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HIV

Potency needs constancy

Nature volume 514, pages 442–443 (2014)Cite this article

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In a finding that highlights ways to optimize the efficacy of antibody-based therapeutics and vaccines, the activity of potent HIV-1-neutralizing antibodies has been confirmed to depend on cellular binding to the antibodies' Fc regions.

Protection conferred against virus infection by licensed antiviral vaccines is mostly due to the generation of 'neutralizing' antibodies that bind to virus particles in such a way that they block their entry into a cell1. Current strategies for designing treatments and vaccines for HIV-1 focus on such antibodies, particularly on the highly potent, broadly neutralizing antibodies that are produced during the immune responses of rare infected individuals2,3 and which bind to the envelope protein (a highly variable protein) of multiple strains of the virus. However, it is becoming clear that the impact of these antibodies is not limited to direct viral neutralization through binding. Writing in Cell, Bournazos et al.4 show that in vivo activity of even the most potent broadly neutralizing anti-HIV-1 antibodies relies on antiviral functions that are triggered by binding of cellular receptors — the Fcγ receptors — to the 'tail' region of antibodies of the immunoglobulin G class, binding that was previously found5 to be crucial for sustaining the in vivo activity of less-potent neutralizing antibodies.

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Figure 1: Antibody-mediated viral control.

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  1. Alexandra Trkola is at the Institute of Medical Virology, University of Zurich, 8057 Zurich, Switzerland.,

    Alexandra Trkola

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  1. Alexandra Trkola
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Correspondence to Alexandra Trkola.

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Trkola, A. Potency needs constancy. Nature 514, 442–443 (2014). https://doi.org/10.1038/514442a

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