Blue fluorescent antibodies as reporters of steric accessibility in virus conjugates.
Nonenveloped viruses provide the chemist with large, preassembled polyvalent protein scaffolds for modification. These structures are typically porous to small molecules but not to large ones. The solution-phase structures and reactivities of such assemblies may be substantially different than indicated by X-ray crystal structures. Here, the attachment of organic compounds to either the inside or outside surface of the cowpea mosaic virus (CPMV) coat protein was verified with an indicating antibody-antigen interaction. Antibody binding was subsequently blocked by the installation of poly(ethylene glycol) chains. These results typify the type of site-specific control that is available with CPMV and related virus building blocks.
Wang
Qian
Q
Department of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA.
Raja
Krishnaswami S
KS
Janda
Kim D
KD
Lin
Tianwei
T
Finn
M G
MG
D000914:Antibodies, Viral / Q000276:immunology; D000937:Antigen-Antibody Reactions; D036022:Capsid Proteins / Q000737:chemistry* / Q000276:immunology; D017798:Comovirus / Q000737:chemistry*; D005456:Fluorescent Dyes; D008958:Models, Molecular; D009930:Organic Chemicals / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D014780:Viruses / Q000737:chemistry
D000914:Antibodies, Viral; D036022:Capsid Proteins; D005456:Fluorescent Dyes; D009930:Organic Chemicals; D011092:Polyethylene Glycols