Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.

Orthohepadnavirus (mammalian hosts) and avihepadnavirus (avian hosts) constitute the family of Hepadnaviridae and differ by their capability and inability for expression of protein X, respectively. Origin and functions of X are unclear. The evolutionary analysis at issue of X indicates that present...

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Autores principales:	Formijn J van Hemert, Maarten A A van de Klundert, Vladimir V Lukashov, Neeltje A Kootstra, Ben Berkhout, Hans L Zaaijer
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9029bd7aa7b44309939203821b3b8be6
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spelling	oai:doaj.org-article:9029bd7aa7b44309939203821b3b8be62021-11-18T06:48:30ZProtein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.1932-620310.1371/journal.pone.0023392https://doaj.org/article/9029bd7aa7b44309939203821b3b8be62011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21850270/?tool=EBIhttps://doaj.org/toc/1932-6203Orthohepadnavirus (mammalian hosts) and avihepadnavirus (avian hosts) constitute the family of Hepadnaviridae and differ by their capability and inability for expression of protein X, respectively. Origin and functions of X are unclear. The evolutionary analysis at issue of X indicates that present strains of orthohepadnavirus started to diverge about 25,000 years ago, simultaneously with the onset of avihepadnavirus diversification. These evolutionary events were preceded by a much longer period during which orthohepadnavirus developed a functional protein X while avihepadnavirus evolved without X. An in silico generated 3D-model of orthohepadnaviral X protein displayed considerable similarity to the tertiary structure of DNA glycosylases (key enzymes of base excision DNA repair pathways). Similarity is confined to the central domain of MUG proteins with the typical DNA-binding facilities but without the capability of DNA glycosylase enzymatic activity. The hypothetical translation product of a vestigial X reading frame in the genome of duck hepadnavirus could also been folded into a DNA glycosylase-like 3D-structure. In conclusion, the most recent common ancestor of ortho- and avihepadnavirus carried an X sequence with orthology to the central domain of DNA glycosylase.Formijn J van HemertMaarten A A van de KlundertVladimir V LukashovNeeltje A KootstraBen BerkhoutHans L ZaaijerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 8, p e23392 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Formijn J van Hemert Maarten A A van de Klundert Vladimir V Lukashov Neeltje A Kootstra Ben Berkhout Hans L Zaaijer Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.
description	Orthohepadnavirus (mammalian hosts) and avihepadnavirus (avian hosts) constitute the family of Hepadnaviridae and differ by their capability and inability for expression of protein X, respectively. Origin and functions of X are unclear. The evolutionary analysis at issue of X indicates that present strains of orthohepadnavirus started to diverge about 25,000 years ago, simultaneously with the onset of avihepadnavirus diversification. These evolutionary events were preceded by a much longer period during which orthohepadnavirus developed a functional protein X while avihepadnavirus evolved without X. An in silico generated 3D-model of orthohepadnaviral X protein displayed considerable similarity to the tertiary structure of DNA glycosylases (key enzymes of base excision DNA repair pathways). Similarity is confined to the central domain of MUG proteins with the typical DNA-binding facilities but without the capability of DNA glycosylase enzymatic activity. The hypothetical translation product of a vestigial X reading frame in the genome of duck hepadnavirus could also been folded into a DNA glycosylase-like 3D-structure. In conclusion, the most recent common ancestor of ortho- and avihepadnavirus carried an X sequence with orthology to the central domain of DNA glycosylase.
format	article
author	Formijn J van Hemert Maarten A A van de Klundert Vladimir V Lukashov Neeltje A Kootstra Ben Berkhout Hans L Zaaijer
author_facet	Formijn J van Hemert Maarten A A van de Klundert Vladimir V Lukashov Neeltje A Kootstra Ben Berkhout Hans L Zaaijer
author_sort	Formijn J van Hemert
title	Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.
title_short	Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.
title_full	Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.
title_fullStr	Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.
title_full_unstemmed	Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.
title_sort	protein x of hepatitis b virus: origin and structure similarity with the central domain of dna glycosylase.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/9029bd7aa7b44309939203821b3b8be6
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Protein X of hepatitis B virus: origin and structure similarity with the central domain of DNA glycosylase.

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