دورية أكاديمية

The structure of myeloid cell-specific TNF inhibitors affects their biological properties.

التفاصيل البيبلوغرافية
العنوان: The structure of myeloid cell-specific TNF inhibitors affects their biological properties.
المؤلفون: Vasilenko EA; Lobachevsky State University, Nizhny Novgorod, Russia., Gorshkova EN; Lobachevsky State University, Nizhny Novgorod, Russia., Astrakhantseva IV; Lobachevsky State University, Nizhny Novgorod, Russia.; Sirius University of Science and Technology, Sochi, Russia., Drutskaya MS; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia., Tillib SV; Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia., Nedospasov SA; Sirius University of Science and Technology, Sochi, Russia.; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.; Lomonosov Moscow State University, Moscow, Russia., Mokhonov VV; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.; Blokhina Scientific Research Institute of Epidemiology and Microbiology of Nizhny Novgorod, Nizhny Novgorod, Russia.
المصدر: FEBS letters [FEBS Lett] 2020 Nov; Vol. 594 (21), pp. 3542-3550. Date of Electronic Publication: 2020 Sep 04.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-3468 (Electronic) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
أسماء مطبوعة: Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
مواضيع طبية MeSH: Myeloid Cells/*drug effects , Tumor Necrosis Factor Inhibitors/*pharmacology, Animals ; Antibodies, Bispecific/pharmacology ; Chemical and Drug Induced Liver Injury ; Galactosamine ; Humans ; Lipopolysaccharides ; Macrophages/drug effects ; Mice ; Survival Rate ; Tumor Necrosis Factor-alpha/pharmacology
مستخلص: Spatial organization and conformational changes of antibodies may significantly affect their biological functions. We assessed the effect of mutual organization of the two V H H domains within bispecific antibodies recognizing human TNF and the surface molecules of murine myeloid cells (F4/80 or CD11b) on TNF retention and inhibition. TNF-neutralizing properties in vitro and in vivo of MYSTI-2 and MYSTI-3 antibodies were compared with new variants with interchanged V H H domains and different linker sequences. The most effective structure of MYSTI-2 and MYSTI-3 proteins required the Ser/Gly-containing 'superflexible' linker. The orientation of the modules was crucial for the activity of the proteins, but not for MYSTI-3 with the Pro/Gln-containing 'semi-rigid' linker. Our results may contribute toward the development of more effective drug prototypes.
(© 2020 Federation of European Biochemical Societies.)
References: Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa EB, Bendahman N, Hamers R and Hammers C (1993) Naturally occurring antibodies devoid of light chains. Nature 363, 446-448.
Henry KA and MacKenzie CR (2018) Antigen recognition by single-domain antibodies: structural latitudes and constraints. MAbs 10, 815-826.
Efimov GA, Kruglov AA, Khlopchatnikova ZV, Rozov FN, Mokhonov VV, Rose-John S, Scheller J, Gordon S, Stacey M, Drutskaya MS, Tillib SV and Nedospasov SA (2016) Cell-type-restricted anti-cytokine therapy: TNF inhibition from one pathogenic source. Proc Natl Acad Sci USA 113, 3006-3011.
Tumanov AV, Grivennikov SI, Kruglov AA, Shebzukhov YV, Koroleva EP, Piao Y, Cui CY, Kuprash DV and Nedospasov SA (2010) Cellular source and molecular form of TNF specify its distinct functions in organization of secondary lymphoid organs. Blood 116, 3456-64.
Kruglov AA, Tumanov AV, Grivennikov SI, Shebzukhov YV, Kuchmiy AA, Efimov GA, Drutskaya MS, Scheller J, Kuprash DV and Nedospasov SA (2011) Modalities of experimental TNF blockade in vivo: mouse models. Adv Exp Med Biol 691, 421-431.
Grivennikov SI, Tumanov AV, Liepinsh DJ, Kruglov AA, Marakusha BI, Shakhov AN, Murakami T, Drutskaya LN, Forster I, Clausen BE, Tessarollo L, Ryffel B, Kuprash DV and Nedospasov SA (2005) Distinct and nonredundant in vivo functions of TNF produced by T cells and macrophages/neutrophils: protective and deleterious effects. Immunity 22, 93-104.
Allie N, Grivennikov SI, Keeton R, Hsu NJ, Bourigault ML, Court N, Fremond C, Yeremeev V, Shebzukhov Y, Ryffel B, Nedospasov SA, Quesniaux VF and Jacobs M (2013) Prominent role for T cell-derived tumour necrosis factor for sustained control of Mycobacterium tuberculosis infection. Sci Rep 3, 1809.
Olleros ML, Chavez-Galan L, Segueni N, Bourigault ML, Vesin D, Kruglov AA, Drutskaya MS, Bisig R, Ehlers S, Aly S, Walter K, Kuprash DV, Chouchkova M, Kozlov SV, Erard F, Ryffel B, Quesniaux VFJ, Nedospasov SA and Garcia I (2015) Control of mycobacterial infections in mice expressing human tumor necrosis factor (TNF) but not mouse TNF. Infect Immun 83, 3612-3623.
Kinne RW, Brauer R, Stuhlmuller B, Palombo-Kinne E and Burmester GR (2000) Macrophages in rheumatoid arthritis. Arthritis Res. 2, 189-202.
Udalova IA, Mantovani A and Feldmann M (2016) Macrophage heterogeneity in the context of rheumatoid arthritis. Nat Rev Rheumatol 12, 472.
Nosenko MA, Atretkhany KN, Mokhonov VV, Efimov GA, Kruglov AA, Tillib SV, Drutskaya MS and Nedospasov SA (2017) VHH-based bispecific antibodies targeting cytokine production. Front Immunol 8, 1073.
George R and Heringa J (2002) An analysis of protein domain linkers: their classification and role in protein folding. Protein Eng. 15, 871-879.
Arai R, Ueda H, Kitayama A, Kamiya N and Nagamune T (2001) Design of the linkers which effectively separate domains of a bifunctional fusion protein. Protein Eng 14, 529-532.
Argos P (1990) An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion. J Mol Biol. 211, 943-958.
van Leeuwen HC, Strating MJ, Rensen M, deLaat W and van der Vliet PC (1997) Linker length and composition influence the flexibility of Oct-1 DNA binding. EMBO J. 16, 2043-2053.
Robinson CR and Sauer RT (1998) Optimizing the stability of single-chain proteins by linker length and composition mutagenesis. Proc Natl Acad Sci USA 95, 5929-5934.
Dong J, Kojima T, Ohashi H and Ueda H (2015) Optimal fusion of antibody binding domains resulted in higher affinity and wider specificity. J Biosci Bioeng 120, 504-9.
Golynskiy MV, Rurup WF and Merkx M (2010) Antibody detection by using a FRET-based protein conformational switch. ChemBioChem 11, 2264-2267.
Li G, Huang Z, Zhang C, Dong B-J, Guo R-H, Yue H-W, Yan L-T and Xing X-H (2016) Construction of a linker library with widely controllable flexibility for fusion protein design. Appl Microbiol Biotechnol 100, 215-225.
Lee M, Bang K, Kwon H and Cho S (2013) Enhanced antibacterial activity of an attacin-coleoptericin hybrid protein fused with a helical linker. Mol Biol Rep 40, 3953-3960.
Silacci M, Baenziger-Tobler N, Lembke W, Zha W, Batey S, Bertschinger J and Grabulovski D (2014) Linker length matters, Fynomer-Fc fusion with an optimized linker displaying picomolar IL-17A inhibition potency. J Biol Chem 289, 14392-14398.
Haga T, Hirakawa H and Nagamune T (2013) Fine tuning of spatial arrangement of enzymes in a PCNA-mediated multienzyme complex using a rigid poly-L-proline linker. PLoS One 8, e75114.
Gramlich PA, Westbroek W, Feldman RA, Awad O, Mello N, Remington MP, Sun Y, Zhang W, Sidransky E, Betenbaugh MJ and Fishman PS (2016) A peptide-linked recombinant glucocerebrosidase for targeted neuronal delivery: design, production, and assessment. J. Biotechnol. 221, 1-12.
Matz J, Kessler P, Bouchet J, Combes O, Ramos OHP, Barin F, Baty D, Martin L, Benichou S and Chames P (2013) Straightforward selection of broadly neutralizing single-domain antibodies targeting the conserved CD4 and coreceptor binding sites of HIV-1 gp120. J Virol 87, 1137-1149.
Bencurova E, Pulzova L, Flachbartova Z and Bhide M (2015) A rapid and simple pipeline for synthesis of mRNA-ribosome-V(H)H complexes used in single-domain antibody ribosome display. Mol. Biosyst. 11, 1515-1524.
Nosenko MA, Atretkhany KN, Mokhonov VV, Vasilenko EA, Kruglov AA, Tillib SV, Drutskaya MS and Nedospasov SA (2019) Modulation of bioavailability of proinflammatory cytokines produced by myeloid cells. Semin Arthritis Rheum. 49 (3S), S39-S42.
Mokhonov VV, Vasilenko EA, Gorshkova EN, Astrakhantseva IV, Novikov DV and Novikov VV (2018) SlyD-deficient Escherichia coli strains: A highway to contaminant-free protein extraction. Biochem Biophys Res Commun. 499 (4), 967-972.
Espevik T and Nissen-Meyer J (1986) A highly sensitive cell line, WEHI 164 clone 13, for measuring cytotoxic factor/tumor necrosis factor from human monocytes. J. Immunol. Methods. 95, 99-105.
Muller M, Eugster HP, Le Hir M, Shakhov A, Di Padova F, Maurer C, Quesniaux VFJ and Ryffel B (1996) Correction or transfer of immunodeficiency due to TNF-LT alpha deletion by bone marrow transplantation. Mol. Med. 2, 247-255.
Laemmli U (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680-685.
Ibanez LI, de Filette M, Hultberg A, Verrips T, Temperton N, Weiss RA, Vandevelde W, Schepens B, Vanlandschoot P and Saelens X (2011) Nanobodies with in vitro neutralizing activity protect mice against H5N1 influenza virus infection. J Infect Dis 203, 1063-1072.
Fischer JA, Hueber AJ, Wilson S, Galm M, Baum W, Kitson C, Auer J, Lorenz SH, Moelleken J, Bader M, Tissot AC, Tan SL, Seeber S and Schett G (2015) Combined inhibition of tumor necrosis factor α and interleukin-17 as a therapeutic opportunity in rheumatoid arthritis development and characterization of a novel bispecific antibody. Arthritis Rheumatol. 67, 51-62.
Qi J, Kan F, Ye X, Guo M, Zhang Y, Ren G and Li D (2012) A bispecific antibody against IL-1β and IL-17A is beneficial for experimental rheumatoid arthritis. Int Immunopharmacol 14, 770-778.
Beirnaert E, Desmyter A, Silvia S, Lauwereys M, Aarden L, Dreier T, Loris R, Silence K, Pollet C, Cambillau C and de Haard H (2017) Bivalent Llama single-domain antibody fragments against tumor necrosis factor have picomolar potencies due to intramolecular interactions. Front. Immunol. 8, 867.
Gokhale RS, Tsuji SY, Cane DE and Khosla C (1999) Dissecting and exploiting intermodular communication in polyketide synthases. Science 284, 482-485.
Gokhale RS and Khosla C (2000) Role of linkers in communication between protein modules. Curr Opin Chem Biol 4, 22-27.
McDaniel R, Kao CM, Hwang SJ and Khosla C (1997) Engineered intermodular and intramodular polyketide synthase fusions. Chem Biol 4, 667-674.
Chen X, Zaro JL and Shen WC (2013) Fusion protein linkers: property, design and functionality. Adv Drug Deliv Rev. 65, 1357-69.
Tollefsen S, Hotta K, Chen X, Simonsen B, Swaminathan K, Mathews II, Sollid LM and Kim CY (2012) Structural and functional studies of trans-encoded HLADQ2.3 (DQA1*03:01/DQB1*02:01) protein molecule. J Biol Chem 287, 13611-13619.
Eldridge B, Cooley RN, Odegrip R, McGregor DP, Fitzgerald KJ and Ullman CG (2009) An in vitro selection strategy for conferring protease resistance to ligand binding peptides. Protein Eng Des Sel. 22, 691-698.
Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa EB, Bendahman N and Hamers R (1993) Naturally occurring antibodies devoid of light chains. Nature 363, 446-448.
Beutler B, Milsark IW and Cerami AC (1985) Passive immunization against cachectin/tumor necrosis factor protects mice from lethal effect of endotoxin. Science. 229, 869-871.
فهرسة مساهمة: Keywords: VHH; anti-TNF therapy; bispecific antibodies; linkers
المشرفين على المادة: 0 (Antibodies, Bispecific)
0 (Lipopolysaccharides)
0 (Tumor Necrosis Factor Inhibitors)
0 (Tumor Necrosis Factor-alpha)
7535-00-4 (Galactosamine)
تواريخ الأحداث: Date Created: 20200901 Date Completed: 20210520 Latest Revision: 20210520
رمز التحديث: 20221213
DOI: 10.1002/1873-3468.13913
PMID: 32865225
قاعدة البيانات: MEDLINE
الوصف
تدمد:1873-3468
DOI:10.1002/1873-3468.13913