Cargando…

SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes

The icosahedral capsid structure of simian virus 40 (diameter, 45 nm) consists of 72 pentameric subunits, with each subunit formed by five VP1 molecules. Electron microscopy, immuno-gold labeling, and ζ-potential analysis showed that purified recombinant VP1 pentamers covered polystyrene beads measu...

Descripción completa

Detalles Bibliográficos
Autores principales: Kawano, Masaaki, Doi, Koji, Fukuda, Hajime, Kita, Yoshinori, Imai, Kensuke, Inoue, Takamasa, Enomoto, Teruya, Matsui, Masanori, Hatakeyama, Mamoru, Yamaguchi, Yuki, Handa, Hiroshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5374266/
https://www.ncbi.nlm.nih.gov/pubmed/28435806
http://dx.doi.org/10.1016/j.btre.2014.12.008
_version_ 1782518863148089344
author Kawano, Masaaki
Doi, Koji
Fukuda, Hajime
Kita, Yoshinori
Imai, Kensuke
Inoue, Takamasa
Enomoto, Teruya
Matsui, Masanori
Hatakeyama, Mamoru
Yamaguchi, Yuki
Handa, Hiroshi
author_facet Kawano, Masaaki
Doi, Koji
Fukuda, Hajime
Kita, Yoshinori
Imai, Kensuke
Inoue, Takamasa
Enomoto, Teruya
Matsui, Masanori
Hatakeyama, Mamoru
Yamaguchi, Yuki
Handa, Hiroshi
author_sort Kawano, Masaaki
collection PubMed
description The icosahedral capsid structure of simian virus 40 (diameter, 45 nm) consists of 72 pentameric subunits, with each subunit formed by five VP1 molecules. Electron microscopy, immuno-gold labeling, and ζ-potential analysis showed that purified recombinant VP1 pentamers covered polystyrene beads measuring 100, 200, and 500 nm in diameter, as well as silica beads. In addition to covering spherical beads, VP1 pentamers covered cubic magnetite beads, as well as the distorted surface structures of liposomes. These findings indicate that VP1 pentamers could coat artificial beads of various shapes and sizes larger than the natural capsid. Technology based on VP1 pentamers may be useful in providing a capsid-like surface for enclosed materials, enhancing their stability and cellular uptake for drug delivery systems.
format Online
Article
Text
id pubmed-5374266
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-53742662017-04-21 SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes Kawano, Masaaki Doi, Koji Fukuda, Hajime Kita, Yoshinori Imai, Kensuke Inoue, Takamasa Enomoto, Teruya Matsui, Masanori Hatakeyama, Mamoru Yamaguchi, Yuki Handa, Hiroshi Biotechnol Rep (Amst) Article The icosahedral capsid structure of simian virus 40 (diameter, 45 nm) consists of 72 pentameric subunits, with each subunit formed by five VP1 molecules. Electron microscopy, immuno-gold labeling, and ζ-potential analysis showed that purified recombinant VP1 pentamers covered polystyrene beads measuring 100, 200, and 500 nm in diameter, as well as silica beads. In addition to covering spherical beads, VP1 pentamers covered cubic magnetite beads, as well as the distorted surface structures of liposomes. These findings indicate that VP1 pentamers could coat artificial beads of various shapes and sizes larger than the natural capsid. Technology based on VP1 pentamers may be useful in providing a capsid-like surface for enclosed materials, enhancing their stability and cellular uptake for drug delivery systems. Elsevier 2014-12-19 /pmc/articles/PMC5374266/ /pubmed/28435806 http://dx.doi.org/10.1016/j.btre.2014.12.008 Text en © 2014 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Kawano, Masaaki
Doi, Koji
Fukuda, Hajime
Kita, Yoshinori
Imai, Kensuke
Inoue, Takamasa
Enomoto, Teruya
Matsui, Masanori
Hatakeyama, Mamoru
Yamaguchi, Yuki
Handa, Hiroshi
SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes
title SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes
title_full SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes
title_fullStr SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes
title_full_unstemmed SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes
title_short SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes
title_sort sv40 vp1 major capsid protein in its self-assembled form allows vp1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5374266/
https://www.ncbi.nlm.nih.gov/pubmed/28435806
http://dx.doi.org/10.1016/j.btre.2014.12.008
work_keys_str_mv AT kawanomasaaki sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT doikoji sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT fukudahajime sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT kitayoshinori sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT imaikensuke sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT inouetakamasa sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT enomototeruya sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT matsuimasanori sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT hatakeyamamamoru sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT yamaguchiyuki sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes
AT handahiroshi sv40vp1majorcapsidproteininitsselfassembledformallowsvp1pentamerstocoatvarioustypesofartificialbeadsinvitroregardlessoftheirsizesandshapes