Natural supramolecular building blocks. Wild-type cowpea mosaic virus.
Cowpea mosaic virus (CPMV) can be isolated in gram quantities, possesses a structure that is known to atomic resolution, and is quite stable. It is therefore of potential use as a molecular entity in synthesis, particularly as a building block on the nanochemical scale. CPMV was found to possess a lysine residue with enhanced reactivity in each asymmetric unit, and thus 60 such lysines per virus particle. The identity of this residue was established by a combination of acylation, protein digestion, and mass spectrometry. Under forcing conditions, up to four lysine residues per asymmetric unit can be addressed. In combination with engineered cysteine reactivity described in the accompanying paper, this provides a powerful platform for the alteration of the chemical and physical properties of CPMV particles.
Wang
Qian
Q
Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Kaltgrad
Eiton
E
Lin
Tianwei
T
Johnson
John E
JE
Finn
M G
MG
D001360:Avidin / Q000737:chemistry / Q000378:metabolism; D001710:Biotin / Q000031:analogs & derivatives / Q000378:metabolism; D002625:Chemistry, Organic / Q000379:methods; D002853:Chromatography, Liquid / Q000379:methods; D017798:Comovirus / Q000737:chemistry* / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D019793:Fluorescein / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008239:Lysine / Q000032:analysis / Q000737:chemistry*; D008854:Microscopy, Electron; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014461:Ultracentrifugation / Q000379:methods
D021122:Protein Subunits; D001360:Avidin; D001710:Biotin; D008239:Lysine; D019793:Fluorescein