Search Results - "Insausti, Sara"

Engineering pan-HIV-1 neutralization potency through multispecific antibody avidity by Rujas, Edurne, Cui, Hong, Burnie, Jonathan, Aschner, Clare Burn, Zhao, Tiantian, Insausti, Sara, Muthuraman, Krithika, Semesi, Anthony, Ophel, Jasper, Nieva, Jose L, Seaman, Michael S, Guzzo, Christina, Treanor, Bebhinn, Julien, Jean-Philippe

“…Deep mining of B cell repertoires of HIV-1-infected individuals has resulted in the isolation of dozens of HIV-1 broadly neutralizing antibodies (bNAbs). Yet,…”
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Molecular recognition of the native HIV-1 MPER revealed by STED microscopy of single virions by Carravilla, Pablo, Chojnacki, Jakub, Rujas, Edurne, Insausti, Sara, Largo, Eneko, Waithe, Dominic, Apellaniz, Beatriz, Sicard, Taylor, Julien, Jean-Philippe, Eggeling, Christian, Nieva, José L.

“…Antibodies against the Membrane-Proximal External Region (MPER) of the Env gp41 subunit neutralize HIV-1 with exceptional breadth and potency. Due to the lack…”
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Functional Optimization of Broadly Neutralizing HIV-1 Antibody 10E8 by Promotion of Membrane Interactions by Rujas, Edurne, Leaman, Daniel P, Insausti, Sara, Ortigosa-Pascual, Lei, Zhang, Lei, Zwick, Michael B, Nieva, José L

“…The 10E8 antibody targets a helical epitope in the membrane-proximal external region (MPER) and transmembrane domain (TMD) of the envelope glycoprotein (Env)…”
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Functional Delineation of a Protein-Membrane Interaction Hotspot Site on the HIV-1 Neutralizing Antibody 10E8 by Insausti, Sara, Garcia-Porras, Miguel, Torralba, Johana, Morillo, Izaskun, Ramos-Caballero, Ander, de la Arada, Igor, Apellaniz, Beatriz, Caaveiro, Jose M M, Carravilla, Pablo, Eggeling, Christian, Rujas, Edurne, Nieva, Jose L

“…Antibody engagement with the membrane-proximal external region (MPER) of the envelope glycoprotein (Env) of HIV-1 constitutes a distinctive molecular…”
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Affinity for the Interface Underpins Potency of Antibodies Operating In Membrane Environments by Rujas, Edurne, Insausti, Sara, Leaman, Daniel P., Carravilla, Pablo, González-Resines, Saul, Monceaux, Valérie, Sánchez-Eugenia, Rubén, García-Porras, Miguel, Iloro, Ibon, Zhang, Lei, Elortza, Félix, Julien, Jean-Philippe, Saéz-Cirión, Asier, Zwick, Michael B., Eggeling, Christian, Ojida, Akio, Domene, Carmen, Caaveiro, Jose M.M., Nieva, José L.

“…The contribution of membrane interfacial interactions to recognition of membrane-embedded antigens by antibodies is currently unclear. This report demonstrates…”
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Peripheral Membrane Interactions Boost the Engagement by an Anti-HIV-1 Broadly Neutralizing Antibody by Rujas, Edurne, Caaveiro, José M.M., Insausti, Sara, García-Porras, Miguel, Tsumoto, Kouhei, Nieva, José L.

“…The 4E10 antibody displays an extreme breadth of HIV-1 neutralization and therefore constitutes a suitable model system for structure-guided vaccine design and…”
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On the antimicrobial properties and endurance of eugenol and 2-phenylphenol functionalized sol-gel coatings by Suárez-Vega, Ana, Berriozabal, Gemma, Perez de Iriarte, Juan, Lorenzo, Jaione, Álvarez, Noelia, Dominguez-Meister, Santiago, Insausti, Sara, Rujas, Edurne, Nieva, Jose L., Brizuela, Marta, Braceras, Iñigo

“…Preventing microbiological surface contamination in public spaces is nowadays of high priority. The proliferation of a microbial infection may arise through…”
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Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope by Torralba, Johana, de la Arada, Igor, Partida-Hanon, Angélica, Rujas, Edurne, Arribas, Madalen, Insausti, Sara, Valotteau, Claire, Valle, Javier, Andreu, David, Caaveiro, José M. M., Jiménez, María Angeles, Apellániz, Beatriz, Redondo-Morata, Lorena, Nieva, José L.

“…Antibodies against the carboxy-terminal section of the membrane-proximal external region (C-MPER) of the HIV-1 envelope glycoprotein (Env) are considered as…”
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Cholesterol Constrains the Antigenic Configuration of the Membrane-Proximal Neutralizing HIV‑1 Epitope by Torralba, Johana, de la Arada, Igor, Carravilla, Pablo, Insausti, Sara, Rujas, Edurne, Largo, Eneko, Eggeling, Christian, Arrondo, José L. R, Apellániz, Beatriz, Nieva, José L

“…The envelope glycoprotein (Env) enables HIV-1 cell entry through fusion of host-cell and viral membranes induced by the transmembrane subunit gp41. Antibodies…”
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Focal accumulation of aromaticity at the CDRH3 loop mitigates 4E10 polyreactivity without altering its HIV neutralization profile by Rujas, Edurne, Leaman, Daniel P., Insausti, Sara, Carravilla, Pablo, García-Porras, Miguel, Largo, Eneko, Morillo, Izaskun, Sánchez-Eugenia, Rubén, Zhang, Lei, Cui, Hong, Iloro, Ibon, Elortza, Félix, Julien, Jean-Philippe, Eggeling, Christian, Zwick, Michael B., Caaveiro, Jose M.M., Nieva, José L.

“…Broadly neutralizing antibodies (bnAbs) against HIV-1 are frequently associated with the presence of autoreactivity/polyreactivity, a property that can limit…”
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A two‐step mechanism for the binding of the HIV ‐1 MPER epitope by the 10 E 8 antibody onto biosensor‐supported lipid bilayers by García‐Porras, Miguel, Torralba, Johana, Insausti, Sara, Valle, Javier, Andreu, David, Apellániz, Beatriz, Nieva, José L.

“…HIV‐1 antibodies targeting the carboxy‐terminal area of the membrane‐proximal external region (ctMPER) are close to exerting viral pan‐neutralization. Here, we…”
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A two‐step mechanism for the binding of the HIV‐1 MPER epitope by the 10E8 antibody onto biosensor‐supported lipid bilayers by García‐Porras, Miguel, Torralba, Johana, Insausti, Sara, Valle, Javier, Andreu, David, Apellániz, Beatriz, Nieva, José L.

“…HIV‐1 antibodies targeting the carboxy‐terminal area of the membrane‐proximal external region (ctMPER) are close to exerting viral pan‐neutralization. Here, we…”
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Generation of a Nonbilayer Lipid Nanoenvironment after Epitope Binding Potentiates Neutralizing HIV‑1 MPER Antibody by Insausti, Sara, Ramos-Caballero, Ander, Wiley, Brian, González-Resines, Saul, Torralba, Johana, Elizaga-Lara, Anne, Shamblin, Christine, Ojida, Akio, Caaveiro, Jose M. M., Zwick, Michael B., Rujas, Edurne, Domene, Carmen, Nieva, José L.

“…Establishment of interactions with the envelope lipids is a cardinal feature of broadly neutralizing antibodies (bnAbs) that recognize the Env…”
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Cholesterol-Mediated Conformational Plasticity Restrains Immunogenicity and Promotes Membrane Fusion by an HIV Sequence Juxtaposed to the Lipid Envelope by Nieva, Jose L., Torralba, Johana, De la Arada, Igor, Insausti, Sara, Largo, Eneko, Tascon, Igor, Garcia-Porras, Miguel, Ubarretxena-Belandia, Iban, Apellaniz, Beatriz

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Strengthening Interactions with the Membrane Interface through Grafted Aromatic Compounds Produces Extremely Potent HIV-1 Neutralizing Antibodies by Nieva, Jose L., Rujas, Edurne, Insausti, Sara, Leaman, Daniel P., Carravilla, Pablo, Sanchez-Eugenia, Ruben, Zhang, Lei, Garcia-Porras, Miguel, Eggeling, Christian, Julien, Jean-Philippe, Ojida, Akio, Zwick, Michael B., Caaveiro, Jose M.

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Functional Contacts between MPER and the Anti-HIV-1 Broadly Neutralizing Antibody 4E10 Extend into the Core of the Membrane by Rujas, Edurne, Insausti, Sara, García-Porras, Miguel, Sánchez-Eugenia, Rubén, Tsumoto, Kouhei, Nieva, José L., Caaveiro, Jose M.M.

“…The exceptional breadth of broadly neutralizing antibodies (bNAbs) against the membrane-proximal external region (MPER) of the transmembrane protein gp41 makes…”
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Molecular Recognition at the Membrane Interface: Protein-Membrane Electrostatic Interactions Modulate the Biological Function of Anti-HIV Antibodies by Nieva, Jose L., Rujas, Edurne, Insausti, Sara, Leaman, Daniel P., Apellaniz, Beatriz, Torralba, Johana, Zhang, Lei, Caaveiro, Jose M., Zwick, Michael B.

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Single Virion Super-Resolution Microscopy Unveils Mechanistic Details of Env Glycoprotein Recognition by the Broadly Neutralizing HIV-1 Antibodies 4E10 and 10E8 by Carravilla, Pablo, Rujas, Edurne, Oar-Arteta, Itziar R, Insausti, Sara, Largo, Eneko, Chojnacki, Jakub, Sicard, Taylor, Julien, Jean-Philippe, Eggeling, Christian, Huarte, Nerea, Requejo-Isidro, José, Nieva, José L

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