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Journal of Biochemistry Advance Access originally published online on February 5, 2007
Journal of Biochemistry 2007 141(2):279-286; doi:10.1093/jb/mvm038
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© 2007 The Japanese Biochemical Society.

Mutational Analysis of the Carboxyl-terminal Region of the SV40 Major Capsid Protein VP1

Naoki Yokoyama1, Masa-aki Kawano1, Hiroko Tsukamoto1, Teruya Enomoto1, Takamasa Inoue1, Ryou-u Takahashi1, Akira Nakanishi2, Takeshi Imai2, Tadashi Wada1,3 and Hiroshi Handa1,*

1Graduate School of Bioscience and Biotechnology, and 3Integrated Research Institute, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8503, Japan; and 2National Institute of Longevity Sciences, 36-3 Gengo, Morioka-machi, Obu 474-8511, Japan

*To whom correspondence should be addressed. Tel: +81-45-924-5872, Fax: +81-45-924-5834, E-mail: hhanda{at}bio.titech.ac.jp

Received November 21, 2006; Accepted December 10, 2006


  Abstract

Virus-like particles (VLPs), a promising next-generation drug delivery vehicle, can be formed in vitro using a recombinant viral capsid protein VP1 from SV40. Seventy-two VP1 pentamers interconnect to form the T = 7d lattice of SV40 capsids, through three types of C-terminal interactions, {alpha}-{alpha}'-{alpha}'', ß-ß' and {gamma}-{gamma}. These appear to require VP1 conformational switch, which involve in particular the region from amino acids 301–312 (herein Region I). Here we show that progressive deletions from the C-terminus of VP1, up to 34 amino acids, cause size and shape variations in the resulting VLPs, including tubular formation, whereas deletions beyond 34 amino acids simply blocked VP1 self-assembly. Mutants carrying in Region I point mutations predicted to disrupt {alpha}-{alpha}'-{alpha}''-type and/or ß-ß'-type interactions formed small VLPs resembling T = 1 symmetry. Chimeric VP1, in which Region I of SV40 VP1 was substituted with the homologous region from VP1 of other polyomaviruses, assembled only into small VLPs. Together, our results show the importance of the integrity of VP1 C-terminal region and the specific amino acid sequences within Region I in the assembly of normal VLPs. By understanding how to alter VLP sizes and shapes contributes to the development of drug delivery systems using VLPs.

Key Words: baculovirus, carboxyl-terminal of VP1, self-assembly, simian virus 40, virus-like particles


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H. Tsukamoto, M.-a. Kawano, T. Inoue, T. Enomoto, R.-u Takahashi, N. Yokoyama, N. Yamamoto, T. Imai, K. Kataoka, Y. Yamaguchi, et al.
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