Predicted 3D model of the M protein of Porcine Epidemic Diarrhea Virus and analysis of its immunogenic potential

Abstract

The membrane protein M of the Porcine Epidemic Diarrhea Virus (PEDV) is the most abundant component of the viral envelope. The M protein plays a central role in the morphogenesis and assembly of the virus through protein interactions of the M-M, M-Spike (S) and M-nucleocapsid (N) type. The M protein is known to induce protective antibodies in pigs and to participate in the antagonistic response of the cellular antiviral system coordinated by the type I and type III interferon pathways. The 3D structure of the PEDV M protein is still unknown. The present work exposes a predicted 3D model of the M protein generated using the Robetta protocol. The M protein model is organized into a transmembrane and a globular region. The obtained 3D model of the PEDV M protein was compared with 3D models of the SARS-CoV-2 M protein created using neural networks and with initial machine learning-based models created using trRosetta. The 3D model of the present study predicted four linear B-cell epitopes (RSVNASSGTG and KHGDYSAVSNPSALT peptides are noteworthy), six discontinuous B-cell epitopes, forty weak binding and fourteen strong binding T-cell epitopes in the CV777 M protein. A high degree of conservation of the epitopes predicted in the PEDV M protein was observed among different PEDV strains isolated in different countries. The data suggest that the M protein could be a potential candidate for the development of new treatments or strategies that activate protective cellular mechanisms against viral diseases.

Porcine epidemic diarrhea virus strain CH/HLJ/18 isolated in China: characterization and phylogenetic analysis

“…The continuous epitopes in the PEDV S protein were predicted using the Bepiprid 1.0 and 2.0 ( http://tools.iedb.org/bcell/ ) tools in the online immune epitope database (IEDB) ( https://www.iedb.org/ ). The threshold value of Bepippred 1.0 was set to 0.35, and that of Bepippred 2.0 was set to 0.5 [ 30 ]. DiscoTope ( http://tools.iedb.org/discotope/ ) and ElliPro ( http://tools.iedb.org/ellipro/ ) were used to predict discontinuous B-cell epitopes.…”

Crystal structure of the membrane (M) protein from a SARS-COV-2-related coronavirus

“…In coronaviruses, M protein is the only multi-spanning transmembrane structural protein and has been shown to interact with various partner proteins, including all viral structural proteins (S, M, E, N) 1,6,[8][9][10][11][12][13][14][15] and some host factors involved in the interferon signaling pathway such as MAVS [16][17][18][19] . However, how M protein interacts with its partners remains largely unknown due to lack of high-resolution structures of M protein [20][21][22][23] . In this study, we aim to determine the structure of a coronavirus M protein using X-ray crystallography.…”

Angiotensin converting enzyme 2 does not facilitate porcine epidemic diarrhea virus entry into porcine intestinal epithelial cells and inhibits it-induced inflammatory injury by promoting STAT1 phosphorylation

“…The M protein is the main component of the viral envelope and interacts with all structural components during the assembly of the virus particle ( Si et al., 2020 ). The M protein is known to induce protective antibodies in pigs and to participate in the antagonistic response of the cellular antiviral system coordinated by the type I and type III interferon pathways ( Zhang et al., 2016 ; Zhang et al., 2018 ; Rodríguez-Enríquez et al., 2022 ). And the M protein interacted with IRF7 to inhibit type I IFN production during viral infection ( Li et al., 2021 ).…”