Insights into the specific feature of the electrostatic recognition binding mechanism between BM2 and BM1: a molecular dynamics simulation study

Matrix protein 2 (M2) and matrix protein 1 (M1) of the influenza B virus are two important proteins, and the interactions between BM2 and BM1 play an important role in the process of virus assembly and replication. However, the interaction details between BM2 and BM1 are still unclear at the atomic...

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Bibliographic Details
Published in:	Physical chemistry chemical physics : PCCP Vol. 26; no. 34; p. 22726
Main Authors:	Xing, Guixuan, Zheng, Qingchuan
Format:	Journal Article
Language:	English
Published:	England 28-08-2024
Subjects:	Binding Sites Hydrogen Bonding Influenza B virus - chemistry Influenza B virus - metabolism Molecular Docking Simulation Molecular Dynamics Simulation Mutation Protein Binding Static Electricity Viral Matrix Proteins - chemistry Viral Matrix Proteins - metabolism Viral Proteins
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Summary:	Matrix protein 2 (M2) and matrix protein 1 (M1) of the influenza B virus are two important proteins, and the interactions between BM2 and BM1 play an important role in the process of virus assembly and replication. However, the interaction details between BM2 and BM1 are still unclear at the atomic level. Here, we constructed the BM2 BM1 complex system using homology modelling and molecular docking methods. Molecular dynamics (MD) simulations were used to illustrate the binding mechanism between BM2 and BM1. The results identify that the eight polar residues (E88 , E89 , H119 , E94 , R101 , K102 , R105 , and E104 ) play an important role in stabilizing the binding through the formation of hydrogen bond networks and salt-bridge interactions at the binding interface. Furthermore, based on the simulation results and the experimental facts, the mutation experiments were designed to verify the influence of the mutation of residues both within and outside the effector domain. The mutations directly or indirectly disrupt interactions between polar residues, thus affecting viral assembly and replication. The results could help us understand the details of the interactions between BM2 and BM1 and provide useful information for the anti-influenza drug design.
ISSN:	1463-9084
DOI:	10.1039/d4cp01936a