Abstract
By targeting the membrane (M) proteins of monkeypox virus (MPXV) strain VEROE6, we analyzed its evolutionary hierarchy and predicted its dominant antigenic B-cell epitope to provide a theoretical basis for the development of MPXV epitope vaccines and related monoclonal antibodies. In this study, phylogenetic trees were constructed based on the nucleic acid sequences of MPXV and the amino acid sequences of M proteins. The 3D structure of the MPXV_VEROE6 M proteins was predicted with AlphaFold v2.0 and the dominant antigenic B-cell epitopes were comprehensively predicted by analyzing parameters such as flexible segments, the hydrophilic index, the antigenic index, and the protein surface probability. The results showed that the M protein of MPXV_VEROE6 contained 377 amino acids, and their spatial configuration was relatively regular with a turning and random coil structure. The results of a comprehensive multiparameter analysis indicated that possible B-cell epitopes were located in the 23–28, 57–63, 67–78, 80–93, 98–105, 125–131, 143–149, 201–206, 231–237, 261–270, 291–303, and 346–362 amino acid segments. This study elucidated the structural and evolutionary characteristics of MPXV membrane proteins with the aim of providing theoretical information for the development of epitope vaccines, rapid diagnostic reagents, and monoclonal antibodies for monkeypox virus.
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