Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit

Abstract The human cytomegalovirus (HCMV) terminase complex consists of several components acting together to cleave viral DNA into unit length genomes and translocate them into capsids, a critical process in the production of infectious virions subsequent to DNA replication. Previous studies sugges...

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Autores principales:	G. Ligat, C. Jacquet, S. Chou, A. Couvreux, S. Alain, S. Hantz
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4759118bc283476584e1bb58514fcdb1
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spelling	oai:doaj.org-article:4759118bc283476584e1bb58514fcdb12021-12-02T16:08:12ZIdentification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit10.1038/s41598-017-09469-72045-2322https://doaj.org/article/4759118bc283476584e1bb58514fcdb12017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-09469-7https://doaj.org/toc/2045-2322Abstract The human cytomegalovirus (HCMV) terminase complex consists of several components acting together to cleave viral DNA into unit length genomes and translocate them into capsids, a critical process in the production of infectious virions subsequent to DNA replication. Previous studies suggest that the carboxyl-terminal portion of the pUL56 subunit interacts with the pUL89 subunit. However, the specific interacting residues of pUL56 remain unknown. We identified a conserved sequence in the C-terminal moiety of pUL56 (671WMVVKYMGFF680). Overrepresentation of conserved aromatic amino acids through 20 herpesviruses homologues of pUL56 suggests an involvement of this short peptide into the interaction between the larger pUL56 terminase subunit and the smaller pUL89 subunit. Use of Alpha technology highlighted an interaction between pUL56 and pUL89 driven through the peptide 671WMVVKYMGFF680. A deletion of these residues blocks viral replication. We hypothesize that it is the consequence of the disruption of the pUL56-pUL89 interaction. These results show that this motif is essential for HCMV replication and could be a target for development of new small antiviral drugs or peptidomimetics.G. LigatC. JacquetS. ChouA. CouvreuxS. AlainS. HantzNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q G. Ligat C. Jacquet S. Chou A. Couvreux S. Alain S. Hantz Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit
description	Abstract The human cytomegalovirus (HCMV) terminase complex consists of several components acting together to cleave viral DNA into unit length genomes and translocate them into capsids, a critical process in the production of infectious virions subsequent to DNA replication. Previous studies suggest that the carboxyl-terminal portion of the pUL56 subunit interacts with the pUL89 subunit. However, the specific interacting residues of pUL56 remain unknown. We identified a conserved sequence in the C-terminal moiety of pUL56 (671WMVVKYMGFF680). Overrepresentation of conserved aromatic amino acids through 20 herpesviruses homologues of pUL56 suggests an involvement of this short peptide into the interaction between the larger pUL56 terminase subunit and the smaller pUL89 subunit. Use of Alpha technology highlighted an interaction between pUL56 and pUL89 driven through the peptide 671WMVVKYMGFF680. A deletion of these residues blocks viral replication. We hypothesize that it is the consequence of the disruption of the pUL56-pUL89 interaction. These results show that this motif is essential for HCMV replication and could be a target for development of new small antiviral drugs or peptidomimetics.
format	article
author	G. Ligat C. Jacquet S. Chou A. Couvreux S. Alain S. Hantz
author_facet	G. Ligat C. Jacquet S. Chou A. Couvreux S. Alain S. Hantz
author_sort	G. Ligat
title	Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit
title_short	Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit
title_full	Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit
title_fullStr	Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit
title_full_unstemmed	Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit
title_sort	identification of a short sequence in the hcmv terminase pul56 essential for interaction with pul89 subunit
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/4759118bc283476584e1bb58514fcdb1
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Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunit

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