[Comparative study of the antigenic and immunogenic properties of native and recombinant Marburg virus VP35 proteins].
Antigenic structure of Marburg virus (MBG) VP35 was compared with that of the recombinant VP35 (f35) expressed in a prokaryotic system. For this purpose, a gene encoding the full-length VP35 was cloned in vector pQE31(QIAGEN) and expressed at about 70 mg/liter culture fluid in Escherichia coli JM103 as a recombinant fusion protein f35. BALB/c mice were immunized with soluble f35 or purified inactivated virions of MBG. Antibodies cross-reacting with VP35 and f35 antigens were detected by ELISA and Western Blot analysis in immune sera. Serum from a convalescent after Marburg disease and polyclonal antibodies from animals immunized with MBG recognized f35 and the MBG VP35. VP35 and its recombinant analog induced the production of specific antiviral antibodies in mice, which cross-reacted with the studied antigens. Competitive EIA showed that VP35 and f35 cross-inhibit the antigenic reactivity with polyclonal antibodies of immune sera. Antigenic structure of f35 protein corresponded to antigenic structure of MBG VP35 protein.
Sorokin
A V
AV
Kazachinskaia
E I
EI
Kachko
A V
AV
Ivanova
A V
AV
Bukreev
A A
AA
Razumov
I A
IA
D000595:Amino Acid Sequence; D000818:Animals; D000956:Antigens, Viral / Q000276:immunology*; D015153:Blotting, Western; D003001:Cloning, Molecular; D003429:Cross Reactions; D004274:DNA, Recombinant; D004797:Enzyme-Linked Immunosorbent Assay; D029024:Marburgvirus / Q000276:immunology*; D051379:Mice; D008807:Mice, Inbred BALB C; D010957:Plasmids; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D054334:Viral Regulatory and Accessory Proteins
D000956:Antigens, Viral; D004274:DNA, Recombinant; D011994:Recombinant Proteins; C080980:VP35 protein, filovirus; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins