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.

Institute of Microbiology Academy of Sciences of the Czech Republic Vídeňská 1083 Prague 4 CZ14220 Czech Republic

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$a Rozbeský, Daniel $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. rozbesky@gmail.com.

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$a Re-evaluation of binding properties of recombinant lymphocyte receptors NKR-P1A and CD69 to chemically synthesized glycans and peptides / $c D. Rozbeský, J. Krejzová, K. Křenek, J. Prchal, R. Hrabal, M. Kožíšek, L. Weignerová, M. Fiore, P. Dumy, V. Křen, O. Renaudet,

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$a 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.

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$a Krejzová, Jana $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. hoficek@centrum.cz.

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$a Křenek, Karel $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. krenek@biomed.cas.cz.

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$a Prchal, Jan $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. jan.prchal@vscht.cz.

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$a Hrabal, Richard $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. richard.hrabal@vscht.cz.

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$a Kožíšek, Milan $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. midlan@seznam.cz.

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$a Weignerová, Lenka $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. lenka.weignerova@gmail.com.

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$a Fiore, Michele $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. michele.fiore@ujf-grenoble.fr.

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$a Dumy, Pascal $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. pascal.dumy@ujf-grenoble.fr.

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$a Křen, Vladimír $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. kren@biomed.cas.cz.

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$a Renaudet, Olivier $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, Prague 4 CZ14220, Czech Republic. ^olivier.renaudet@ujf-grenoble.fr.

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