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• Mechanisms for Virus-Induced Membrane Fusion

• The bilayer collective properties govern the interaction of an HIV-1 antibody with the viral membrane

  Carravilla, P.; Darré, L.; Oar-Arteta, I.R.; Vesga, A.G.; Rujas, E.; Heras-Martínez, G. de las; Domene, C.; Nieva, J.L.; Requejo-Isidro, J.

  Biophys. J. 118, 44–56 (2020)

• Molecular recognition of the native HIV-1 MPER revealed by STED microscopy of single virions

  P Carravilla, J Chojnacki, E Rujas, S Insausti, E Largo, D Waithe, B Apellaniz, T Sicard, JP Julien, C Eggeling and JL Nieva

  Nat Commun. 10(1):78. doi: 10.1038/s41467-018-07962-9 (2019)

• Molecular Characterization of the Viroporin Function of Foot-and-Mouth Disease Virus Nonstructural Protein 2B

  DP Gladue, E Largo, I de la Arada, VM Aguilella, A Alcaraz, JLR Arrondo, LG Holinka, E Brocchi, E Ramirez-Medina, EA Vuono, KA Berggren, C Carrillo, JL Nieva, MV Borca.

  J Virol. 92(23). pii: e01360-18. doi: 10.1128/JVI.01360-18. (2018)

• Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Permeability at the Endoplasmic Reticulum

  Gladue DP, Largo E, Holinka LG, Ramirez-Medina E, Vuono EA, Berggren KA, Risatti GR, Nieva JL, Borca MV.

  Viruses. 2018 ;10(9). pii: E460. doi: 10.3390/v10090460. (2018)

• Exposure of the HIV-1 broadly neutralizing antibody 10E8 MPER epitope on the membrane surface by gp41 transmembrane domain scaffolds

  Oakes V, Torralba J, Rujas E, Nieva JL, Domene C, Apellaniz B.

  . Biochim Biophys Acta. 2018;1860(6):1259-1271. doi: 10.1016/j.bbamem.2018.02.019 (2018)

• Functional Optimization of Broadly Neutralizing HIV-1 Antibody 10E8 by Promotion of Membrane Interactions

  Rujas E, Leaman DP, Insausti S, Ortigosa-Pascual L, Zhang L, Zwick MB, Nieva JL.

  J Virol. 2018;92(8). pii: e02249-17. doi: 10.1128/JVI.02249-17 (2018)

• HIV antivirals: targeting the functional organization of the lipid envelope

  Carravilla P, Nieva, JL.

  Future Virology. 2018; 13, 129-140. doi: 10.2217/fvl-2017-0114 (2018)

• Mutation-induced changes of transmembrane pore size revealed by combined ion-channel conductance and single vesicle permeabilization analyses

  Largo E, Gladue DP, Torralba J, Aguilella VM, Alcaraz A, Borca MV, Nieva JL.

  Biochim Biophys Acta. 2018;1860(5):1015-1021. doi: 10.1016/j.bbamem (2018)

• Structure-Related Roles for the Conservation of the HIV-1 Fusion Peptide Sequence Revealed by Nuclear Magnetic Resonance

  S. Serrano, N. Huarte, E. Rujas, D. Andreu, J.L. Nieva and M.A. Jimenez

  Biochemistry 56, 5503-5511 doi: 10.1021/acs.biochem.7b00745 (2017)

• Effects of HIV-1 gp41-Derived Virucidal Peptides on Virus-like Lipid Membranes

  P. Carravilla, A. Cruz, I. Martin-Ugarte, I.R. Oar-Arteta, J. Torralba, B. Apellaniz, J. Perez-Gil, J. Requejo-Isidro, N. Huarte and J.L. Nieva

  Biophys J 113, 1301-1310 doi: 10.1016/j.bpj.2017.06.061 (2017)

• Functional Contacts between MPER and the Anti-HIV-1 Broadly Neutralizing Antibody 4E10 Extend into the Core of the Membrane

  E. Rujas, S. Insausti, M. Garcia-Porras, R. Sanchez-Eugenia, K. Tsumoto, J.L. Nieva and JJ.M.M. Caaveiro

  . J Mol Biol 429, 1213-1226 doi: 10.1016/j.jmb.2017.03.008 (2017)

• Peripheral Membrane Interactions Boost the Engagement by an Anti-HIV-1 Broadly Neutralizing Antibody

  E. Rujas, J.M.M. Caaveiro, S. Insausti, M. Garcia-Porras, K. Tsumoto and J.L. Nieva

  J Biol Chem 292, 5571-5583 doi: 10.1074/jbc.M117.775429 (2017)

• Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface

  E. Rujas, J.M. Caaveiro, A. Partida-Hanon, N. Gulzar, K. Morante, B. Apellániz, M. García-Porras, M. Bruix, K. Tsumoto, J.K. Scott, M.A. Jiménez and J.L. Nieva.

  Sci Rep. 6, 38177 doi.10.1038/srep38177 (2016)

• Alteration of a second putative fusion peptide of structural glycoprotein E2 of classical swine fever virus alters virus replication and virulence in swine

  L.G. Holinka, E. Largo, D.P. Glaude, V. O’Donnell, G.R. Risatti, J.L. Nieva and M.V. Borca

  J.Virol. 90, 10299-10308 (2016)

• Functional organizacion of the HIV lipid envelope

  N. Huarte, P. Carravilla, A. Cruz, M. Lorizate, J.A. Nieto-Garai, H.G. Kräusslich, J. Perez-Gil, J.M. Requejo and J.L. Nieva

  Sci Rep 6 34190. doi: 10.1038/srep34190 (2016)

• Reply to The broadly neutralizing, anti-HIV antibody 4E10: an open and shut case?

  E. Rujas, N. Gulzar, K. Morante, K. Tsumoto, J.K. Scott, J.L. Nieva and J.M. Caaveiro

  J Virol. 90(6):3276-7. doi: 10.1128/JVI.02970-15 (2016)

• Ion channel activity of the CSFV p7 viroporin in surrogates of the ER lipid bilayer

  E. Largo, C. Verdiá-Báguena, V.M. Aguilella, J.L. Nieva and A. Alcaraz

  Biochim Biophys Acta.1858, 30-37 (2016)

• The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region

  Apellaniz B, Rujas E, Serrano S, Morante K, Tsumoto K, Caaveiro JM, Jimenez MA, Nieva JL

  J Biol Chem. 290:12999-3015 (2015)

• The Use of Liposomes to Shape Epitope Structure and Modulate Immunogenic Responses of Peptide Vaccines Against HIV MPER

  Apellaniz B, Nieva JL

  Adv Protein Chem Str Biol 99:15-54 (2015)

• Fusion-competent state induced by a C-terminal HIV-1 fusion peptide in cholesterol-rich membranes

  B. Apellániz J.L. Nieva.

  Biochim. Biophys. Acta 1848, 1014–1022 (2015)

• Two-Photon Laurdan Studies of the Ternary Lipid Mixture DOPC:SM:Cholesterol Reveal a Single Liquid Phase at Sphingomyelin:Cholesterol Ratios Lower Than 1

  P. Carravilla, J.L. Nieva, F.M. Goñi, J. Requejo-Isidro and N. Huarte

  Langmuir. 31(9):2808-17 (2015)

• Cholesterol-dependent membrane fusion induced by the gp41 membrane-proximal external region-transmembrane domain connection suggests a mechanism for broad HIV-1 neutralization.

  B. Apellániz, E. Rujas, P. Carravilla, J. Requejo-Isidro, N. Huarte, C. Domene and J.L. Nieva.

  J Virol. 88, 13367-13377 (2014).

• The three lives of viral fusion peptides

  B. Apellániz, N. Huarte, E. Largo and J.L. Nieva.

  Chem Phys Lipids. 181, 40-55 (2014).

• Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on classical swine fever virus replication.

  I.J. Fernández-Sainz, E. Largo, D.P. Gladue, P. Fletcher, V. O\'Donnell, L.G. Holinka, L.B. Carey, X. Lu, J.L. Nieva and M.V. Borca.

  Virology. 456, 121-130 (2014).

• Structure and immunogenicity of a peptide vaccine, including the complete HIV-1 gp41 2F5 epitope: implications for antibody recognition mechanism and immunogen design.

  S. Serrano, A. Araujo, B. Apellániz, S. Bryson, P. Carravilla, I. de la Arada, N. Huarte, E. Rujas, E.F. Pai, J.L.R. Arrondo, C. Domene, M.A. Jiménez and J.L. Nieva.

  J Biol Chem. 289, 6565-6580 (2014).

• Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function.

  E. Largo, D.P. Gladue, N. Huarte, M.V. Borca and J.L. Nieva.

  Antiviral Res. 101, 30-36 (2014).

• Charge pair interactions in transmembrane helices and turn propensity of the connecting sequence promote helical hairpin insertion.

  M. Bañó-Polo, L. Martínez-Gil, B. Wallner, J.L. Nieva, A. Elofsson and I. Mingarro.

  J Mol Biol. 425, 830-840 (2013).

• Recognition of membrane-bound fusion-peptide/MPER complexes by the HIV-1 neutralizing 2F5 antibody: implications for Anti-2F5 immunogenicity.

  N. Huarte, A. Araujo, R. Arranz, M. Lorizate, H. Quendler, R. Kunert, J.M. Valpuesta and J.L. Nieva.

  PLoS One, 7, e52740. doi: 10.1371 (2012).

• Viroporins: structure and biological functions.

  J.L. Nieva, V. Madan and L. Carrasco.

  Nat Rev Microbiol. 10, 563-74 (2012).