The Merkel cell polyomavirus minor capsid protein.

The surface of polyomavirus virions is composed of pentameric knobs of the major capsid protein, VP1. In previously studied polyomavirus species, such as SV40, two interior capsid proteins, VP2 and VP3, emerge from the virion to play important roles during the infectious entry process. Translation o...

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Autores principales:	Rachel M Schowalter, Christopher B Buck
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/de0d2acb4a8d419eb85da9eaa010620d
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spelling	oai:doaj.org-article:de0d2acb4a8d419eb85da9eaa010620d2021-11-18T06:07:45ZThe Merkel cell polyomavirus minor capsid protein.1553-73661553-737410.1371/journal.ppat.1003558https://doaj.org/article/de0d2acb4a8d419eb85da9eaa010620d2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23990782/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The surface of polyomavirus virions is composed of pentameric knobs of the major capsid protein, VP1. In previously studied polyomavirus species, such as SV40, two interior capsid proteins, VP2 and VP3, emerge from the virion to play important roles during the infectious entry process. Translation of the VP3 protein initiates at a highly conserved Met-Ala-Leu motif within the VP2 open reading frame. Phylogenetic analyses indicate that Merkel cell polyomavirus (MCV or MCPyV) is a member of a divergent clade of polyomaviruses that lack the conserved VP3 N-terminal motif. Consistent with this observation, we show that VP3 is not detectable in MCV-infected cells, VP3 is not found in native MCV virions, and mutation of possible alternative VP3-initiating methionine codons did not significantly affect MCV infectivity in culture. In contrast, VP2 knockout resulted in a >100-fold decrease in native MCV infectivity, despite normal virion assembly, viral DNA packaging, and cell attachment. Although pseudovirus-based experiments confirmed that VP2 plays an essential role for infection of some cell lines, other cell lines were readily transduced by pseudovirions lacking VP2. In cell lines where VP2 was needed for efficient infectious entry, the presence of a conserved myristoyl modification on the N-terminus of VP2 was important for its function. The results show that a single minor capsid protein, VP2, facilitates a post-attachment stage of MCV infectious entry into some, but not all, cell types.Rachel M SchowalterChristopher B BuckPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 8, p e1003558 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Rachel M Schowalter Christopher B Buck The Merkel cell polyomavirus minor capsid protein.
description	The surface of polyomavirus virions is composed of pentameric knobs of the major capsid protein, VP1. In previously studied polyomavirus species, such as SV40, two interior capsid proteins, VP2 and VP3, emerge from the virion to play important roles during the infectious entry process. Translation of the VP3 protein initiates at a highly conserved Met-Ala-Leu motif within the VP2 open reading frame. Phylogenetic analyses indicate that Merkel cell polyomavirus (MCV or MCPyV) is a member of a divergent clade of polyomaviruses that lack the conserved VP3 N-terminal motif. Consistent with this observation, we show that VP3 is not detectable in MCV-infected cells, VP3 is not found in native MCV virions, and mutation of possible alternative VP3-initiating methionine codons did not significantly affect MCV infectivity in culture. In contrast, VP2 knockout resulted in a >100-fold decrease in native MCV infectivity, despite normal virion assembly, viral DNA packaging, and cell attachment. Although pseudovirus-based experiments confirmed that VP2 plays an essential role for infection of some cell lines, other cell lines were readily transduced by pseudovirions lacking VP2. In cell lines where VP2 was needed for efficient infectious entry, the presence of a conserved myristoyl modification on the N-terminus of VP2 was important for its function. The results show that a single minor capsid protein, VP2, facilitates a post-attachment stage of MCV infectious entry into some, but not all, cell types.
format	article
author	Rachel M Schowalter Christopher B Buck
author_facet	Rachel M Schowalter Christopher B Buck
author_sort	Rachel M Schowalter
title	The Merkel cell polyomavirus minor capsid protein.
title_short	The Merkel cell polyomavirus minor capsid protein.
title_full	The Merkel cell polyomavirus minor capsid protein.
title_fullStr	The Merkel cell polyomavirus minor capsid protein.
title_full_unstemmed	The Merkel cell polyomavirus minor capsid protein.
title_sort	merkel cell polyomavirus minor capsid protein.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/de0d2acb4a8d419eb85da9eaa010620d
work_keys_str_mv	AT rachelmschowalter themerkelcellpolyomavirusminorcapsidprotein AT christopherbbuck themerkelcellpolyomavirusminorcapsidprotein AT rachelmschowalter merkelcellpolyomavirusminorcapsidprotein AT christopherbbuck merkelcellpolyomavirusminorcapsidprotein
_version_	1718424570125352960

The Merkel cell polyomavirus minor capsid protein.

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