Zobrazeno 1 - 10
of 14
pro vyhledávání: '"O. P. Vostrikova"'
Publikováno v:
Вестник войск РХБ защиты, Vol 3, Iss 4, Pp 350-372 (2023)
The purpose of the study is to summarize our own data and literature data on the significance of poreforming proteins of the outer membrane of Yersinia as factors of their pathogenicity and as diagnostic and protective antigens, and their role in pat
Externí odkaz:
https://doaj.org/article/237443ead8ec4f259ba4a28c36e6b8e3
Autor:
V. A. Khomenko, Olga D. Novikova, N. Yu. Kim, Marina Isaeva, O. P. Vostrikova, Galina N. Likhatskaya, Tamara F. Solov'eva
Publikováno v:
Biochemistry (Moscow). 78:496-504
OmpC-like porin was isolated from the outer membrane (OM) of Yersinia enterocolitica cultured at 37°C (the "warm" variant) and its physicochemical and functional properties were studied. The amino acid sequence of OmpC porin was established, and the
Autor:
V. A. Khomenko, Olga D. Novikova, Tamara F. Solov'eva, O. V. Sidorova, O. P. Vostrikova, O. Yu. Portnyagina
Publikováno v:
Russian Journal of Bioorganic Chemistry. 36:713-721
Multiple antigenic peptides (MAPs) that included the common antigenic epitopes of porins from the outer membranes (OM) of bacteria from the Yersinia genus (Y. pseudotuberculosis, Y. enterocolitica, and Y. pestis that are pathogenic for humans) were s
Publikováno v:
Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology. 3:438-446
The diagnostic test system based on a species-specific antigen, pore-forming protein from the outer membrane of Yersinia enterocolitica, for yersiniosis verification by the method of ELISA has been developed and approved. The proposed ELISA test syst
Autor:
V. A. Khomenko, Olga D. Novikova, N. Yu. Kim, Tamara F. Solov'eva, V. I. Emel’yanenko, O. P. Vostrikova, Galina N. Likhatskaya, S. M. Kuznetsova
Publikováno v:
Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology. 1:145-153
The changes in the structural and functional properties of yersinin, a porin from the outer membrane of Yersinia pseudotuberculosis, were studied in the pH range 8.0–2.0 using SDs-PAGE, scanning microcalorimetry, optical spectroscopy and bilayer li
Autor:
Vakorina Ti, O. P. Vostrikova, Likhatskaia Gn, Konstantin V. Guzev, V. A. Khomenko, Olga D. Novikova, Kim NIu, Tamara F. Solov'eva
Publikováno v:
Russian Journal of Bioorganic Chemistry. 32:333-344
The molecular organization and functional activity of porins isolated from the outer membrane (OM) of the Yersinia enterocolitica and three phylogenetically close nonpathogenic Yersinia species (Y. intermedia, Y. kristensenii, and Y. frederiksenii) c
Publikováno v:
Bulletin of Experimental Biology and Medicine. 128:1035-1038
The dynamics of immune response to pore-forming protein isolated from the outer membrane ofYersinia pseudotuberculosis was studied on CBA and BALB/c mice. Experiments revealed a waveform curves of antibody levels to different porin forms reflecting t
Autor:
O. Yu. Portnyagina, V. A. Khomenko, Olga D. Novikova, Tamara F. Solov'eva, Yu. S. Ovodov, O. P. Vostrikova
Publikováno v:
Bulletin of Experimental Biology and Medicine. 121:593-596
The pore-forming proteins porins isolated fromYersinia pseudotuberculosis andY. enterocolitica outer membranes and purified were found, by means of enzyme-linked immunosorbent assays, to be genus-specific antigens. Antiporin antibodies were detected
Autor:
O Iu, Portniagina, O V, Sidorova, O D, Novikova, O P, Vostrikova, V A, Khomenko, T F, Solov'eva
Publikováno v:
Bioorganicheskaia khimiia. 36(6)
Multiple antigenic peptides (MAPs), a sequence which include common antigenic epitopes of outer membrane porins (OM) bacteria of the genus Yersinia (Y. pseudotuberculosis, Y. enterocolitica, Y. pestis), pathogenic for humans have been synthesized. Af
Autor:
O. P. Vostrikova, O. Yu. Portnyagina, T. F. Solovjeva, O. V. Sidorova, V. A. Khomenko, Olga D. Novikova
Publikováno v:
Bulletin of experimental biology and medicine. 148(1)
We studied the capacity of outer membrane pore-forming recombinant protein from Yersinia pseudotuberculosis to initiate the development of immune response in CBA mice. Immunization with the recombinant protein induces the production of IgG antibodies