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Heterologous expression, purification and characterization of L-type lectin homologue from Leishmania donovani

dc.contributor.authorSingh, V.
dc.contributor.authorNair, D.N.
dc.contributor.authorKaushal, R.S.
dc.contributor.authorKumar, M.
dc.contributor.authorPappachan, A.
dc.contributor.authorSingh, D.D.
dc.date.accessioned2018-07-14T01:18:50Z
dc.date.available2018-07-14T01:18:50Z
dc.date.issued2015
dc.identifier.citationSingh, V., Nair, D. N., Kaushal, R. S., Kumar, M., Pappachan, A., & Singh, D. D. (2015). Heterologous expression, purification and characterization of L-type lectin homologue from Leishmania donovani. Biotechnology Reports, 8, 81-87. doi: 10.1016/j.btre.2015.09.004en_US
dc.identifier.issn2215017X
dc.identifier.urihttp://kr.cup.edu.in/handle/32116/1356
dc.description.abstractLeishmaniasis, a disease of the developing world affects about 12 million people and has limited therapeutic interventions available. L-type lectins, Endoplasmic Reticulum Golgi Intermediate Compartment/Vesicular Integral Proteins (ERGIC-53/VIP36) are involved in protein sorting in luminal compartments of animal cells and are important for parasite biology. A lectin homologue was identified through a bioinformatics analysis of Leishmania genome and it was found to have N-terminal conserved carbohydrate recognition domain (CRD) and a unique C-terminal region rich in repetitive amino acids and a poly glutamine tract. The N-terminal CRD region was cloned and expressed in Escherichia coli, but gave an insoluble expression which was re-solubilized by on column refolding. The fold integrity was checked through CD, fluorescence and functional assay of hemagglutination activity using rabbit erythrocyte. Bioinformatics analysis identified 15 members from Tritryps (Leishmania spp., Trypanosoma spp.) and they separate out as a distinct clade in the global phylogenetic analysis of all ERGIC-53/VIP36 sequences downloaded from Uniprot. Our analysis shows that the extended C-terminal regions with repeats is unique to Tritryps and this repeat pattern is different in sequences from Leishmania spp. and Trypanosoma spp. and all these features make this protein an interesting candidate for further detailed studies. ? 2015 The Author. Published by Elsevier B.V.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectlectin bioinformaticsen_US
dc.subjectfluorescenceen_US
dc.subjectgene amplificationen_US
dc.subjecthemagglutinationen_US
dc.subjectLeishmania donovanien_US
dc.subjectmass spectrometryen_US
dc.subjectnonhumanen_US
dc.subjectphylogenyen_US
dc.subjectpolyacrylamide gel electrophoresisen_US
dc.subjectpolymerase chain reactionen_US
dc.subjectprotein analysisen_US
dc.subjectprotein expressionen_US
dc.subjectprotein purificationen_US
dc.subjectprotein refoldingen_US
dc.subjectrabbiten_US
dc.subjectsequence analysisen_US
dc.subjectTrypanosomaen_US
dc.titleHeterologous expression, purification and characterization of L-type lectin homologue from Leishmania donovanien_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.btre.2015.09.004
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S2215017X15000545?via%3Dihub
dc.title.journalBiotechnology Reports
dc.type.accesstypeOpen Accessen_US


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