Re-evaluation of binding properties of recombinant lymphocyte receptors NKR-P1A and CD69 to chemically synthesized glycans and peptides

. 2014 Jan 17 ; 15 (1) : 1271-83. [epub] 20140117

Jazyk angličtina Země Švýcarsko Médium electronic

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid24445261

The binding of monosaccharides and short peptides to lymphocyte receptors (human CD69 and rat NKR-P1A) was first reported in 1994 and then in a number of subsequent publications. Based on this observation, numerous potentially high-affinity saccharide ligands have been synthesized over the last two decades in order to utilize their potential in antitumor therapy. Due to significant inconsistencies in their reported binding properties, we decided to re-examine the interaction between multiple ligands and CD69 or NKR-P1A. Using NMR titration and isothermal titration calorimetry we were unable to detect the binding of the tested ligands such as N-acetyl-D-hexosamines and oligopeptides to both receptors, which contradicts the previous observations published in more than twenty papers over the last fifteen years.

Zobrazit více v PubMed

Moretta A., Poggi A., Pende D., Tripodi G., Orengo A.M., Pella N., Augugliaro R., Bottino C., Ciccone E., Moretta L. CD69-mediated pathway of lymphocyte activation: Anti-CD69 monoclonal antibodies trigger the cytolytic activity of different lymphoid effector cells with the exception of cytolytic T lymphocytes expressing T cell receptor alpha/beta. J. Exp. Med. 1991;174:1393–1398. PubMed PMC

Giorda R., Rudert W.A., Vavassori C., Chambers W.H., Hiserodt J.C., Trucco M. NKR-P1, a signal transduction molecule on natural killer cells. Science. 1990;249:1298–1300. PubMed

Bezouska K., Vlahas G., Horvath O., Jinochova G., Fiserova A., Giorda R., Chambers W.H., Feizi T., Pospisil M. Rat natural killer cell antigen, NKR-P1, related to C-type animal lectins is a carbohydrate-binding protein. J. Biol. Chem. 1994;269:16945–16952. PubMed

Bezouska K., Yuen C.T., O’Brien J., Childs R.A., Chai W., Lawson A.M., Drbal K., Fiserova A., Pospisil M., Feizi T. Oligosaccharide ligands for NKR-P1 protein activate NK cells and cytotoxicity. Nature. 1994;372:150–157. PubMed

Bezouska K., Nepovim A., Horvath O., Pospisil M., Hamann J., Feizi T. CD 69 antigen of human lymphocytes is a calcium-dependent carbohydrate-binding protein. Biochem. Biophys. Res. Commun. 1995;208:68–74. PubMed

Kogelberg H., Montero E., Bay S., Lawson A.M., Feizi T. Re-evaluation of monosaccharide binding property of recombinant soluble carbohydrate recognition domain of the natural killer cell receptor NKR-P1A. J. Biol. Chem. 1999;274:30335–30336. PubMed

Childs R.A., Galustian C., Lawson A.M., Dougan G., Benwell K., Frankel G., Feizi T. Recombinant soluble human CD69 dimer produced in Escherichia coli: Re-evaluation of saccharide binding. Biochem. Biophys. Res. Commun. 1999;266:19–23. PubMed

Bezouska K., Sklenar J., Dvorakova J., Havlicek V., Pospisil M., Thiem J., Kren V. NKR-P1A protein, an activating receptor of rat natural killer cells, binds to the chitobiose core of uncompletely glycosylated N-linked glycans, and to linear chitooligomers. Biochem. Biophys. Res. Commun. 1997;38:149–153. PubMed

Krist P., Herkommerova-Rajnochova E., Rauvolfova J., Semenuk T., Vavruskova P., Pavlicek J., Bezouska K., Petrus L., Kren V. Toward an optimal oligosaccharide ligand for rat natural killer cell activation receptor NKR-P1. Biochem. Biophys. Res. Commun. 2001;287:11–20. PubMed

Sedmera P., Prikrylova V., Bezouska K., Rajnochova E., Thiem J., Kren V. Preparation of ManNAc containing chitooligomers by isomerisation and their binding to NKR-P1 protein. J. Carbohydr. Chem. 1998;17:1351–1357.

Kren V., Dvorakova J., Gambert U., Sedmera P., Havlicek V., Thiem J., Bezouska K. β-Glucosylation of chitooligomers by galactosyltransferase. Carbohydr. Res. 1997;305:517–523. PubMed

Bezouska K., Kren V., Kieburg C., Lindhorst T.K. GlcNAc-terminated glycodendrimers form defined precipitates with the soluble dimeric receptor of rat natural killer cells, sNKR-P1A. FEBS Lett. 1998;26:243–247. PubMed

Pospisil M., Vannucci L., Fiserova A., Krausova K., Horvath O., Kren V., Mosca F., Lindhorst T.K., Sadalapure K., Bezouska K. Glycodendrimeric ligands of c-type lectin receptors as therapeutic agents in experimental cancer. Prog. Basic Clin. Immunol. 2001;495:343–347. PubMed

Krist P., Vannucci L., Kuzma M., Man P., Sadalapure K., Patel A., Bezouska K., Pospisil M., Petrus L., Lindhorst T.K., et al. Fluorescent labelled thiourea-bridged glycodendrons. ChemBioChem. 2004;5:445–452. PubMed

Vannucci L., Fiserova A., Sadalapure K., Lindhorst T.K., Kuldova M., Rossmann P., Horvath O., Kren V., Krist P., Bezouska K., et al. Effects of N-acetyl-glucosamine-coated glycodendrimers as biological modulators in the B16F10 melanoma model in vivo. Int. J. Oncol. 2003;23:285–296. PubMed

Pavlicek J., Sopko B., Ettrich R., Kopecky V., Baumruk V., Man P., Havlicek V., Vrbacky M., Martinkova L., Kren V., et al. Molecular characterization of binding of calcium and carbohydrates by an early activation antigen of lymphocytes CD69. Biochemistry. 2003;42:9295–9306. PubMed

Natarajan K., Sawicki M.W., Margulies D.H., Mariuzza R.A. Crystal structure of human CD69: A C-type lectin-like activation marker of hematopoietic cells. Biochemistry. 2000;39:14779–14786. PubMed

Kavan D., Kubickova M., Bily J., Vanek O., Hofbauerova K., Mrazek H., Rozbesky D., Bojarova P., Kren V., Zidek L., et al. Cooperation between subunits is essential for high-affinity binding of N-acetyl-D-hexosamines to dimeric soluble and dimeric cellular forms of human CD69. Biochemistry. 2010;49:4060–4067. PubMed

Kovalova A., Ledvina M., Saman D., Zyka D., Kubickova M., Zidek L., Sklenar V., Pompach P., Kavan D., Bily J., et al. Synthetic N-acetyl-D-glucosamine based fully branched tetrasaccharide, a mimetic of the endogenous ligand for CD69, activates CD69+ killer lymphocytes upon dimerization via a hydrophilic flexible linker. J. Med. Chem. 2010;53:4050–4065. PubMed

Attolino E., Bonaccorsi F., Catelani G., D’Andrea F., Krenek K., Bezouska K., Kren V. Improved preparation of β-D-ManNAc-(1→4)-D -Glc and β-D-TalNAc-(1→4)-D-Glc disaccharides and evaluation of their activating properties on the natural killer cells NKR-P1 and CD69 receptors. J. Carbohydr. Chem. 2008;27:156–171.

Catelani G., D’Andrea F., Griselli A., Guazzelli L., Nemcova P., Bezouska K., Krenek K., Kren V. Deoxynojirimycin and its hexosaminyl derivatives bind to natural killer cell receptors rNKR-P1A and hCD69. Bioorg. Med. Chem. Lett. 2010;20:4645–4648. PubMed

Bojarova P., Krenek K., Kuzma M., Petraskova L., Bezouska K., Namdjou D.J., Elling L., Kren V. N-acetylhexosamine triad in one molecule: Chemoenzymatic introduction of 2-acetamido- 2-deoxy-beta-D-galactopyranosyluronic acid residue into a complex oligosaccharide. J. Mol. Catal. B Enzym. 2008;50:69–73.

Fialova P., Namdjou D.J., Ettrich R., Prikrylova V., Rauvolfova J., Krenek K., Kuzma M., Elling L., Bezouska K., Kren V. Combined application of galactose oxidase and β-N-acetylhexosaminidase in the synthesis of complex immunoactive N-acetyl-D-galactosaminides. Adv. Synth. Catal. 2005;347:997–1006.

Bojarova P., Slamova K., Krenek K., Gazak R., Kulik N., Ettrich R., Pelantova H., Kuzma M., Riva S., Adamek D., et al. Charged hexosaminides as new substrates for β-N-acetylhexosaminidase-catalyzed synthesis of immunomodulatory disaccharides. Adv. Synth. Catal. 2011;353:2409–2420.

Bojarova P., Krenek K., Wetjen K., Adamiak K., Pelantova H., Bezouska K., Elling L., Kren V. Synthesis of LacdiNAc-terminated glycoconjugates by mutant galactosyltransferase—A way to new glycodrugs and materials. Glycobiology. 2009;19:509–517. PubMed

Drozdova A., Bojarova P., Krenek K., Weignerova L., Henssen B., Elling L., Christensen H., Jensen H.H., Pelantova H., Kuzma M., et al. Enzymatic synthesis of dimeric glycomimetic ligands of NK cell activation receptors. Carbohydr. Res. 2011;346:1599–1609. PubMed

Bezouska K., Snajdrova R., Krenek K., Vancurova M., Kadek A., Adamek D., Lhotak P., Kavan D., Hofbauerova K., Man P., et al. Carboxylated calixarenes bind strongly to CD69 and protect CD69(+) killer cells from suicidal cell death induced by tumor cell surface ligands. Bioorg. Med. Chem. 2010;18:1434–1440. PubMed

Slamova K., Marhol P., Bezouska K., Lindkvist L., Hansen S.G., Kren V., Jensen H.H. Synthesis and biological activity of glycosyl-1H-1,2,3-triazoles. Bioorg. Med. Chem. Lett. 2010;20:4263–4265. PubMed

Renaudet O., Krenek K., Bossu I., Dumy P., Kadek A., Adamek D., Vanek O., Kavan D., Gazak R., Sulc M., et al. Synthesis of multivalent glycoconjugates containing the immunoactive LELTE peptide: Effect of glycosylation on cellular activation and natural killing by human peripheral blood mononuclear cells. J. Am. Chem. Soc. 2010;132:6800–6808. PubMed

Bezouska K., Pavlicek J., Sopko B., Kren V., Fiserová A., Pospisil M., Novak P., Havlicek V. Interaction of CD69, the earliest activation antigen of lymphocytes, with calcium and saccharides in three dimensions. Scand. J. Imunnol. 2001;54:26.

Bezouska K., Kubinkova Z., Stribny J., Volfova B., Pompach P., Kuzma M., Sirova M., Rihova B. Dimerization of an immunoactivating peptide derived from mycobacterial hsp65 using N-hydroxysuccinimide based bifunctional reagents is critical for its antitumor properties. Bioconjug. Chem. 2012;23:2032–2041. PubMed

Vanek O., Nalezkova M., Kavan D., Borovickova I., Pompach P., Novak P., Kumar V., Vannucci L., Hudecek J., Hofbauerova K., et al. Soluble recombinant CD69 receptors optimized to have an exceptional physical and chemical stability display prolonged circulation and remain intact in the blood of mice. FEBS J. 2008;275:5589–5606. PubMed

Kveberg L., Dai K., Westgaard I.H., Daws M.R., Fossum S., Naper C., Vaage J.T. Two major groups of rat NKR-P1 receptors can be distinguished based on chromosomal localization, phylogenetic analysis and Clr ligand binding. Eur. J. Imunnol. 2009;39:541–551. PubMed

Hartmann J., Tran T.V., Kaudeer J., Oberle K., Herrmann J., Quagliano I., Abel T., Cohnen A., Gatterdam V., Jacobs A., et al. The stalk domain and the glycosylation status of the activating natural killer cell receptor NKp30 are important for ligand binding. J. Biol. Chem. 2012;287:31527–31539. PubMed PMC

Rozbesky D., Kavan D., Chmelik J., Novak P., Vanek O., Bezouska K. High-level expression of soluble form of mouse natural killer cell receptor NKR-P1C(B6) in Escherichia coli. Protein Expr. Purif. 2011;77:178–184. PubMed

Report of the Joint Ethical Committee of the Institute of Microbiology, Prague and Charles University in Prague. English Translation Can Be Found in the Supplementary Material. [(accessed on 15 January 2014)]. Available online: http://www.biomed.cas.cz/mbu/doc/VyjadreniEK.PDF.

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...