Now showing items 1-6 of 6

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      Affinity for the Interface Underpins Potency of Antibodies Operating In Membrane Environments 

      Rujas Díez, Edurne; Insausti González, Sara; Leaman, Daniel P.; Carravilla Palomanes, Pablo; González Resines, Saul; Monceaux, Valérie; Sánchez Eugenia, Rubén ORCID; García Porras, Miguel; Iloro, Ibon; Zhang, Lei; Elortza, Felix; Julien, Jean Philippe; Sáez Cirión, Asier; Zwick, Michael B.; Eggeling, Christian; Ojida, Akio; Domene, Carmen; Caaveiro, Jose M.M.; Nieva Escandón, José Luis (Cell Press, 2020-08-18)
      The contribution of membrane interfacial interactions to recognition of membrane-embedded antigens by antibodies is currently unclear. This report demonstrates the optimization of this type of antibodies via chemical ...
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      Focal accumulation of aromaticity at the CDRH3 loop mitigates 4E10 polyreactivity without altering its HIV neutralization profile 

      Rujas Díez, Edurne; Leaman, Daniel P.; Insausti González, Sara; Carravilla Palomanes, Pablo; García Porras, Miguel; Largo Pereda, Eneko; Morillo Melero, Izaskun; Sánchez Eugenia, Rubén ORCID; Zhang, Lei; Cui, Hong; Iloro, Ibon; Elortza, Felix; Julien, Jean-Philippe; Eggeling, Christian; Zwick, Michael B.; Caaveiro, Jose M.M.; Nieva Escandón, José Luis (Cell Press, 2021-09-24)
      Broadly neutralizing antibodies (bnAbs) against HIV-1 are frequently associated with the presence of autoreactivity/polyreactivity, a property that can limit their use as therapeutic agents. The bnAb 4E10, targeting the ...
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      Functional Delineation of a Protein–Membrane Interaction Hotspot Site on the HIV-1 Neutralizing Antibody 10E8 

      Insausti González, Sara; García Porras, Miguel; Torralba Iturbe, Johana ORCID; Morillo Melero, Izaskun; Ramos Caballero, Ander; De la Arada Echevarría, Igor ORCID; Apellaniz Unzalu, Beatriz ORCID; Caaveiro, Jose M.M.; Carravilla Palomanes, Pablo; Eggeling, Christian; Rujas Díez, Edurne; Nieva Escandón, José Luis (MDPI, 2022-09-15)
      Antibody engagement with the membrane-proximal external region (MPER) of the envelope glycoprotein (Env) of HIV-1 constitutes a distinctive molecular recognition phenomenon, the full appreciation of which is crucial for ...
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      Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope. 

      Torralba Iturbe, Johana ORCID; De la Arada Echevarría, Igor ORCID; Partida Hanon, Angélica; Rujas Díez, Edurne; Arribas, Madalen; Insausti Gonzalez, Sara; Valotteau, Claire; Valle García, Javier; Andreu, David; Caaveiro, Jose M.M.; Jiménez, María Ángeles; Apellaniz Unzalu, Beatriz ORCID; Redondo Morata, Lorena; Nieva Escandón, José Luis (Nature, 2022)
      Antibodies against the carboxy-terminal section of the membrane-proximal external region (C-MPER) of the HIV-1 envelope glycoprotein (Env) are considered as nearly pan-neutralizing. Development of vaccines capable of ...
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      Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface 

      Rujas Díez, Edurne; Caaveiro, Jose M.M.; Partida Hanon, Angélica; Gulzar, Naveed; Morante, Koldo; Apellaniz Unzalu, Beatriz ORCID; García Porras, Miguel; Bruix, Marta; Tsumoto, Kouhei; Scott, Jamie K.; Jiménez, María Ángeles; Nieva Escandón, José Luis (Springer Nature, 2016-12-01)
      The mechanism by which the HIV-1 MPER epitope is recognized by the potent neutralizing antibody 10E8 at membrane interfaces remains poorly understood. To solve this problem, we have optimized a 10E8 peptide epitope and ...
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      The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region 

      Apellaniz Unzalu, Beatriz ORCID; Rujas Díez, Edurne; Serrano, Soraya; Morante, Koldo; Tsumoto, Kouhei; Caaveiro, Jose M.M.; Jiménez, María Ángeles; Nieva Escandón, José Luis (Elsevier, 2015-03-18)
      The membrane-proximal external region (MPER) C-terminal segment and the transmembrane domain (TMD) of gp41 are involved in HIV-1 envelope glycoprotein-mediated fusion and modulation of immune responses during viral infection. ...