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Your search keyword '"Kulikova, N. L."' showing total 7 results
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7 results on '"Kulikova, N. L."'

3. Structural and Functional Properties of IL-4δ2, an Alternative Splice Variant of Human IL-4

Author

Vasiliev, A. M., Vasilenko, R. N., Kulikova, N. L., Andreev, S. M., Chikileva, I. O., Puchkova, G. Y., Kosarev, I. V., Khodyakova, A. V., Khlebnikov, V. S., Ptitsyn, L. R., Shcherbakov, G. Y., Uversky, V. N., DuBuske, L. M., and Abramov, V. M.

Abstract

Structural and functional properties of recombinant IL-4δ2, a naturally occurring splice variant of human IL-4 with a deletion of the loop region 22−37, have been analyzed. IL-4δ2 has α-helical structure and most likely preserves the “up−up−down−down” topology typical of the four-helix-bundle cytokines. IL-4δ2 interacts specifically with the α chain of IL-4R and competes effectively with IL-4 for the common binding sites. Thus, IL-4δ2 may act as a regulator of the cytokine net, being the natural antagonist of IL-4. Keywords: interleukin 4 • interleukine receptor • splice variant • cytokine • four-helix-bundle cytokine

Published
2003

4. Structural and Functional Properties of Yersinia pestis Caf1 Capsular Antigen and Their Possible Role in Fulminant Development of Primary Pneumonic Plague

Author

Abramov, V. M., Vasiliev, A. M., Khlebnikov, V. S., Vasilenko, R. N., Kulikova, N. L., Kosarev, I. V., Ishchenko, A. T., Gillespie, J. R., Millett, I. S., Fink, A. L., and Uversky, V. N.

Abstract

Yersinia pestis capsular antigen Caf1 is shown to be a β-structural protein that in polymeric form possesses very high conformational stability. Different approaches show that a dimer is the minimal cooperative block of Caf1 adhesin. Caf1 dimer interacts effectively with IL-1 receptors of human macrophage and epithelial cells. The specificity of such interaction is confirmed by the inhibition of IL-1α binding by Caf1. The Caf1 role in pneumonic plague pathogenesis is discussed. Keywords: bubonic plague • pneumonic plague • capsular antigen Caf1 • molecular adhesin • conformational stability

Published
2002
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6. [Production of mycobacterial antigenes merged with cellulose binding protein domain in order to produce subunit vaccines against tuberculosis].

Author

Sergienko OV, Liashchuk AM, Aksenova EI, Galushkina ZM, Poletaeva NN, Sharapova NE, Semikhin AS, Kotnova AR, Veselov AM, Bashkirov VN, Kulikova NL, Khlebnikov VS, Kondrat'eva TK, Kariagina-Zhulina AS, Apt AS, Lunin VG, and Gintsburg AL

Subjects
Antigens, Bacterial chemistry, Antigens, Bacterial immunology, Base Sequence, Cloning, Molecular, Humans, Molecular Sequence Data, Protein Structure, Tertiary, Tuberculosis microbiology, Tuberculosis prevention & control, Antigens, Bacterial genetics, Genes, Bacterial genetics, Mycobacterium tuberculosis genetics, Recombinant Fusion Proteins genetics, Tuberculosis genetics, Tuberculosis Vaccines genetics, Tuberculosis Vaccines immunology, Vaccines, Subunit genetics, Vaccines, Subunit immunology
Abstract

Protein genes Ag85A, Esat-6, and Cfp10 of Mycobacterium tuberculosis were sequenced using the database GenBank to implement selection and synthesis of primer pairs of given genes. PCR was used to obtain target amplicons of the genes. Chromosome DNA of M. tuberculosis H37Rv was used as the DNA amplification matrix. The PCR products were obtained using the plasmid pQE6, cloned, and amplified in the Escherichia coli M15 strain. Chimere products containing mycobacterial genes and cellulose binding protein domain (CBD), were obtained using the plasmid treated with restriction endonucleases. CBD fragment obtained using similar treatment of the ptt10 plasmid. The plasmids containing merged sequences of mycobacterial genes-antigenes and CBD were selected. The 3 mycobacterial genes were expressed in the E. coli M15 cells resulting in biosynthesis of corresponding recombinant proteins of expected molecular weight. Concentration of CBD, Cfp10-CBD, Ag85A-CBD, and ESAT6-CBD was 20%, 15%, and 15% total protein, respectively. The resulting chimere proteins provide high affinity for cellulose and high stability. Immobilization of CBD-containing recombinant proteins proceeds as one-stage process providing target protein purification and adsorption on cellulose. The vaccines produced using this technology are inexpensive because of low cost of cellulose sorbents as well as simultaneous use of cellulose for purification and immobilization of protein. Many cellulose preparations are not toxic, biocompatible, and widely used in medicine.

Published
2012

7. Structural and functional similarity between Yersinia pestis capsular protein Caf1 and human interleukin-1 beta.

Author

Abramov VM, Vasiliev AM, Vasilenko RN, Kulikova NL, Kosarev IV, Khlebnikov VS, Ishchenko AT, MacIntyre S, Gillespie JR, Khurana R, Korpela T, Fink AL, and Uversky VN

Subjects
3T3 Cells, Anilino Naphthalenesulfonates chemistry, Animals, Chromatography, Gel, Circular Dichroism, Exoribonucleases, Fibroblasts metabolism, Humans, Interleukin-1 metabolism, Mice, Protein Binding, Protein Conformation, Protein Structure, Secondary, Repressor Proteins, Ribonucleases, Spectrometry, Fluorescence, Spectroscopy, Fourier Transform Infrared, Structure-Activity Relationship, Thermodynamics, Transcription Factors metabolism, Ultracentrifugation, Interleukin-1 chemistry, Interleukin-1 physiology, Proteins, Transcription Factors chemistry, Transcription Factors physiology, Yersinia pestis chemistry, Yersinia pestis physiology
Abstract

A comparative study of the structural and functional properties of recombinant Yersinia pestis Caf1 and human IL-1beta was performed. According to Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) data, IL-1beta and Caf1 are typical beta-structural proteins. Neither protein interacts with the hydrophobic probe ANS (8-anilino-1-naphthalenesulfonate) under physiological conditions. Specific binding of Caf1 [K(d) = (5.4 +/- 0.1) x 10(-10) M] to interleukin-1 receptors (IL-1Rs) on the surface of finite mouse fibroblasts (line NIH 3T3) was observed. Caf1 is able to inhibit high-affinity binding of (125)I-labeled IL-1beta to NIH 3T3 cells, and in the presence of Caf1, the binding of [(125)I]IL-1beta is characterized by a K(d) of (2.0 +/- 0.3) x 10(-9) M. Caf1 binding to IL-1R could reflect adhesive properties of the capsular subunits responsible for the contact of bacteria with the host immunocompetent cells. In its turn, this may represent a signal for the initiation of the expression and secretion of the proteins of Y. pestis Yop virulon. Thus, these results help to explain the importance of Caf1 in the interaction of Y. pestis with the host immune system.

Published
2001
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