničko
područje, polje i grana		BIOMEDICINA I ZDRAVSTVO
Temeljne medicinske znanosti
Sažetak (engleski)
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.
Ključne riječi (engleski)
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran - međunarodna recenzija
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaJournal of Biological Chemistry
Brojčani podacivol. 298, br. 3, 101625
p-ISSN0021-9258
DOIhttps://doi.org/10.1016/j.jbc.2022.101625
URN:NBNurn:nbn:hr:184:243588
Datum objave publikacije2022-03
URL dokumentahttps://linkinghub.elsevier.com/retrieve/pii/S0021925822000655
Vrsta resursaTekst
Prava pristupaOtvoreni pristup
Uvjeti korištenjaIkona licence Imenovanje-Nekomercijalno-Bez prerada 4.0 međunarodna (CC BY-NC-ND 4.0)
Datum i vrijeme pohrane2022-04-26 11:30:22