Abstract:
:hRSV is the major causative agent of acute respiratory infections. Among its eleven proteins, M2-1 is a transcription antiterminator, making it an interesting target for antivirals. Quercetin is a flavonol which inhibits some virus infectivity and replication. In the present work, the M2-1 gene was cloned, expressed and the protein was purified. Thermal stability and secondary structure were analyzed by circular dichroism and the interaction with Quercetin was evaluated by fluorescence spectroscopy. Molecular docking experiments were performed to understand this mechanism of interaction. The purified protein is mainly composed of α-helix, with a melting temperature of 328.6K (≈55°C). M2-1 titration with Quercetin showed it interacts with two sites, one with a strong constant association K1 (site 1≈1.5×106M-1) by electrostatic interactions, and another with a weak constant association K2 (site 2≈1.1×105M-1) by a hydrophobic interaction. Ligand's docking shows it interacts with the N-terminus face in a more polar pocket and, between the domains of oligomerization and RNA and P protein interaction, in a more hydrophobic pocket, as predicted by experimental data. Therefore, we postulated this ligand could be interacting with important domains of the protein, avoiding viral replication and budding.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Teixeira TS,Caruso ÍP,Lopes BR,Regasini LO,Toledo KA,Fossey MA,Souza FPdoi
10.1016/j.ijbiomac.2016.11.033subject
Has Abstractpub_date
2017-02-01 00:00:00pages
63-71eissn
0141-8130issn
1879-0003pii
S0141-8130(16)32356-Xjournal_volume
95pub_type
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