HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 15, 10164-10173, April 14, 2006

This Article Full Text Full Text (PDF) All Versions of this Article: 281/15/10164    most recent M511261200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kawano, M.-a. Articles by Handa, H. Search for Related Content PubMed PubMed Citation Articles by Kawano, M.-a. Articles by Handa, H. Social Bookmarking                      What's this?

The VP2/VP3 Minor Capsid Protein of Simian Virus 40 Promotes the in Vitro Assembly of the Major Capsid Protein VP1 into Particles^*

Masa-aki Kawano, Takamasa Inoue, Hiroko Tsukamoto, Tatsuya Takaya, Teruya Enomoto, Ryou-u Takahashi, Naoki Yokoyama, Noriaki Yamamoto, Akira Nakanishi, Takeshi Imai, Tadashi Wada, Kohsuke Kataoka^¶, and Hiroshi Handa¹

From the Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8503, National Institute of Longevity Sciences, Obu 474-8522, and ^¶Graduate School of Biological Science, Nara Institute of Science and Technology, Ikoma 630-0192, Japan

The SV40 capsid is composed primarily of 72 pentamers of the VP1 major capsid protein. Although the capsid also contains the minor capsid protein VP2 and its amino-terminally truncated form VP3, their roles in capsid assembly remain unknown. An in vitro assembly system was used to investigate the role of VP2 in the assembly of recombinant VP1 pentamers. Under physiological salt and pH conditions, VP1 alone remained dissociated, and at pH 5.0, it assembled into tubular structures. A stoichiometric amount of VP2 allowed the assembly of VP1 pentamers into spherical particles in a pH range of 7.0 to 4.0. Electron microscopy observation, sucrose gradient sedimentation analysis, and antibody accessibility tests showed that VP2 is incorporated into VP1 particles. The functional domains of VP2 important for VP1 binding and for enhancing VP1 assembly were further explored with a series of VP2 deletion mutants. VP3 also enhanced VP1 assembly, and a region common to VP2 and VP3 (amino acids 119-272) was required to promote VP1 pentamer assembly. These results are relevant for controlling recombinant capsid formation in vitro, which is potentially useful for the in vitro development of SV40 virus vectors.

Received for publication, October 17, 2005 , and in revised form, January 19, 2006.

^* This work was supported by a grant-in-aid for scientific research, the 21st Century COE Program of the Ministry of Education, Culture, Sports, Science, and Technology in Japan, and a grant for research and development projects in cooperation with academic institutions from the New Energy and Industrial Technology Development Organization. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-8503, Japan. Tel.: 81-45-924-5872; Fax: 81-45-924-5834; E-mail: hhanda{at}bio.titech.ac.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				H. Tsukamoto, M.-a. Kawano, T. Inoue, T. Enomoto, R.-u Takahashi, N. Yokoyama, N. Yamamoto, T. Imai, K. Kataoka, Y. Yamaguchi, et al. Evidence that SV40 VP1-DNA interactions contribute to the assembly of 40-nm spherical viral particles. Genes Cells, November 1, 2007; 12(11): 1267 - 1279. [Abstract] [Full Text] [PDF]

				N. Yokoyama, M.-a. Kawano, H. Tsukamoto, T. Enomoto, T. Inoue, R.-u Takahashi, A. Nakanishi, T. Imai, T. Wada, and H. Handa Mutational Analysis of the Carboxyl-terminal Region of the SV40 Major Capsid Protein VP1 J. Biochem., February 1, 2007; 141(2): 279 - 286. [Abstract] [Full Text] [PDF]

				M. L. Gasparovic, G. V. Gee, and W. J. Atwood JC Virus Minor Capsid Proteins Vp2 and Vp3 Are Essential for Virus Propagation. J. Virol., November 1, 2006; 80(21): 10858 - 10861. [Abstract] [Full Text] [PDF]