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Confocal microscopy of giant vesicles supports the absence of HIV‐1 neutralizing 2F5 antibody reactivity to plasma membrane phospholipids
Author(s) -
Apellaniz Beatriz,
García-Sáez Ana J.,
Huarte Nerea,
Kunert Renate,
Vorauer-Uhl Karola,
Katinger Hermann,
Schwille Petra,
Nieva José L.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.03.021
Subject(s) - epitope , monoclonal antibody , vesicle , membrane , chemistry , antibody , membrane curvature , confocal microscopy , phospholipid , biophysics , lipid bilayer , fluorescence microscope , microbiology and biotechnology , virology , biology , biochemistry , fluorescence , immunology , physics , quantum mechanics
The broadly neutralizing anti‐HIV‐1 2F5 monoclonal antibody recognizes a gp41 epitope proximal to the viral membrane. Potential phospholipid autoreactivity at cell surfaces has raised concerns about the use of this antibody for development of vaccines or immunotherapy. In this study, confocal microscopy of giant unilamellar vesicles (GUVs) was used to assess 2F5 reactivity with phospholipids assembled into bilayers with surface charge and curvature stress approximating those of the eukaryotic plasma membranes. Antibody partitioning into lipid bilayers required the specific recognition of membrane‐inserted epitope, indicating that 2F5 was unable to directly react with GUV phospholipids, even under fluid phase segregation conditions. Our results thus support the feasibility of raising 2F5‐like neutralizing responses through vaccination, and the medical safety of mAb infusions.