Predicted 3D Model of the Rabies Virus Glycoprotein Trimer.
The RABVG ectodomain is a homotrimer, and trimers are often called spikes. They are responsible for the attachment of the virus through the interaction with nicotinic acetylcholine receptors, neural cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR). This makes them relevant in viral pathogenesis. The antigenic structure differs significantly between the trimers and monomers. Surfaces rich in hydrophobic amino acids are important for trimer stabilization in which the C-terminal of the ectodomain plays an important role; to understand these interactions between the G proteins, a mechanistic study of their functions was performed with a molecular model of G protein in its trimeric form. This verified its 3D conformation. The molecular modeling of G protein was performed by a I-TASSER server and was evaluated via a Rachamandran plot and ERRAT program obtained 84.64% and 89.9% of the residues in the favorable regions and overall quality factor, respectively. The molecular dynamics simulations were carried out on RABVG trimer at 310 K. From these theoretical studies, we retrieved the RMSD values from Cα atoms to assess stability. Preliminary model of G protein of rabies virus stable at 12 ns with molecular dynamics was obtained.
Laboratorio de Medicina Traslacional, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico; Laboratorio de Biología Molecular, Laboratorio Estatal de Salud Pública del Estado de México, Paseo Tollocan s/n, La moderna de la cruz, 50180 Toluca, MEX, Mexico.
Bastida-González
BG
Fernando
Laboratorio de Medicina Traslacional, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico.
Celaya-Trejo
CT
Yersin
Laboratorio de Modelado Molecular y Bioinformática, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico.
Correa-Basurto
CB
José
Laboratorio de Medicina Traslacional, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, Santo Tomas, Miguel Hidalgo, 11340 Ciudad de México, DF, Mexico; Departamento de Bioprocesos, Unidad Profesional Interdisciplinaria de Biotecnología, Instituto Politécnico Nacional, Avenida Acueducto de Guadalupe s/n, Ticoman, Gustavo A. Madero, 07340 Ciudad de México, DF, Mexico.
Zárate-Segura
ZS
Paola
D000465:Algorithms; D000956:Antigens, Viral / Q000737:chemistry*; D019002:CD56 Antigen / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry*; D021621:Imaging, Three-Dimensional / Q000379:methods*; D007107:Immune System; D056004:Molecular Dynamics Simulation; D009419:Nerve Tissue Proteins / Q000737:chemistry; D000072417:Protein Domains; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011820:Rabies virus; D017475:Receptors, Nerve Growth Factor / Q000737:chemistry; D014759:Viral Envelope Proteins / Q000737:chemistry*
D000956:Antigens, Viral; D019002:CD56 Antigen; D006023:Glycoproteins; C522918:NCAM1 protein, human; C484065:NGFR protein, human; D009419:Nerve Tissue Proteins; D017475:Receptors, Nerve Growth Factor; D014759:Viral Envelope Proteins; C064951:glycoprotein G, Rabies virus