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The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89
Journal of Virology, 87 (2013), 3; 1720-1732. https://doi.org/10.1128/JVI.01955-12
Borst, Eva Maria; Kleine-Albers, Jennifer; Gabaev, Ildar; Babić, Marina; Wagner, Karen; Binz, Anne; Degenhardt, Inga; Kalesse, Markus; Jonjić, Stipan; Bauerfeind, Rudolf; Messerle, Martin

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Borst, E. M., Kleine Albers, J., Gabaev, I., Babić, M., Wagner, K., Binz, A. ... Messerle, M. (2013). The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89. Journal of Virology, 87. (3), 1720-1732. doi: 10.1128/JVI.01955-12

Borst, Eva Maria, et al. "The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89." Journal of Virology, vol. 87, br. 3, 2013, str. 1720-1732. https://doi.org/10.1128/JVI.01955-12

Borst, Eva Maria, Jennifer Kleine Albers, Ildar Gabaev, Marina Babić, Karen Wagner, Anne Binz, Inga Degenhardt, et al. "The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89." Journal of Virology 87, br. 3 (2013): 1720-1732. https://doi.org/10.1128/JVI.01955-12

Borst, E. M., et al. (2013) 'The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89', Journal of Virology, 87(3), str. 1720-1732. doi: 10.1128/JVI.01955-12

Borst EM, Kleine Albers J, Gabaev I, Babić M, Wagner K, Binz A, i sur.. The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89. Journal of Virology [Internet]. 01.02.2013. [pristupljeno 19.11.2024.];87(3):1720-1732. doi: 10.1128/JVI.01955-12

E. M. Borst, et al., "The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89", Journal of Virology, vol. 87, br. 3, str. 1720-1732, Veljača 2013. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:184:589071. [Citirano: 19.11.2024.]

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Naslov (engleski)The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89
AutorEva Maria Borst
AutorJennifer Kleine-Albers
AutorIldar Gabaev
AutorMarina Babić
AutorKaren Wagner
AutorAnne Binz
AutorInga Degenhardt
AutorMarkus Kalesse
AutorStipan Jonjić
AutorRudolf Bauerfeind
AutorMartin Messerle
Autorova ustanovaSveučilište u Rijeci
Medicinski fakultet
(Katedra za histologiju i embriologiju)
Znanstveno / umjetničko
područje, polje i grana		BIOMEDICINA I ZDRAVSTVO
Temeljne medicinske znanosti
Sažetak (engleski)
ABSTRACT Cleavage of human cytomegalovirus (HCMV) genomes as well as their packaging into capsids is an enzymatic process mediated by viral proteins and therefore a promising target for antiviral therapy. The HCMV proteins pUL56 and pUL89 form the terminase and play a central role in cleavage-packaging, but several additional viral proteins, including pUL51, had been suggested to contribute to this process, although they remain largely uncharacterized. To study the function of pUL51 in infected cells, we constructed HCMV mutants encoding epitope-tagged versions of pUL51 and used a conditionally replicating virus (HCMV-UL51-ddFKBP), in which pUL51 levels could be regulated by a synthetic ligand. In cells infected with HCMV-UL51-ddFKBP, viral DNA replication was not affected when pUL51 was knocked down. However, no unit-length genomes and no DNA-filled C capsids were found, indicating that cleavage of concatemeric HCMV DNA and genome packaging into capsids did not occur in the absence of pUL51. pUL51 was expressed mainly with late kinetics and was targeted to nuclear replication compartments, where it colocalized with pUL56 and pUL89. Upon pUL51 knockdown, pUL56 and pUL89 were no longer detectable in replication compartments, suggesting that pUL51 is needed for their correct subnuclear localization. Moreover, pUL51 was found in a complex with the terminase subunits pUL56 and pUL89. Our data provide evidence that pUL51 is crucial for HCMV genome cleavage-packaging and may represent a third component of the viral terminase complex. Interference with the interactions between the terminase subunits by antiviral drugs could be a strategy to disrupt the HCMV replication cycle.
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran - međunarodna recenzija
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaJournal of Virology
Brojčani podacivol. 87, br. 3, str. 1720-1732
p-ISSN0022-538X
e-ISSN1098-5514
DOIhttps://doi.org/10.1128/JVI.01955-12
URN:NBNurn:nbn:hr:184:589071
Datum objave publikacije2013-02-01
Datum objave publikacije2012-11-21
URL dokumentahttp://jvi.asm.org/lookup/doi/10.1128/JVI.01955-12
Vrsta resursaTekst
Prava pristupaOtvoreni pristup
Uvjeti korištenjaIkona licence Imenovanje 4.0 međunarodna (CC BY 4.0)
Datum i vrijeme pohrane2019-02-25 22:56:17