Point mutation in calcium-binding domain of mouse polyomavirus VP1 protein does not prevent virus-like particle formation, but changes VP1 interactions with Saccharomyces cerevisiae cell structures

  • Adamec T
  • Palková Z
  • Velková K
 et al. 
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Abstract

The mouse polyomavirus gene for the major structural protein, VP1, with point mutation in the calcium-binding pocket (VP1Ala), was expressed in Saccharomyces cerevisiae and in a baculovirus expression system. Surprisingly, VP1Alaforms virus-like particles (VLPs) in nuclei of both yeast and insect cells. VP1Ala-VLPs produced in S. cerevisiae are unstable and, unlike wild-type VP1 (VP1wt)-VLPs, they disassemble during the purification procedure and storage. In contrast to VP1wt, VP1Aladoes not interact with the yeast mitotic spindle. Nevertheless, both wild-type and mutated VP1 inhibit yeast cell growth. The inhibition is cAMP-dependent. The production of VP1Alaand VP1wt-VLPs in insect cells also revealed differences in their interactions with cellular protein(s). Thus, the mutation in the VP1 calcium pocket alters the stability and surface conformation of VLPs rather than the ability of VP1 to self-assemble. © 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

Author-supplied keywords

  • Baculovirus
  • Heterologous expression
  • Polyomavirus VP1
  • Saccharomyces cerevisiae

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Authors

  • Tomáš Adamec

  • Zdena Palková

  • Klára Velková

  • Jitka Štokrová

  • Jitka Forstová

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