Repozitorij Univerze v Novi Gorici

Izpis gradiva
A+ | A- | Pomoč | SLO | ENG

Naslov:Phosphorylation of HPV-16 L2 Contributes To Efficient Virus Infectious Entry
Avtorji:ID Broniarczyk, Justyna (Avtor)
ID Massimi, Paola (Avtor)
ID Pim, David, ICGEB (Avtor)
ID Bergant Marušič, Martina (Avtor)
ID Myers, Michael P. (Avtor)
ID Garcea, Robert L. (Avtor)
ID Banks, Lawrence (Avtor)
Datoteke: Gradivo nima datotek, ki so prostodostopne za javnost. Gradivo je morda fizično dosegljivo v knjižnici fakultete, zalogo lahko preverite v COBISS-u. Povezava se odpre v novem oknu
Jezik:Angleški jezik
Vrsta gradiva:Članek v reviji
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:UNG - Univerza v Novi Gorici
Opis:The Human Papillomavirus (HPV) capsid comprises two viral proteins, L1 and L2, with the L2 component being essential to ensure efficient endocytic transport of incoming viral genomes. Several studies have previously reported that L1 and L2 are post-translationally modified, but it is uncertain whether these modifications affect HPV infectious entry. Using a proteomic screen, we identified a highly conserved phospho-acceptor site on the HPV-16 and BPV-1 L2 proteins. The phospho-modification of L2, and its presence in HPV pseudovirions (PsVs), was confirmed using anti-phospho L2-specific antibodies. Mutation of the phospho-acceptor sites of both HPV-16 and BPV-1 L2 resulted in the production of infectious virus particles, with no differences in efficiency of packaging the reporter DNA. However, these mutated PsVs showed marked defects in infectious entry. Further analysis revealed a defect in uncoating, characterized by a delay in the exposure of a conformational epitope on L1 that indicates capsid uncoating. This uncoating defect was accompanied by a delay in the proteolysis of both L1 and L2 in mutated HPV-16 PsVs. Taken together, these studies indicate that phosphorylation of L2 during virus assembly plays an important role in optimal uncoating of virions during infection, suggesting that phosphorylation of the viral capsid proteins contributes to infectious entry.
Ključne besede:HPV, L2, infection, protein phosphorylation
Verzija publikacije:Nerecenzirani rokopis
Leto izida:2019
Št. strani:14
Številčenje:0
PID:20.500.12556/RUNG-4565-6b4290bd-3e16-077b-159f-ce3035d65145 Novo okno
COBISS.SI-ID:5402619 Novo okno
DOI:10.1128/JVI.00128-19 Novo okno
NUK URN:URN:SI:UNG:REP:EIBNRM1Y
Datum objave v RUNG:05.06.2019
Število ogledov:4833
Število prenosov:0
Metapodatki:XML DC-XML DC-RDF
:
BRONIARCZYK, Justyna, MASSIMI, Paola, PIM, David, BERGANT MARUŠIČ, Martina, MYERS, Michael P., GARCEA, Robert L. in BANKS, Lawrence, 2019, Phosphorylation of HPV-16 L2 Contributes To Efficient Virus Infectious Entry. Journal of Virology [na spletu]. 2019. Vol. 0. [Dostopano 12 april 2025]. DOI 10.1128/JVI.00128-19. Pridobljeno s: https://repozitorij.ung.si/IzpisGradiva.php?lang=slv&id=4565
Kopiraj citat
  
Skupna ocena:
0.5
1
1.5
2
2.5
3
3.5
4
4.5
5
(0 glasov)
Vaša ocena:Ocenjevanje je dovoljeno samo prijavljenim uporabnikom.
Objavi na:Bookmark and Share


Podobna dela iz repozitorija:

Ni podobnih del

Podobna dela iz ostalih repozitorijev:

Ni podobnih del

Postavite miškin kazalec na naslov za izpis povzetka. Klik na naslov izpiše podrobnosti ali sproži prenos.

Gradivo je del revije

Naslov:Journal of Virology
Leto izida:2019

Licence

Licenca:CC BY-NC-ND 4.0, Creative Commons Priznanje avtorstva-Nekomercialno-Brez predelav 4.0 Mednarodna
Povezava:http://creativecommons.org/licenses/by-nc-nd/4.0/deed.sl
Opis:Najbolj omejujoča licenca Creative Commons. Uporabniki lahko prenesejo in delijo delo v nekomercialne namene in ga ne smejo uporabiti za nobene druge namene.
Začetek licenciranja:03.06.2019

Nazaj