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Size and position of truncations in the carboxy-terminal region of major capsid protein VP1 of hamster polyomavirus expressed in yeast determine its assembly capacity

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Summary.

The hamster polyomavirus major capsid protein VP1 was modified in its carboxy-terminal region by consecutive truncations and single amino acid exchanges. The ability of yeast-expressed VP1 variants to form virus-like particles (VLPs) strongly depended on the size and position of the truncation. VP1 variants lacking 21, 69, and 79 amino acid (aa) residues in their carboxy-terminal region efficiently formed VLPs similar to those formed by the unmodified VP1 (diameter 40–45 nm). In contrast, VP1 derivatives with carboxy-terminal truncations of 35 to 56 aa residues failed to form VLPs. VP1 mutants with a single A336G aa exchange or internal deletions of aa 335 to aa 346 and aa 335 to aa 363 resulted in the formation of VLPs of a smaller size (diameter 20 nm). These data indicate that certain parts of the carboxy-terminal region of VP1 are not essential for pentamer–pentamer interactions in the capsid, at least in the yeast expression system used.

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Authors and Affiliations

  1. Institute of Biotechnology, Vilnius, Lithuania

    A. Gedvilaite, E. Aleksaite & K. Sasnauskas

  2. Institute of Botany, Vilnius, Lithuania

    J. Staniulis

  3. Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute for Epidemiology, Wusterhausen, Germany

    R. Ulrich

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  1. A. Gedvilaite
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  2. E. Aleksaite
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  3. J. Staniulis
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  4. R. Ulrich
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  5. K. Sasnauskas
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Gedvilaite, A., Aleksaite, E., Staniulis, J. et al. Size and position of truncations in the carboxy-terminal region of major capsid protein VP1 of hamster polyomavirus expressed in yeast determine its assembly capacity. Arch Virol 151, 1811–1825 (2006). https://doi.org/10.1007/s00705-006-0745-8

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