Epitope Mapping of Lymphocyte Phosphatase-Associated Phosphoprotein

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A. V. Filatov^1*, T. D. Meshkova², and D. V. Mazurov¹

¹Institute of Immunology, Federal Medical-Biological Agency, Kashirskoe Shosse 24/2, 115478 Moscow, Russia; fax: (499) 617-7765; E-mail: avfilat@rambler.ru

²Faculty of Biology, Lomonosov Moscow State University, 119234 Moscow, Russia; E-mail: meshkova.tatiana@yandex.ru

^* To whom correspondence should be addressed.

Received July 12, 2014

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Lymphocyte phosphatase-associated phosphoprotein (LPAP) is a transmembrane protein with unknown function. The available data on its close association with phosphatase CD45 and its phosphorylation depending on cell activation suggest that LPAP can play a significant role in the antigenic stimulation of lymphocytes. We have localized three antigenic epitopes of the LPAP molecule that can be detected using monoclonal antibodies prepared earlier. Experiments on reactions of antibodies with point mutants and shortened forms of the LPAP protein revealed regions of the amino acid sequence that correspond to the epitopes recognized by the antibodies.

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KEY WORDS: LPAP, monoclonal antibodies, site directed mutagenesis, human lymphocytes

DOI: 10.1134/S0006297914120153

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