{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T21:45:03Z","timestamp":1787694303200,"version":"build-2784847793"},"reference-count":80,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,9,23]],"date-time":"2022-09-23T00:00:00Z","timestamp":1663891200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cell. Infect. Microbiol."],"abstract":"<jats:p>Cyanovirin-N (CV-N), a lectin from <jats:italic>Nostoc ellipsosporum<\/jats:italic> was found an infusion inhibitory protein for human immunodeficiency virus (HIV)-1. A tandem-repeat of the engineered domain-swapped dimer bound specific sites at hemagglutinin (HA), Ebola and HIV spike glycoproteins as well as dimannosylated HA peptide, N-acetyl-D-glucosamine and high-mannose containing oligosaccharides. Among these, CV-N bound the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) spike protein at a dissociation constant (K<jats:sub>D<\/jats:sub>) of 18.6 \u00b5M (and K<jats:sub>D<\/jats:sub>=260 \u00b5M to RBD), which was low-affinity carbohydrate-binding as compared with the recognition of the other viral spikes. Binding of dimannosylated peptide to homo-dimeric CVN2 and variants of CVN2 that were pairing Glu-Arg residues sterically located close to its high-affinity carbohydrate binding sites, was measured using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC). Binding affinity increased with polar interactions, when the mutated residues were used to substitute a single, or two disulfide bonds, in CVN2. Site-specific N-linked glycans on spikes were mediating the infection with influenza virus by broadly neutralizing antibodies to HA and lectin binding to HA was further investigated <jats:italic>via<\/jats:italic> modes of saturation transfer difference (STD)-NMR. Our findings showed that stoichiometry and the lectin\u2019s binding affinity were revealed by an interaction of CVN2 with dimannose units and either the high- or low-affinity binding site. To understand how these binding mechanisms add to viral membrane fusion we compare our tested HA-derived peptides in affinity with SARS-CoV-2 glycoprotein and review lectins and their mechanisms of binding to enveloped viruses for a potential use to simulate neutralization ability.<\/jats:p>","DOI":"10.3389\/fcimb.2022.990875","type":"journal-article","created":{"date-parts":[[2022,9,23]],"date-time":"2022-09-23T12:59:13Z","timestamp":1663937953000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":3,"title":["Engineering recombinantly expressed lectin-based antiviral agents"],"prefix":"10.3389","volume":"12","author":[{"given":"Irene","family":"Maier","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,9,23]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"2134","DOI":"10.3390\/molecules26082134","article-title":"Algae-derived bioactive molecules for the potential treatment of SARS-CoV-2","volume":"26","author":"Alam","year":"2021","journal-title":"Molecules"},{"key":"B2","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/j.virol.2010.03.021","article-title":"Mannose-rich glycosylation patterns on HIV-1 subtype c gp120 and sensitivity to the lectins, griffithsin, cyanovirin-n and scytovirin","volume":"402","author":"Alexandre","year":"2010","journal-title":"J. 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