In silico and in vitro analysis of boAP3d1 protein interaction with bovine leukaemia virus gp51
| Autor: | Nury N. Olaya-Galán, Janneth Gonzalez, María Fernanda Gutiérrez, Luis Alfredo Baquero, Adriana Patricia Corredor, Manuel A. Patarroyo, Hernando Curtidor |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Sitio de unión
Protein Expression Bovine Leukemia Virus Plasma protein binding No humano Biochemistry Binding Analysis Viral Envelope Proteins línea celular mdbk Mdbk Cell Line Protein Interaction Mapping Macromolecular Structure Analysis Formación compleja Protein Protein Interaction lcsh:Science Peptide sequence Alanine Bovine leukemia virus Alanina Dominio de proteínas Molecular Docking Quimotripsina Amino Terminal Sequence Glicoproteína viral Boap3D1 Protein Asparagine Hydrophobic and Hydrophilic Interactions Asparagina Cell Binding Glicoproteína 5 Protein Structure Cell Physiology Bioinformatics In silico 030106 microbiology Article 03 medical and health sciences Unclassified Drug Protein Domains Expresión de proteínas Interacción Proteína Proteína Computer Simulation Amino Acid Sequence Molecular Biology Chemical Characterization Ácido aspártico Virus Glycoprotein Proteína Boap3D1 Lysine lcsh:R Binding Site Biology and Life Sciences Proteins Cell Interaction Molecular Sequence Annotation Lisina Tripsina Proteína adaptadora In Vitro Study 030104 developmental biology Virus de la leucemia bovina Secuencia amino terminal Cattle lcsh:Q Secuencia terminal carboxi 0301 basic medicine lcsh:Medicine Acoplamiento molecular Protein Structure Prediction Protein Structure Secondary Database and Informatics Methods Protein structure Leukemia Virus Bovine Serine Chymotrypsin Ácido glutamico Trypsin Serina Multidisciplinary biology Chemistry Tryptophan Signal transducing adaptor protein Bioinformática Triptófano Recombinant Proteins Adaptor Protein Complex delta Subunits Molecular Docking Simulation Thermodynamics Glycoprotein 5 Sequence Analysis Research Article Protein Binding Producción animal (Zootecnia) Leucemia bovina Medicamento no clasificado Protein Domain Protein domain Arginina Glutamic Acid Interacción celular Research and Analysis Methods Arginine Cell Line Protein–protein interaction Estudio in vitro Histidina Animals Histidine Controlled Study Complex Formation Protein Interactions Aspartic Acid Reproducibility of Results Cell Biology Estudio controlado Carboxy Terminal Sequence biology.organism_classification Nonhuman Adaptor Protein Enlace proteico Sequence Alignment |
| Zdroj: | (2017) International Committee on Taxonomy of Viruses, ICTV Repositorio EdocUR-U. Rosario Universidad del Rosario instacron:Universidad del Rosario PLoS ONE, Vol 13, Iss 6, p e0199397 (2018) PLoS ONE |
| Popis: | The envelope glycoprotein 51 (gp51) is essential for bovine leukaemia virus (BLV) entry to bovine B-lymphocytes. Although the bovine adaptor protein 3 complex subunit delta-1 (boAP3D1) has been proposed as the potential receptor, the specific ligand-receptor interaction has not yet been completely defined and boAP3D1 receptor and gp51 3D structures have not been determined. This study was thus aimed at a functional annotation of boAP3D1 cellular adaptor protein and BLV gp51 and, proposing a reliable model for gp51-AP3D1 interaction using bioinformatics tools. The boAP3D1 receptor interaction patterns were calculated based on models of boAP3D1 receptor and gp51 complexes’ 3D structures, which were constructed using homology techniques and data-driven docking strategy. The results showed that the participation of 6 key amino acids (aa) on gp51 (Asn170, Trp127, His115, Ala97, Ser98 and Glu128) and 4 aa on AP3D1 (Lys925, Asp807, Asp695 and Arg800) was highly probable in the interaction between gp51 and BLVR domains. Three gp51 recombinant peptides were expressed and purified to validate these results: the complete domain (rgp51), the N-terminal portion (rNgp51) and the C-terminal fragment (rCgp51); and binding assays to Madin-Darby bovine kidney (MDBK) cells were then carried out with each recombinant. It was found that rNgp51 preferentially bound to MDBK cells, suggesting this domain’s functional role during invasion. The rNgp51-MDBK cell interaction was sensitive to trypsin (98% reduction) and chymotrypsin treatment (80% reduction). These results highlighted that the N-terminal portion of gp51 interacted in vitro with the AP3D1 receptor and provides a plausible in silico interaction model. © 2018 Corredor et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|