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

FEMS Yeast Res. 2005 Feb;5(4-5):331-40. doi: 10.1016/j.femsyr.2004.10.012.


The mouse polyomavirus gene for the major structural protein, VP1, with point mutation in the calcium-binding pocket (VP1(Ala)), was expressed in Saccharomyces cerevisiae and in a baculovirus expression system. Surprisingly, VP1(Ala) forms virus-like particles (VLPs) in nuclei of both yeast and insect cells. VP1(Ala)-VLPs produced in S. cerevisiae are unstable and, unlike wild-type VP1 (VP1(wt))-VLPs, they disassemble during the purification procedure and storage. In contrast to VP1(wt), VP1(Ala) does 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 VP1(Ala) and VP1(wt)-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Baculoviridae / genetics
  • Baculoviridae / metabolism
  • Calcium / metabolism*
  • Capsid Proteins / chemistry*
  • Capsid Proteins / genetics
  • Cells, Cultured
  • Mice
  • Point Mutation*
  • Polyomavirus / genetics
  • Polyomavirus / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Spindle Apparatus / metabolism
  • Spodoptera
  • Tubulin / metabolism
  • Virion / metabolism*
  • Virus Assembly


  • Capsid Proteins
  • Tubulin
  • VP1 protein, polyomavirus
  • Calcium