Univerzita Pardubice Fakulta chemicko- technologická

Univerzita Pardubice

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Publikace detail

Cross-reactivity of autoantibodies in patient with multiple myeloma in long lasting remission

Autoři: Kročová Eliška | Novák Josef | Kupčík Rudolf | Jankovičová Barbora | Škultéty L'udovít | Lakota Ján | Bílková Zuzana

Rok: 2016

Druh publikace: ostatní - přednáška nebo poster

Strana od-do: nestránkováno

Tituly:

Jazyk	Název	Abstrakt	Klíčová slova
eng	Cross-reactivity of autoantibodies in patient with multiple myeloma in long lasting remission	The immune system can react in the presence of tumor by production of specific autoantibodies. Identification of the specific targets of autoantibodies in cancer may reveal potential biomarkers for cancer diagnosis determine the impact of immune regulation on cancer progression and provide information about the reaction mechanisms useful for immunotherapy development. In our study, the specific autoantibodies against carbonic anhydrase I (CA I) were observed by serological proteome analysis in patient with multiple myeloma in long lasting remission. Moreover, these autoantibodies exhibit cross-reactivity with protein α-enolase (Eno1). CA I plays a crucial role in hematopoietic stem-cell differentiation, except of reversible hydration of carbon dioxide. Eno1 has several functions in organism, e.g. glycolytic protein, plasminogen binding receptor, hypoxic stress protein, heat-shock protein or tumor repressor, which could cause its involvement in tumor development and invasion. The epitope specificity was characterized in detail to be able to describe the mechanism of cross-reactivity accurately. Based on epitope extraction and bioinformatics analysis the position of interaction between antibody and both antigens (CA I and Eno1) were described with focus on their sequence and structure similarity. We presume that the autoantibodies with specificity against CA I and Eno1 could have an impact on tumor regression and the knowledge of epitope recognition site could be useful for immunotherapy development. Acknowledgements: This work was supported by grant No. (SGS_2016_004) and (APVV-0854-12).	Carbonic anhydrase I; enolase 1; cross-reactivity