Viruses: incredible nanomachines. New advances with filamentous phages

M.A. Hemminga, W.L. Vos, P.V. Nazarov, R.B.M. Koehorst, C.J.A.M. Wolfs, R.B. Spruijt, D. Stopar

Research output: Contribution to journalArticleAcademicpeer-review

64 Citations (Scopus)


During recent decades, bacteriophages have been at the cutting edge of new developments in molecular biology, biophysics, and, more recently, bionanotechnology. In particular filamentous viruses, for example bacteriophage M13, have a virion architecture that enables precision building of ordered and defect-free two and three-dimensional structures on a nanometre scale. This could not have been possible without detailed knowledge of coat protein structure and dynamics during the virus reproduction cycle. The results of the spectroscopic studies conducted in our group compellingly demonstrate a critical role of membrane embedment of the protein both during infectious entry of the virus into the host cell and during assembly of the new virion in the host membrane. The protein is effectively embedded in the membrane by a strong C-terminal interfacial anchor, which together with a simple tilt mechanism and a subtle structural adjustment of the extreme end of its N terminus provides favourable thermodynamical association of the protein in the lipid bilayer. This basic physicochemical rule cannot be violated and any new bionanotechnology that will emerge from bacteriophage M13 should take this into accou
Original languageEnglish
Pages (from-to)541-550
JournalEuropean Biophysics Journal
Issue number4
Publication statusPublished - 2010


  • major coat protein
  • transmembrane alpha-helix
  • membrane-protein
  • bacteriophage m13
  • nmr-spectroscopy
  • ff fd
  • site
  • dynamics
  • display
  • domain


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