The VP2/VP3 minor capsid protein of SV40 promotes the in vitro assembly of the major capsid protein VP1 into particles

doi:10.1074/jbc.M511261200

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Papers In Press, published online ahead of print February 14, 2006
J. Biol. Chem, 10.1074/jbc.M511261200
Submitted on October 17, 2005
Revised on January 19, 2006
Accepted on February 14, 2006

The VP2/VP3 minor capsid protein of SV40 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 Handa

Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Kanagawa 226-8503

Corresponding Author: hhanda{at}bio.titech.ac.jp

The simian virus 40 (SV40)1 capsid is composed primarily of 72 pentamers of the VP1 major capsid protein. While 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 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.

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