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Peptide‐Controlled Access to the Interior Surface of Empty Virus Nanoparticles
Author(s) -
Sainsbury Frank,
Saunders Keith,
Aljabali Alaa A. A.,
Evans David J.,
Lomonossoff George P.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100482
Subject(s) - cowpea mosaic virus , capsid , peptide , chemistry , virus like particle , nanoparticle , rational design , nanotechnology , c terminus , virus , amino acid , biophysics , biochemistry , materials science , virology , biology , plant virus , recombinant dna , gene
The structure of Cowpea mosaic virus (CPMV) is known to high resolution, thereby enabling the rational use of the particles in diverse applications, from vaccine design to nanotechnology. A recently devised method for the production of empty virus‐like particles (eVLPs) has opened up new possibilities for CPMV capsid‐based technologies, such as internal mineralisation of the particle. We have investigated the role of the carboxyl (C) terminus of the small coat (S) protein in controlling access to the interior of CPMV eVLPs by determining the efficiency of internal mineralisation. The presence of the C‐terminal 24‐amino acid peptide of the S protein was found to inhibit internal mineralisation, an effect that could be eliminated by enzymatic removal of this region. We have also demonstrated the amenability of the C terminus to genetic modification. Substitution with six histidine residues generated stable particles and facilitated external mineralisation by cobalt. These findings demonstrate consistent internal and external mineralisation of CPMV, and will aid the further exploration and development of the use of eVLPs for bionanotechnological and medical applications.