In silico and in vitro analysis of boAP3d1 protein interaction with bovine leukaemia virus gp51
AuthorCorredor Figueroa, Adriana Patricia
Baquero, Luis Alfredo
Patarroyo, Manuel A.
Gutiérrez, María Fernanda
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.
Adaptor Protein ; Alanine ; Arginine ; Asparagine ; Aspartic Acid ; Boap3D1 Protein ; Chymotrypsin ; Glutamic Acid ; Glycoprotein 5 ; Histidine ; Lysine ; Serine ; Trypsin ; Tryptophan ; Unclassified Drug ; Virus Glycoprotein ; Amino Terminal Sequence ; Binding Site ; Bioinformatics ; Bovine Leukemia Virus ; Carboxy Terminal Sequence ; Cell Interaction ; Complex Formation ; Controlled Study ; In Vitro Study ; Mdbk Cell Line ; Molecular Docking ; Nonhuman ; Protein Binding ; Protein Domain ; Protein Expression ; Protein Protein Interaction ;
- Artículos 
Showing items related by title, author, creator and subject.
Receptor–ligand and parasite protein–protein interactions in Plasmodium vivax: Analysing rhoptry neck proteins 2 and 4 Bermúdez M.; Arévalo-Pinzón G.; Rubio L.; Chaloin O.; Muller S.; Curtidor H.; Patarroyo M.A."Elucidating receptor–ligand and protein–protein interactions represents an attractive alternative for designing effective Plasmodium vivax control methods. This article describes the ability of P. vivax rhoptry neck ...Artículo. 2018
Self-assembling functional programmable protein array for studying protein-protein interactions in malaria parasites Arévalo-Pinzón, Gabriela; González-González, María; Suarez Martinez, Carlos Fernando; Curtidor, Hernando; Carabias-Sánchez, Javier; Muro, Antonio; LaBaer, Joshua; Patarroyo, Manuel A.; Fuentes, ManuelBackground: Plasmodium vivax is the most widespread malarial species, causing significant morbidity worldwide. Knowledge is limited regarding the molecular mechanism of invasion due to the lack of a continuous in vitro ...Artículo. 2018
Synthetic peptides from conserved regions of the Plasmodium falciparum early transcribed membrane and ring exported proteins bind specifically to red blood cell proteins Garcia, Jeison; Curtidor, Hernando; Obando-Martinez, Ana Z.; Vizcaíno, Carolina; Pinto, Martha; Martinez, Nora L.; Patarroyo, Manuel A.; Patarroyo, Manuel E."Severe malaria pathology is directly associated with cytoadherence of infected red blood cells (iRBCs) to healthy RBCs and/or endothelial cells occurring during the intraerythrocytic development of Plasmodium falciparum. ...Artículo. 2009