A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies

Foot and mouth disease is caused by a non-enveloped virus (FMDV), which disposes several antigenic sites at the surface of their capsid proteins. The most relevant and immunodominant antigenic site of FMDV (site A or AnSA) includes a key virus-cell interaction element (RGD motif) located in the Vira...

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Autor principal: Marrero, R.
Otros Autores: Limardo, R.R, Carrillo, E., König, G.A, Turjanski, A.G
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Elsevier B.V. 2015
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-84943661009 
024 7 |2 cas  |a amino acid, 65072-01-7; arginylglycylaspartic acid, 99896-85-2; protein VP1, 92354-95-5; Antibodies, Monoclonal; Antibodies, Neutralizing; Antibodies, Viral; Antigens, Viral; Capsid Proteins; Epitopes; Immunodominant Epitopes; VP1 protein, Foot-and-mouth disease virus 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JIMMB 
100 1 |a Marrero, R. 
245 1 2 |a A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies 
260 |b Elsevier B.V.  |c 2015 
270 1 0 |m König, G.A.; Laboratorio de Virus Animales, Instituto de Biotecnología, CICVyA, INTA CastelarArgentina; email: konig.guidoalberto@inta.gob.ar 
506 |2 openaire  |e Política editorial 
504 |a Bonnet, E., Van De Peer, Y., Zt: a software tool for simple and partial Mantel tests (2002) J. Stat. Softw., 7, p. 1 
504 |a Doel, T.R., FMD vaccines (2003) Virus Res., 91, p. 81 
504 |a Feigelstock, D.A., Mateu, M.G., Valero, M.L., Andreu, D., Domingo, E., Palma, E.L., Emerging foot-and-mouth disease virus variants with antigenically critical amino acid substitutions predicted by model studies using reference viruses (1996) Vaccine, 14, p. 97 
504 |a Fry, E.E., Lea, S.M., Jackson, T., Newman, J.W., Ellard, F.M., Blakemore, W.E., Abu-Ghazaleh, R., Stuart, D.I., The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex (1999) EMBO J., 18, p. 543 
504 |a Jackson, T., King, A.M., Stuart, D.I., Fry, E., Structure and receptor binding (2003) Virus Res., 91, p. 33 
504 |a Kiel, C., Serrano, L., Prediction of Ras-effector interactions using position energy matrices (2007) Bioinformatics, 23, p. 2226 
504 |a Kiel, C., Serrano, L., Herrmann, C., A detailed thermodynamic analysis of ras/effector complex interfaces (2004) J. Mol. Biol., 340, p. 1039 
504 |a Kiel, C., Wohlgemuth, S., Rousseau, F., Schymkowitz, J., Ferkinghoff-Borg, J., Wittinghofer, F., Serrano, L., Recognizing and defining true Ras binding domains II: in silico prediction based on homology modelling and energy calculations (2005) J. Mol. Biol., 348, p. 759 
504 |a Kim, M.O., Nichols, S.E., Wang, Y., McCammon, J.A., Effects of histidine protonation and rotameric states on virtual screening of M. tuberculosis RmlC (2013) J. Comput. Aided Mol. Des., 27, p. 235 
504 |a Lauck, F., Smith, C.A., Friedland, G.F., Humphris, E.L., Kortemme, T., RosettaBackrub-a web server for flexible backbone protein structure modeling and design (2010) Nucleic Acids Res., 38, p. W569 
504 |a London, N., Raveh, B., Cohen, E., Fathi, G., Schueler-Furman, O., Rosetta FlexPepDock web server-high resolution modeling of peptide-protein interactions (2011) Nucleic Acids Res., 39, p. W249 
504 |a Mateu, M.G., Verdaguer, N., Functional and structural aspects of the interaction of Foot-and-Mouth Disease Virus with antibodies (2004) Foot-and-Mouth Disease Virus: Current Perspective, p. 223. , Horizon Bioscience, F. Sobrino, E. Domingo (Eds.) 
504 |a Mateu, M.G., Rocha, E., Vicente, O., Vayreda, F., Navalpotro, C., Andreu, D., Pedroso, E., Domingo, E., Reactivity with monoclonal antibodies of viruses from an episode of foot-and-mouth disease (1987) Virus Res., 8, p. 261 
504 |a Mateu, M.G., Martinez, M.A., Capucci, L., Andreu, D., Giralt, E., Sobrino, F., Brocchi, E., Domingo, E., A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C (1990) J. Gen. Virol., 71, p. 629 
504 |a Ochoa, W.F., Kalko, S.G., Mateu, M.G., Gomes, P., Andreu, D., Domingo, E., Fita, I., Verdaguer, N., A multiply substituted G-H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules (2000) J. Gen. Virol., 81, p. 1495 
504 |a Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., Ferrin, T.E., UCSF Chimera-a visualization system for exploratory research and analysis (2004) J. Comput. Chem., 25, p. 1605 
504 |a Petukh, M., Stefl, S., Alexov, E., The role of protonation states in ligand-receptor recognition and binding (2013) Curr. Pharm. Des., 19, p. 4182 
504 |a Rueckert, R.R., Picornaviridae: the viruses and their replication (1996) Fields Virology, p. 609. , Lippincott-Raven Publishers, Philadelphia, B.N. Fields, D.M. Knipe, P.M. Howley (Eds.) 
504 |a Sali, A., Blundell, T.L., Comparative protein modelling by satisfaction of spatial restraints (1993) J. Mol. Biol., 234, p. 779 
504 |a Sanner, M.F., Olson, A.J., Spehner, J.C., Reduced surface: an efficient way to compute molecular surfaces (1996) Biopolymers, 38, p. 305 
504 |a Schymkowitz, J., Borg, J., Stricher, F., Nys, R., Rousseau, F., Serrano, L., The FoldX web server: an online force field (2005) Nucleic Acids Res., 33, p. W382 
504 |a Smith, C.A., Kortemme, T., Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction (2008) J. Mol. Biol., 380, p. 742 
504 |a Smith, C.A., Kortemme, T., Structure-based prediction of the peptide sequence space recognized by natural and synthetic PDZ domains (2010) J. Mol. Biol., 402, p. 460 
504 |a Smith, C.A., Kortemme, T., Predicting the tolerated sequences for proteins and protein interfaces using RosettaBackrub flexible backbone design (2011) PLoS One, 6, p. e20451 
504 |a Surovoi, A., Ivanov, V.T., Chepurkin, A.V., Ivaniushchenkov, V.N., Driagalin, N.N., Is the Arg-Gly-Asp sequence the site for foot-and-mouth disease virus binding with cell receptor? (1988) Bioorg. Khim., 14, p. 965 
504 |a Sutmoller, P., Barteling, S.S., Olascoaga, R.C., Sumption, K.J., Control and eradication of foot-and-mouth disease (2003) Virus Res., 91, p. 101 
504 |a Verdaguer, N., Mateu, M.G., Bravo, J., Tormo, J., Giralt, E., Andreu, D., Domingo, E., Fita, I., Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide (1994) Proteins, 18, p. 201 
504 |a Verdaguer, N., Mateu, M.G., Andreu, D., Giralt, E., Domingo, E., Fita, I., Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction (1995) EMBO J., 14, p. 1690 
504 |a Verdaguer, N., Mateu, M.G., Bravo, J., Domingo, E., Fita, I., Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mouth-disease virus (1996) J. Mol. Biol., 256, p. 364 
504 |a Verdaguer, N., Fita, I., Domingo, E., Mateu, M.G., Efficient neutralization of foot-and-mouth disease virus by monovalent antibody binding (1997) J. Virol., 71, p. 9813 
504 |a Verdaguer, N., Sevilla, N., Valero, M.L., Stuart, D., Brocchi, E., Andreu, D., Giralt, E., Fita, I., A similar pattern of interaction for different antibodies with a major antigenic site of foot-and-mouth disease virus: implications for intratypic antigenic variation (1998) J. Virol., 72, p. 739 
504 |a Verdaguer, N., Schoehn, G., Ochoa, W.F., Fita, I., Brookes, S., King, A., Domingo, E., Hewat, E.A., Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation (1999) Virology, 255, p. 260 
520 3 |a Foot and mouth disease is caused by a non-enveloped virus (FMDV), which disposes several antigenic sites at the surface of their capsid proteins. The most relevant and immunodominant antigenic site of FMDV (site A or AnSA) includes a key virus-cell interaction element (RGD motif) located in the Viral Protein 1 (VP1), more precisely at the GH loop. AnSA includes a set of overlapped and mainly linear epitopes, which are the main targets of the humoral immune response. Taking advantage over specific structural features of the GH loop, we have evaluated the influence of every amino acid residue at AnSA in the interaction with 2 neutralizing antibodies by molecular modeling techniques. Additionally, we constructed diverse interaction complexes with multiple site A mutants and discussed about the structural influence of amino acidic insertions in such relevant antigenic site of FMDV. Our approach is in agreement with previous ELISA experiments and allows the understanding of how FMDV mutations may alter the interaction with different antibodies, as we can estimate the contribution of each amino acid to the interaction. Overall, our work contributes to the development of specific vaccination strategies for FMD control. © 2015 Elsevier B.V.  |l eng 
536 |a Detalles de la financiación: Instituto Nacional de Tecnología Agropecuaria, PE_AESA_201721 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, 1728/OC-AR-PAE 
536 |a Detalles de la financiación: Instituto Nacional de Tecnología Agropecuaria Project PE_AESA_201721 and Agencia Nacional de Promoción Científica y Tecnológica Project INTA-BID 1728/OC-AR-PAE 37206-PICT No 33 . Appendix A 
593 |a Laboratorio de Virus Animales, Instituto de Biotecnología, CICVyA, INTA Castelar, Buenos Aires, Argentina 
593 |a Laboratorio de Bioinformática Estructural, Departamento de Química Biológica, INQUIMAE FCEN, UBA, Buenos Aires, Argentina 
593 |a CONICET, Argentina 
593 |a INQUIMAE/CONICET, Argentina 
690 1 0 |a ANTIBODY 
690 1 0 |a BIOINFORMATICS 
690 1 0 |a ELISA 
690 1 0 |a EPITOPE 
690 1 0 |a FMDV 
690 1 0 |a INTERACTION ENERGY 
690 1 0 |a AMINO ACID 
690 1 0 |a ARGINYLGLYCYLASPARTIC ACID 
690 1 0 |a EPITOPE 
690 1 0 |a MONOCLONAL ANTIBODY 
690 1 0 |a NEUTRALIZING ANTIBODY 
690 1 0 |a PROTEIN VP1 
690 1 0 |a CAPSID PROTEIN 
690 1 0 |a MONOCLONAL ANTIBODY 
690 1 0 |a NEUTRALIZING ANTIBODY 
690 1 0 |a VIRUS ANTIBODY 
690 1 0 |a VIRUS ANTIGEN 
690 1 0 |a VP1 PROTEIN, FOOT-AND-MOUTH DISEASE VIRUS 
690 1 0 |a ANTIBODY RESPONSE 
690 1 0 |a ANTIGEN ANTIBODY COMPLEX 
690 1 0 |a ANTIGEN ANTIBODY REACTION 
690 1 0 |a ANTIGENICITY 
690 1 0 |a ARTICLE 
690 1 0 |a BINDING AFFINITY 
690 1 0 |a BIOINFORMATICS 
690 1 0 |a ENZYME LINKED IMMUNOSORBENT ASSAY 
690 1 0 |a FOOT AND MOUTH DISEASE VIRUS 
690 1 0 |a HUMORAL IMMUNITY 
690 1 0 |a MATHEMATICAL ANALYSIS 
690 1 0 |a MOLECULAR MODEL 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a VIRUS CELL INTERACTION 
690 1 0 |a VIRUS MUTATION 
690 1 0 |a ANIMAL 
690 1 0 |a BIOLOGY 
690 1 0 |a FOOT AND MOUTH DISEASE 
690 1 0 |a FOOT AND MOUTH DISEASE VIRUS 
690 1 0 |a IMMUNOLOGY 
690 1 0 |a PROCEDURES 
690 1 0 |a SERODIAGNOSIS 
690 1 0 |a ANIMALS 
690 1 0 |a ANTIBODIES, MONOCLONAL 
690 1 0 |a ANTIBODIES, NEUTRALIZING 
690 1 0 |a ANTIBODIES, VIRAL 
690 1 0 |a ANTIGENS, VIRAL 
690 1 0 |a CAPSID PROTEINS 
690 1 0 |a COMPUTATIONAL BIOLOGY 
690 1 0 |a EPITOPES 
690 1 0 |a FOOT-AND-MOUTH DISEASE 
690 1 0 |a FOOT-AND-MOUTH DISEASE VIRUS 
690 1 0 |a IMMUNITY, HUMORAL 
690 1 0 |a IMMUNODOMINANT EPITOPES 
690 1 0 |a NEUTRALIZATION TESTS 
700 1 |a Limardo, R.R. 
700 1 |a Carrillo, E. 
700 1 |a König, G.A. 
700 1 |a Turjanski, A.G. 
773 0 |d Elsevier B.V., 2015  |g v. 425  |h pp. 51-57  |p J. Immunol. Methods  |x 00221759  |w (AR-BaUEN)CENRE-5615  |t Journal of Immunological Methods 
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