5fmo

Publication Abstract from PubMed

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 A 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.

Crystal Structure and Proteomics Analysis of Empty Virus-like Particles of Cowpea Mosaic Virus.,Huynh NT, Hesketh EL, Saxena P, Meshcheriakova Y, Ku YC, Hoang LT, Johnson JE, Ranson NA, Lomonossoff GP, Reddy VS Structure. 2016 Apr 5;24(4):567-75. doi: 10.1016/j.str.2016.02.011. Epub 2016 Mar, 24. PMID:27021160^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.