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 i...

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Published in:BioMed Research International Vol. 2016; pp. 1 - 12
Main Authors: Fernando, Bastida-González, Yersin, Celaya-Trejo, José, Correa-Basurto, Paola, Zárate-Segura
Format: pictorial research tables/charts Journal Article
Published: Wiley-Blackwell 4/24/2016
Online Access:View this record in EBSCOhost
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      jtl: BioMed Research International
      issn: 23146133
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      dt: 4/24/2016
      vid: 2016
      pid: 480
      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        114761912
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        10.1155/2016/1674580
        114761912
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      ppct: 11
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        atl: Predicted 3D Model of the Rabies Virus Glycoprotein Trimer.
      aug:
        au:
          Fernando, Bastida-González
          Yersin, Celaya-Trejo
          José, Correa-Basurto
          Paola, Zárate-Segura
        affil: 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
      sug:
        subj:
          Rabies Pathology
          Glycoproteins
          Models, Biological
          Models, Structural
          Cell Adhesion Molecules
          Receptors, Cholinergic
          Receptors, Cell Surface
          Antigens, Viral
          Descriptive Statistics
          Simulations
          Algorithms
          Amino Acids
          Molecular Structure
          Sulfur Compounds
      ab: 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.
      pubtype: Academic Journal
      doctype:
        pictorial
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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