{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T07:38:38Z","timestamp":1782459518147,"version":"3.54.5"},"reference-count":157,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2022,1,20]],"date-time":"2022-01-20T00:00:00Z","timestamp":1642636800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Pathogenic enveloped viruses are covered with a glycan shield that provides a dual function: the glycan structures contribute to virus protection as well as host cell recognition. The three classical types of N-glycans, in particular complex glycans, high-mannose glycans, and hybrid glycans, together with some O-glycans, participate in the glycan shield of the Ebola virus, influenza virus, human cytomegalovirus, herpes virus, human immunodeficiency virus, Lassa virus, and MERS-CoV, SARS-CoV, and SARS-CoV-2, which are responsible for respiratory syndromes. The glycans are linked to glycoproteins that occur as metastable prefusion glycoproteins on the surface of infectious virions such as gp120 of HIV, hemagglutinin of influenza, or spike proteins of beta-coronaviruses. Plant lectins with different carbohydrate-binding specificities and, especially, mannose-specific lectins from the Vicieae tribe, such as pea lectin and lentil lectin, can be used as glycan probes for targeting the glycan shield because of their specific interaction with the \u03b11,6-fucosylated core Man3GlcNAc2, which predominantly occurs in complex and hybrid glycans. Other plant lectins with Neu5Ac specificity or GalNAc\/T\/Tn specificity can also serve as potential glycan probes for the often sialylated complex glycans and truncated O-glycans, respectively, which are abundantly distributed in the glycan shield of enveloped viruses. The biomedical and therapeutical potential of plant lectins as antiviral drugs is discussed.<\/jats:p>","DOI":"10.3390\/cells11030339","type":"journal-article","created":{"date-parts":[[2022,1,20]],"date-time":"2022-01-20T22:40:20Z","timestamp":1642718420000},"page":"339","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1360-8491","authenticated-orcid":false,"given":"Annick","family":"Barre","sequence":"first","affiliation":[{"name":"UMR 152 PharmaDev, Institut de Recherche et D\u00e9veloppement, Facult\u00e9 de Pharmacie, Universit\u00e9 Paul Sabatier, 35 Chemin des Mara\u00eechers, F-31062 Toulouse, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9848-766X","authenticated-orcid":false,"given":"Els J. M.","family":"Van Damme","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, B-9000 Ghent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernard","family":"Klonjkowski","sequence":"additional","affiliation":[{"name":"UMR Virologie, INRA, ANSES, Ecole Nationale V\u00e9t\u00e9rinaire d\u2019Alfort, F-94700 Maisons-Alfort, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9303-5584","authenticated-orcid":false,"given":"Mathias","family":"Simplicien","sequence":"additional","affiliation":[{"name":"UMR 152 PharmaDev, Institut de Recherche et D\u00e9veloppement, Facult\u00e9 de Pharmacie, Universit\u00e9 Paul Sabatier, 35 Chemin des Mara\u00eechers, F-31062 Toulouse, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Sudor","sequence":"additional","affiliation":[{"name":"UMR 152 PharmaDev, Institut de Recherche et D\u00e9veloppement, Facult\u00e9 de Pharmacie, Universit\u00e9 Paul Sabatier, 35 Chemin des Mara\u00eechers, F-31062 Toulouse, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Herv\u00e9","family":"Benoist","sequence":"additional","affiliation":[{"name":"UMR 152 PharmaDev, Institut de Recherche et D\u00e9veloppement, Facult\u00e9 de Pharmacie, Universit\u00e9 Paul Sabatier, 35 Chemin des Mara\u00eechers, F-31062 Toulouse, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9936-7843","authenticated-orcid":false,"given":"Pierre","family":"Roug\u00e9","sequence":"additional","affiliation":[{"name":"UMR 152 PharmaDev, Institut de Recherche et D\u00e9veloppement, Facult\u00e9 de Pharmacie, Universit\u00e9 Paul Sabatier, 35 Chemin des Mara\u00eechers, F-31062 Toulouse, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,1,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1016\/j.cell.2018.02.054","article-title":"Common features of enveloped viruses and implications for immunogen design for next-generation vaccines","volume":"172","author":"Rey","year":"2018","journal-title":"Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/s00709-010-0152-6","article-title":"Mechanisms of viral entry: Seaking in the front door","volume":"244","author":"Thorley","year":"2010","journal-title":"Protoplasma"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1126\/science.1126548","article-title":"Crystal structure of glycoprotein B from herpes simplex virus 1","volume":"313","author":"Heldwein","year":"2006","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1038\/nature09555","article-title":"Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography","volume":"468","author":"Voss","year":"2010","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1128\/JVI.79.2.1223-1231.2005","article-title":"Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein","volume":"79","author":"Modis","year":"2005","journal-title":"J. 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