Abstract
Cowpea mosaic virus is composed of 60 identical copies of a two-subunit protein organized in pentameric assemblies around the icosahedral 5-fold symmetry axis. Treatment of the virus with the Ni(II) complex of the tripeptide GGH and a peroxide oxidant, or irradiation in the presence of Ru(bpy)(3)(2+) and persulfate generates covalent crosslinks across the pentameric subunit boundaries, effectively stitching the subunits together. Intersubunit crosslinking was found to occur exclusively at adjacent tyrosine residues (Y52-Y103), as predicted from the X-ray crystal structure of the capsid, and to be more extensive with the photochemical ruthenium system. The Ni/GGH oxidative procedure was also used to make covalent attachments to the virion by trapping with a functionalized disulfide reagent.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Capsid Proteins / antagonists & inhibitors
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Capsid Proteins / chemistry*
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Capsid Proteins / genetics
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Capsid Proteins / metabolism*
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Comovirus / chemistry
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Comovirus / genetics
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Comovirus / metabolism
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Cross-Linking Reagents / chemistry*
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Crystallography, X-Ray
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Cysteine / metabolism
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Hydrogen-Ion Concentration
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Models, Molecular
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Molecular Structure
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Mutation / genetics
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Nickel / chemistry
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Oxidation-Reduction
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Peptides / chemistry
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Peptides / metabolism
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Photochemistry
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Phthalic Acids / chemistry
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Protein Structure, Quaternary
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Ruthenium / chemistry
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Spectrum Analysis
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Temperature
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Tyrosine / genetics
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Tyrosine / metabolism*
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Virion / chemistry
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Virion / metabolism
Substances
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Capsid Proteins
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Cross-Linking Reagents
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Peptides
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Phthalic Acids
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Tyrosine
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Nickel
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Ruthenium
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Cysteine
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magnesium monoperoxyphthalate