Journal
VIROLOGY
Volume 393, Issue 2, Pages 329-337Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2009.08.023
Keywords
Cowpea mosaic virus; Virus-like particle; Empty particle; Coat protein precursor; Proteolytic processing; Insect cell expression; Transient expression
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Funding
- Marie Curie Early Stage Training Fellowship [MEST-CT-2004-504273]
- John Innes Foundation
- EU [KBBE-227056]
- Biotechnology and Biological Science Research Council (BBSRC) UK
- Biotechnology and Biological Sciences Research Council [BBS/E/J/000CA374, BBS/E/J/00000166] Funding Source: researchfish
- BBSRC [BBS/E/J/000CA374] Funding Source: UKRI
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To elucidate the mechanism of formation of cowpea mosaic virus (CPMV) particles, RNA-2-encoded precursor proteins were expressed in Spodoptera frugiperda cells. Processing of the 105K and 95K polyproteins in trans to give the mature Large (L) and Small (S) coat proteins required both the 32K proteinase cofactor and the 24K proteinase itself, while processing of VP60, consisting of the fused L-S protein, required only the 24K proteinase. Release of the L and S proteins resulted in the formation of virus-like particles (VLPs), showing that VP60 can act as a precursor of virus capsids. Processing of VP60 expressed in plants also led to efficient production of VLPs. Analysis of the VLPs produced by the action of the 24K proteinase on precursors showed that they were empty (RNA-free). This has important implications for the use of CPMV VLPs in biotechnology and nanotechnology as it will permit the use of noninfectious particles. (C) 2009 Elsevier Inc. All rights reserved.
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