• Medientyp: E-Book; Hochschulschrift
  • Titel: Struktur-Funktions-Beziehungen des Pseudorabies Virus pUL31 während der Kernfreisetzung neusynthetisierter Nukleokapside
  • Beteiligte: Rönfeldt, Sebastian [VerfasserIn]; Mettenleiter, Thomas C. [AkademischeR BetreuerIn]; Antonin, Wolfram [AkademischeR BetreuerIn]
  • Körperschaft: Universität Greifswald
  • Erschienen: Greifswald, Juli 2020
  • Umfang: 1 Online-Ressource (PDF-Datei: 150 Seite, 19047 Kilobyte); Illustrationen (teilweise farbig), Diagramme (teilweise farbig)
  • Sprache: Deutsch; Englisch
  • Identifikator:
  • Entstehung:
  • Schlagwörter: Herpesviren > Capsid > Herpesvirus suis > Nucleocapsid > Kernhülle > Fragmentierung
  • Beschreibung: Herpesviren, Kapsid, Pseudorabies, Kernexport, UL31, UL34, NEC, Nuclear Egress, Structure

    The nuclear egress of newly synthesized capsids represents a key feature in herpesvirus replication. However, the underlying mechanism of this vesicle-mediated translocation has not yet been fully understood. Nuclear egress is orchestrated by two viral proteins, designated as pUL31 and pUL34 in PrV and HSV-1/-2, which are conserved throughout the Herpesviridae. Both proteins interact at the inner nuclear membrane, where they form the so-called nuclear egress complex (NEC). While pUL34 is a membrane-bound protein autonomously locating to the nuclear envelope, soluble pUL31 is actively transported into the nucleus. Although the first step of nuclear egress, i.e. the formation of vesicles and their scission at the inner nuclear membrane, has already been well investigated and the crystal structures of the NEC have been determined for various herpesviruses, many questions remain. At the beginning of this work it was still unclear how the capsids are incorporated into these vesicles and what role the non-conserved and flexible N-terminal domain of pUL31, which could not be represented in the crystal structures, plays for the regulation of this process. Therefore, this work focussed on the question of how the capsids interact with the NEC (Paper I and II) and how the N-terminal part of pUL31 influences this unusual transport route (Paper III). Papers I and II: Investigations on the nucleocapsid/NEC interaction It is still unclear how the NEC interacts with its cargo, the ...
  • Anmerkungen: Literaturverzeichnis: Seite 115-136
    Text deutsch, Publikationen englisch
  • Zugangsstatus: Freier Zugang