Structural analyzes suggest that MiSSP13 and MiSSP16.5 may act as proteases inhibitors during ectomycorrhiza establishment in Laccaria bicolor.

•The signaling process during mycorrhiza establishment involves intense molecular communication between symbionts. It has been suggested that a group of protein effectors, the so-called MiSSPs, plays a broader function in the symbiosis metabolism, however, many of these remain uncharacterized structurally and functionally. •Herein we used three-dimensional protein structure modeling methods, ligand analysis, and molecular docking to structurally characterize and describe two protein effectors, MiSSP13 and MiSSP16.5, with enhanced expression during the mycorrhizal process in Laccaria bicolor. •MiSSP13 and MiSSP16.5 show structural homology with the cysteine and aspartate protease inhibitor, cocaprin (CCP1). Through structural analysis, it was observed that MiSSP13 and MiSSP16.5 have an active site similar to that observed in CCP1. The protein-protein docking data showed that MiSSP13 and MiSSP16.5 interact with the papain and pepsin proteases at sites that are near to where CCP1 interacts with these same targets, suggesting a function as inhibitor of cysteine and aspartate proteases. The interaction of MiSSP13 with papain and MiSSP16.5 with pepsin was stronger than the interaction of CCP1 with these proteases, suggesting that the MiSSPs had a greater activity in inhibiting these classes of proteases. Based on the data supplied, a model is proposed for the function of MiSSPs 13 and 16.5 during the symbiosis establishment. Our findings, while derived from in silico analyses, enable us formulate intriguing hypothesis on the function of MiSSPs in ectomycorrhization, which will require experimental validation.

Prediction of MicroRNAs in the Epstein-Barr Virus Reveals Potential Targets for the Viral Self-Regulation.

Studies involving miRNAs have opened discussions about their broad participation in viral infections. Regarding the Human gammaherpesvirus 4 or Epstein-Barr virus (EBV), miRNAs are important regulators of viral and cellular gene expression during the infectious process, promoting viral persistence and, in some cases, oncogenic processes. We identified 55 miRNAs of EBV type 2 and inferred the viral mRNA target to self-regulate. This data indicate that gene self-repression is an important strategy for maintenance of the viral latent phase. In addition, a protein network was constructed to establish essential proteins in the self-regulation process. We found ten proteins that work as hubs, highlighting BTRF1 and BSRF1 as the most important proteins in the network. These results open a new way to understand the infection by EBV type 2, where viral genes can be targeted for avoiding oncogenic processes, as well as new therapies to suppress and combat the persistent viral infection.