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Aim. Latent membrane protein 2A (LMP2A) of Epstein-Barr virus is implicated in the regulation of viral latency. The aim of the current study was to identify proteins interacting with proline-rich motifs of LMP2A. Methods. In silico prediction with Scansite allowed to recognize amphiphysin 1 (Amph1) as a binding partner of LMP2A. Molecular cloning techniques, site-directed mutagenesis, in vitro binding assay made it possible to study the interaction interface of Amph1/LMP2A complex. Sequential centrifugation steps were used to isolate an exosomal fraction. Results. LMP2A but not LMP2NT mutant has been found to bind the SH3 domain of Amph1 via three distinct proline-rich motifs located in the N-terminal tail. All three motifs seem to be interchangeable as the presence of at least one of them was sufficient to mediate LMP2A/Amph1 interaction. Furthermore, the binding of LMP2A to Amph1 and related protein amphiphysin 2 was demonstrated by co-immunoprecipitation of endogenous complexes. We have found that inability of LMP2A mutant to bind Amph1 leads to the vanishing of the viral protein from the exosomal fraction. Conclusions. The latent membrane protein 2A of Epstein-Barr virus forms complexes with endocytic adaptor proteins Amph1 and Amph2. Described interaction might be involved in the regulation of intracellular traffic and secretion of LMP2A

Amphiphysin 1 and 2 interact with latent membrane protein 2A of Epstein-Barr virus and regulate its exosomal secretion