Use of a dual-origin temperature-controlled amplifiable replicon for optimization of human interleukin-1β synthesis in Escherichia coli

Mashko, Sergey V.; Mochulsky, Andrey V.; Kotenko, Sergey V.; Lebedeva, Marina I.; Lapidus, Alla; Mochulskaya, Natalya A.; Izotova, Lara S.; Вейко, В. П.; Vinetsky, Yury P.; Ketlinsky, S.; Дебабов, В. Г.

doi:10.1016/0378-1119(91)90060-o

Cited by 7 publications

(5 citation statements)

References 26 publications

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“…Recombinant hIL-lfl was purified as described by Mashko et al [18] and iodinated using the chloramine-T method [19] to a specific activity of 80 Ci/mole. 16 to 18 h cultures of HB101/pl2R were washed in LB and resuspended in 50 mM Tris-HCl pH 7.2, 150 mM NaCI containing 1 mM PMSF (TSP-buffer).…”

Section: Kinetics Of Ll-l~ Bindingmentioning

confidence: 99%

Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

et al. 1995

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Section: Kinetics Of Ll-l~ Bindingmentioning

confidence: 99%

Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

et al. 1995

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“…The plasmids pET-TGATG-hLI-1R and pPR-TGATG-hLI-1β-tsr have been described previously. 18 Cell Cultures and Growth Conditions. The TEC2.HS human thymic epithelial cell line and the U-937 macrophage cell line were supplied from the Institute of Immunology, Moscow.…”

Section: Methodsmentioning

confidence: 99%

“…The pFM1 plasmid contained two genes, encoding Caf1 and Caf1M proteins under the control of tac- promoter. The plasmids pET-TGATG-hLI-1α and pPR-TGATG-hLI-1β-tsr have been described previously …”

Section: Methodsmentioning

confidence: 99%

“…Human recombinant IL-1α and IL-1β were produced by E. coli BL21(DE3) and E. coli C600, respectively, transformed by the plasmids pET-TGATG-hLI-1α or pPR-TGATG-hLI-1β-tsr . Recombinant IL-1α or IL-1β was purified by gel filtraion, ion-exchange chromatography, and high-pressure liquid chromatography , to greater than 98%. The biological activities of purified proteins detected by murine thymocyte proliferative responses were 1 × 10 8 U per 1 mg of the protein.…”

Section: Methodsmentioning

confidence: 99%

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

et al. 2002

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Yersinia pestis capsular antigen Caf1 is shown to be a beta-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-1alpha binding by Caf1. The Caf1 role in pneumonic plague pathogenesis is discussed.

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“…Recombinant human IL-1β was produced by E. coli C600 cells transformed with the plasmid (pPR-TGATG-hLI-1b̃tsr), containing cDNA of IL-1β, and purified by gel filtration, ion exchange chromatography, and high-pressure liquid chromatography ( , ).…”

Section: Methodsmentioning

confidence: 99%

Structural and Functional Similarity between Yersinia pestis Capsular Protein Caf1 and Human Interleukin-1β

et al. 2001

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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.

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Use of a dual-origin temperature-controlled amplifiable replicon for optimization of human interleukin-1β synthesis in Escherichia coli

Cited by 7 publications

References 26 publications

Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis

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

Structural and Functional Similarity between Yersinia pestis Capsular Protein Caf1 and Human Interleukin-1β

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