Editing Lectin (section)

==Use==
===In medicine and medical research===
Purified lectins are important in a clinical setting because they are used for [[blood typing]].<ref>{{Cite journal |doi=10.1093/glycob/cwh122 |pmid=15229195 |title=History of lectins: From hemagglutinins to biological recognition molecules |journal=Glycobiology |volume=14 |issue=11 |pages=53R–62R |year=2004 |last1=Sharon |first1=N. |last2=Lis |first2=H |doi-access=free}}</ref> Some of the glycolipids and glycoproteins on an individual's red blood cells can be identified by lectins.
* A lectin from ''[[Dolichos biflorus]]'' is used to identify cells that belong to the A1 blood group.
* A lectin from ''[[Ulex europaeus]]'' is used to identify the H blood group antigen.
* A lectin from ''[[Vicia graminea]]'' is used to identify the N blood group antigen.
* A lectin from ''[[Iberis amara]]'' is used to identify the M blood group antigen.
Non blood-group antigens can be identified by lectins:
* A lectin from [[coconut milk]] is used to identify ''Theros'' antigen.
* A lectin from ''[[Carex]]'' is used to identify R antigen.
In neuroscience, the [[anterograde labeling method]] is used to trace the path of [[efferent nerve fiber|efferent]] [[axon]]s with [[PHA-L]], a lectin from the [[kidney bean]].<ref name="Carlson">{{cite book |author=Carlson, Neil R. |title=Physiology of behavior |publisher=Pearson Allyn & Bacon |location=Boston |year=2007 |isbn=978-0-205-46724-2}}{{page?|date=May 2025}}</ref>

A lectin ([[BanLec]]) from bananas inhibits [[HIV-1]] ''in vitro''.<ref>{{cite journal |doi=10.1074/jbc.M109.034926 |pmid=20080975 |title=A Lectin Isolated from Bananas is a Potent Inhibitor of HIV Replication |journal=Journal of Biological Chemistry |volume=285 |issue=12 |pages=8646–8655 |year=2010 |last1=Swanson |first1=M. D. |last2=Winter |first2=H. C. |last3=Goldstein |first3=I. J. |last4=Markovitz |first4=D. M. |pmc=2838287 |doi-access=free}}</ref> Achylectins, isolated from ''Tachypleus tridentatus'', show specific agglutinating activity against human A-type erythrocytes. Anti-B agglutinins such as anti-BCJ and anti-BLD separated from ''Charybdis japonica'' and ''Lymantria dispar'', respectively, are of value both in routine blood grouping and research.<ref>{{cite journal |doi=10.1080/11250003.2010.492794 |title=Prospect for lectins in arthropods |journal=Italian Journal of Zoology |volume=77 |issue=3 |pages=254–260 |year=2010 |last1=Viswambari Devi |first1=R. |last2=Basilrose |first2=M. R. |last3=Mercy |first3=P. D. |s2cid=84825587|doi-access=free }}</ref>

===In studying carbohydrate recognition by proteins===
[[File:Parasite160010-fig2 - Lectins in Paralichthys olivaceus infected by Kudoa septempunctata - Lectin histochemistry.png|thumb|Lectin [[histochemistry]] of fish muscles infected by a [[myxozoa]]n]]
Lectins from legume plants, such as [[Phytohaemagglutinin|PHA]] or [[concanavalin A]], have been used widely as model systems to understand the molecular basis of how proteins recognize carbohydrates, because they are relatively easy to obtain and have a wide variety of sugar specificities. The many [[crystal structures]] of legume lectins have led to a detailed insight of the atomic interactions between carbohydrates and proteins.

Legume seed lectins have been studied for their insecticidal potential and have shown harmful effects for the development of pest.<ref>{{cite journal | doi=10.1016/j.cbpb.2022.110770 | title=Characterization and expression of prohibitin during the mexican bean weevil (Zabrotes subfasciatus, Boheman, 1833) larvae development | date=2022 | last1=Villegas-Coronado | first1=Diana | last2=Guzman-Partida | first2=Ana María | last3=Aispuro-Hernandez | first3=Emmanuel | last4=Vazquez-Moreno | first4=Luz | last5=Huerta-Ocampo | first5=José Ángel | last6=Sarabia-Sainz | first6=José Andre-i | last7=Teran-Saavedra | first7=Nayelli Guadalupe | last8=Minjarez-Osorio | first8=Christian | last9=Castro-Longoria | first9=Reina | last10=Maldonado | first10=Amir | last11=Lagarda-Diaz | first11=Irlanda | journal=Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | volume=262 | page=110770 | pmid=35644320 | s2cid=249145357 }}</ref>

===As a biochemical tool===
Concanavalin A and other commercially available lectins have been used widely in [[affinity chromatography]] for purifying glycoproteins.<ref>{{cite web |url=http://legacy.gelifesciences.com/webapp/wcs/stores/servlet/catalog/en/GELifeSciences-se/products/AlternativeProductStructure_17334/ |title=Immobilized Lectin |website=legacy.gelifesciences.com }}{{Dead link|date=February 2023 |bot=InternetArchiveBot |fix-attempted=yes }}</ref>

In general, proteins may be characterized with respect to [[glycoform]]s and carbohydrate structure by means of [[affinity chromatography]], [[blotting]], [[affinity electrophoresis]], and [[immunoelectrophoresis|affinity immunoelectrophoreis]] with lectins, as well as in [[microarray]]s, as in [[wikt:evanescent|evanescent]]-field fluorescence-assisted lectin microarray.<ref>[http://www.gpbio.jp/english/tech.html Glyco Station, Lec Chip, Glycan profiling technology] {{webarchive |url=https://web.archive.org/web/20100223005811/http://www.gpbio.jp/english/tech.html |date=2010-02-23 }}</ref>

===In biochemical warfare===
One example of the powerful biological attributes of lectins is the biochemical warfare agent ricin. The protein ricin is isolated from seeds of the [[castor oil plant]] and comprises two [[protein domains]]. [[Abrin]] from the [[Rosary pea|jequirity pea]] is similar:
* One domain is a lectin that binds cell surface galactosyl residues and enables the protein to enter cells.
* The second domain is an N-[[glycosidase]] that cleaves nucleobases from ribosomal RNA, resulting in inhibition of protein synthesis and cell death.