[Native and renatured oligomer-dependent epitopes of intracellular influenza virus nucleocapsid protein].
Intracellular NP oligomers have been shown to react with some anti-NP monoclonal antibodies (mAbs) in radio-immnoprecipitation, immunoblotting, and dot immunoassay. Soluble NP monomers obtained after thermal dissociation of NP oligomers are not recognized by mAbs unlike the NP monomers whose concentration increased by about 100-fold due to transfer to the nitrocellulose membrane after polyacrylamide gel electrophoresis. The findings demonstrated that in the intact NP oligomers there were epitopes determined by their quaternary structure. These oligomer-dependent epitopes may be renaturated in vitro under the conditions allowing for a concentration-dependent NP-NP association.
Semenova
N P
NP
Prokudina
E N
EN
Chumakov
V M
VM
Grigor'eva
T A
TA
Stitz
L
L
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000914:Antibodies, Viral / Q000276:immunology; D000918:Antibody Specificity; D002460:Cell Line; D004285:Dogs; D018604:Epitope Mapping; D000939:Epitopes / Q000276:immunology* / Q000378:metabolism; D006358:Hot Temperature; D015151:Immunoblotting; D053123:Influenza A Virus, H3N8 Subtype / Q000276:immunology*; D019590:Nucleocapsid Proteins / Q000276:immunology* / Q000378:metabolism; D009976:Orthomyxoviridae Infections / Q000276:immunology*; D011487:Protein Conformation; D015531:Radioimmunoprecipitation Assay; D012995:Solubility
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D000939:Epitopes; D019590:Nucleocapsid Proteins