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dc.contributor.authorBishnoi, Ritika
dc.contributor.authorSousa, Gregory L
dc.contributor.authorContet, Alicia
dc.contributor.authorDay, Christopher J
dc.contributor.authorHou, Chun-Feng David
dc.contributor.authorProfitt, Lauren A
dc.contributor.authorSingla, Deepak
dc.contributor.authorJennings, Michael P
dc.contributor.authorValentine, Ann M
dc.contributor.authorPovelones, Michael
dc.contributor.authorBaxter, Richard HG
dc.date.accessioned2020-02-24T00:59:59Z
dc.date.available2020-02-24T00:59:59Z
dc.date.issued2019
dc.identifier.issn2045-2322
dc.identifier.doi10.1038/s41598-019-51353-z
dc.identifier.urihttp://hdl.handle.net/10072/391804
dc.description.abstractMalaria, the world’s most devastating parasitic disease, is transmitted between humans by mosquitoes of the Anopheles genus. An. gambiae is the principal malaria vector in Sub-Saharan Africa. The C-type lectins CTL4 and CTLMA2 cooperatively influence Plasmodium infection in the malaria vector Anopheles. Here we report the purification and biochemical characterization of CTL4 and CTLMA2 from An. gambiae and An. albimanus. CTL4 and CTLMA2 are known to form a disulfide-bridged heterodimer via an N-terminal tri-cysteine CXCXC motif. We demonstrate in vitro that CTL4 and CTLMA2 intermolecular disulfide formation is promiscuous within this motif. Furthermore, CTL4 and CTLMA2 form higher oligomeric states at physiological pH. Both lectins bind specific sugars, including glycosaminoglycan motifs with β1-3/β1-4 linkages between glucose, galactose and their respective hexosamines. Small-angle x-ray scattering data supports a compact heterodimer between the CTL domains. Recombinant CTL4/CTLMA2 is found to function in vivo, reversing the enhancement of phenol oxidase activity in dsCTL4-treated mosquitoes. We propose these molecular features underline a common function for CTL4/CTLMA2 in mosquitoes, with species and strain-specific variation in degrees of activity in response to Plasmodium infection.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherSpringer Science and Business Media LLC
dc.relation.ispartofpagefrom15191
dc.relation.ispartofissue1
dc.relation.ispartofjournalScientific Reports
dc.relation.ispartofvolume9
dc.subject.fieldofresearchHost-parasite interactions
dc.subject.fieldofresearchMedical parasitology
dc.subject.fieldofresearchClinical sciences
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchcode310407
dc.subject.fieldofresearchcode320704
dc.subject.fieldofresearchcode3202
dc.subject.fieldofresearchcode3107
dc.titleSolution structure, glycan specificity and of phenol oxidase inhibitory activity of Anopheles C-type lectins CTL4 and CTLMA2
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationBishnoi, R; Sousa, GL; Contet, A; Day, CJ; Hou, CFD; Profitt, LA; Singla, D; Jennings, MP; Valentine, AM; Povelones, M; Baxter, RHG, Solution structure, glycan specificity and of phenol oxidase inhibitory activity of Anopheles C-type lectins CTL4 and CTLMA2, Scientific Reports, 2019, 9 (1), pp. 15191-
dcterms.dateAccepted2019-09-27
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
dc.date.updated2020-02-24T00:56:09Z
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 2019 The Authors. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
gro.hasfulltextFull Text
gro.griffith.authorJennings, Michael P.
gro.griffith.authorDay, Christopher J.


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