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The imune system is responsible for eliminating threatening organisms and toxins, as well as for avoiding autoimmune responses that could be potentially harmful to the human tissues. Through special features of the imune cells, which can detect a massive variety of structures specific to pathogens, the imune system can mediate the adequate response to each specific situation. B cells are considered focal elements of the adaptative imune response since the recognition of pathogen’s antigens, and consequently activation and differentiation of B cells, results in the capture and elimination of the hazardous microbes and toxins. In order to successfully recognize potential threats, B cells are equipped with B cell receptors or BCRs. Antigen binding to the BCRs triggers na enormous number of downstream events in the cells, orchestrating numerous processes such as antigen internalization and actin reorganization. Despite the importance pf B cell responses for the imune system, many molecular players behind the regulation of the BCR signalling complexes and its interplay with other celular processes such as antigen internalization and cytoskeletal rearrangements are still unknown or poorly understood. Therefore, this work aims to set up and optimize a new pull-down method for the isolation of proteins recruited to the imune synapse site following BCR activation. Mass spectometry (MS) protein analysis will reveal potential candidates to regulate the immunological synapse formation and, ultimately the imune response.
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Immune system Immune synapse B cells BCR proteome BCR activation Mass spectrometry