Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2021-08-31

AUTHORS

Florian A. Lempp, Leah B. Soriaga, Martin Montiel-Ruiz, Fabio Benigni, Julia Noack, Young-Jun Park, Siro Bianchi, Alexandra C. Walls, John E. Bowen, Jiayi Zhou, Hannah Kaiser, Anshu Joshi, Maria Agostini, Marcel Meury, Exequiel Dellota, Stefano Jaconi, Elisabetta Cameroni, Javier Martinez-Picado, Júlia Vergara-Alert, Nuria Izquierdo-Useros, Herbert W. Virgin, Antonio Lanzavecchia, David Veesler, Lisa A. Purcell, Amalio Telenti, Davide Corti

ABSTRACT

SARS-CoV-2 infection—which involves both cell attachment and membrane fusion—relies on the angiotensin-converting enzyme 2 (ACE2) receptor, which is paradoxically found at low levels in the respiratory tract1–3, suggesting that there may be additional mechanisms facilitating infection. Here we show that C-type lectin receptors, DC-SIGN, L-SIGN and the sialic acid–binding immunoglobulin-like lectin 1 (SIGLEC1) function as attachment receptors by enhancing ACE2-mediated infection and modulating the neutralizing activity of different classes of spike-specific antibodies. Antibodies to the amino-terminal domain or to the conserved site at the base of the receptor-binding domain, while poorly neutralizing infection of ACE2-overexpressing cells, effectively block lectin-facilitated infection. Conversely, antibodies to the receptor binding motif, while potently neutralizing infection of ACE2-overexpressing cells, poorly neutralize infection of cells expressing DC-SIGN or L-SIGN and trigger fusogenic rearrangement of the spike, promoting cell-to-cell fusion. Collectively, these findings identify a lectin-dependent pathway that enhances ACE2-dependent infection by SARS-CoV-2 and reveal distinct mechanisms of neutralization by different classes of spike-specific antibodies. More... »

PAGES

342-347

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41586-021-03925-1

    DOI

    http://dx.doi.org/10.1038/s41586-021-03925-1

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1140772677

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/34464958


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