J Virol Methods 2015 Dec 2;225:23-9. Epub 2015 Sep 2.
Biomolecular Diversity Laboratory, Unidad de Genómica Avanzada, Centro de Investigación y Estudios Avanzados del Instituto Politécnico Nacional, Unidad Irapuato, Mexico. Electronic address:
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BMC Biotechnol 2015 Aug 27;15:80. Epub 2015 Aug 27.
Laboratory of Virology, Wageningen University, Droevendaalsesteeg 1, 6708 PB, Wageningen, The Netherlands.
Background & Methods: Within the last decade Virus-Like Particles (VLPs) have increasingly received attention from scientists for their use as a carrier of (peptide) molecules or as scaffold to present epitopes for use in subunit vaccines. To test the feasibility of Cowpea chlorotic mottle virus (CCMV) particles as a scaffold for epitope presentation and identify sites for epitope fusion or insertion that would not interfere with virus-like-particle formation, chimeric CCMV coat protein (CP) gene constructs were engineered, followed by expression in E. coli and assessment of VLP formation. Read More
J Gen Virol 2004 Apr;85(Pt 4):1049-53
Department of Plant Sciences and Plant Pathology, Montana State University, Bozeman, MT 59717, USA.
We have developed methods for producing viral-based protein cages in high yield that are amenable to genetic modification. Expression of the structural protein of Cowpea chlorotic mottle bromovirus (CCMV) using the yeast-based Pichia pastoris heterologous expression system resulted in the assembly of particles that were visibly indistinguishable from virus particles produced in the natural host. We have shown that a collection of non-infectious CCMV coat protein mutants expressed in the P. Read More
J Mol Biol 2014 Mar 19;426(5):1050-60. Epub 2013 Oct 19.
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA; California NanoSystems Institute, and Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA. Electronic address:
The strength of attraction between capsid proteins (CPs) of cowpea chlorotic mottle virus (CCMV) is controlled by the solution pH. Additionally, the strength of attraction between CP and the single-stranded RNA viral genome is controlled by ionic strength. By exploiting these properties, we are able to control and monitor the in vitro co-assembly of CCMV CP and single-stranded RNA as a function of the strength of CP-CP and CP-RNA attractions. Read More
Virol J 2016 11 29;13(1):196. Epub 2016 Nov 29.
Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, 44270, Guadalajara, Jalisco, Mexico.
Background: Assembly of recombinant capsid proteins into virus-like particles (VLPs) still represents an interesting challenge in virus-based nanotechnologies. The structure of VLPs has gained importance for the development and design of new adjuvants and antigen carriers. The potential of Tobacco etch virus capsid protein (TEV CP) as adjuvant has not been evaluated to date. Read More