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

Pablo Carravilla, Jakub Chojnacki, Edurne Rujas, Sara Insausti, Eneko Largo, Dominic Waithe, Beatriz Apellaniz, Taylor Sicard, Jean-Philippe Julien, Christian Eggeling () and José L. Nieva ()
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Pablo Carravilla: University of the Basque Country (UPV/EHU)
Jakub Chojnacki: University of Oxford
Edurne Rujas: University of the Basque Country (UPV/EHU)
Sara Insausti: University of the Basque Country (UPV/EHU)
Eneko Largo: University of the Basque Country (UPV/EHU)
Dominic Waithe: University of Oxford
Beatriz Apellaniz: University of the Basque Country (UPV/EHU)
Taylor Sicard: The Hospital for Sick Children Research Institute
Jean-Philippe Julien: The Hospital for Sick Children Research Institute
Christian Eggeling: University of Oxford
José L. Nieva: University of the Basque Country (UPV/EHU)

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract 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 of knowledge on the MPER native structure and accessibility, different and exclusive models have been proposed for the molecular mechanism of MPER recognition by broadly neutralizing antibodies. Here, accessibility of antibodies to the native Env MPER on single virions has been addressed through STED microscopy. STED imaging of fluorescently labeled Fabs reveals a common pattern of native Env recognition for HIV-1 antibodies targeting MPER or the surface subunit gp120. In the case of anti-MPER antibodies, the process evolves with extra contribution of interactions with the viral lipid membrane to binding specificity. Our data provide biophysical insights into the recognition of the potent and broadly neutralizing MPER epitope on HIV virions, and as such is of importance for the design of therapeutic interventions.

Date: 2019
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DOI: 10.1038/s41467-018-07962-9

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