A virus-based biocatalyst.
Virus particles are probably the most precisely defined nanometre-sized objects that can be formed by protein self-assembly. Although their natural function is the storage and transport of genetic material, they have more recently been applied as scaffolds for mineralization and as containers for the encapsulation of inorganic compounds. The reproductive power of viruses has been used to develop versatile analytical methods, such as phage display, for the selection and identification of (bio)active compounds. To date, the combined use of self-assembly and reproduction has not been used for the construction of catalytic systems. Here we describe a self-assembled system based on a plant virus that has its coat protein genetically modified to provide it with a lipase enzyme. Using single-object and bulk catalytic studies, we prove that the virus-anchored lipase molecules are catalytically active. This anchored biocatalyst, unlike man-made supported catalysts, has the capability to reproduce itself in vivo, generating many independent catalytically active copies.
Carette
Noëlle
N
Interactions Plante Virus, UMR GDPP, IBVM, INRA, BP 81, F-33883, Villenave d'Ornon, France.
Engelkamp
Hans
H
Akpa
Eric
E
Pierre
Sebastien J
SJ
Cameron
Neil R
NR
Christianen
Peter C M
PC
Maan
Jan C
JC
Thies
Jens C
JC
Weberskirch
Ralf
R
Rowan
Alan E
AE
Nolte
Roeland J M
RJ
Michon
Thierry
T
Van Hest
Jan C M
JC
D002384:Catalysis; D003460:Crystallization / Q000379:methods*; D046911:Macromolecular Substances / Q000737:chemistry; D008422:Materials Testing; D008968:Molecular Conformation; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D036103:Nanotechnology / Q000379:methods*; D010316:Particle Size; D013499:Surface Properties; D014771:Virion / Q000737:chemistry* / Q000648:ultrastructure*
D046911:Macromolecular Substances