5FMO

Crystal structure and proteomics analysis of empty virus like particles of Cowpea mosaic virus

Summary for 5FMO

• Entry DOI: 10.2210/pdb5fmo/pdb
• Descriptor: EMPTY VIRUS LIKE PARTICLES OF COWPEA MOSAIC VIRUS (3 entities in total)
• Functional Keywords: virus, cpmv, evlps
• Biological source: COWPEA MOSAIC VIRUS (CPMV); More
• Total number of polymer chains: 2
• Total formula weight: 65026.75

Authors

Huynh, N.,Hesketh, E.L.,Saxena, P.,Meshcheriakova, Y.,Ku, Y.C.,Hoang, L.,Johnson, J.E.,Ranson, N.A.,Lomonossoff, G.P.,Reddy, V.S. (deposition date: 2015-11-07, release date: 2016-03-09, Last modification date: 2024-01-10)

Primary citation

Huynh, N.T.,Hesketh, E.L.,Saxena, P.,Meshcheriakova, Y.,Ku, Y.,Hoang, L.T.,Johnson, J.E.,Ranson, N.A.,Lomonossoff, G.P.,Reddy, V.S.
Crystal Structure and Proteomics Analysis of Empty Virus-Like Particles of Cowpea Mosaic Virus.
Structure, 24:567-, 2016

PubMed Abstract: Empty virus-like particles (eVLPs) of Cowpea mosaic virus (CPMV) are currently being utilized as reagents in various biomedical and nanotechnology applications. Here, we report the crystal structure of CPMV eVLPs determined using X-ray crystallography at 2.3 Å resolution and compare it with previously reported cryo-electron microscopy (cryo-EM) of eVLPs and virion crystal structures. Although the X-ray and cryo-EM structures of eVLPs are mostly similar, there exist significant differences at the C terminus of the small (S) subunit. The intact C terminus of the S subunit plays a critical role in enabling the efficient assembly of CPMV virions and eVLPs, but undergoes proteolysis after particle formation. In addition, we report the results of mass spectrometry-based proteomics analysis of coat protein subunits from CPMV eVLPs and virions that identify the C termini of S subunits undergo proteolytic cleavages at multiple sites instead of a single cleavage site as previously observed.

PubMed: 27021160
DOI: 10.1016/J.STR.2016.02.011

Experimental method

X-RAY DIFFRACTION (2.3 Å)