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...
Autores principales: | , , , , , , , , , , |
---|---|
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 |