title: Functional recombinants designed from a fetuin/asialofetuin-specific marine algal lectin, rhodobindin.
abstract: Plant lectins have attracted much attention for biomedical applications including targeted drug delivery system and therapy against tumors and microbial infections. The main problem of using lectins as a biomedical tool is a batch-to-batch variation in isoforms content. The production of lectins using recombination tools has the advantage of obtaining high amounts of proteins with more precise properties, but there are only a handful of functional recombinant lectins presently available. A fetuin/asialo-fetuin specific lectin, Rhodobindin, has unique tandem repeats structure which makes it useful in exploiting for recombinant lectin. We developed three functional recombinant lectins using E. coli expression system: one from full cDNA sequence and two from fragmentary sequences of Rhodobindin. Hemagglutinating activity and solubility of the recombinant lectins were highest at OD 0.7 cell concentration at 20 °C. The optimized process developed in this study was suitable for the quality-controlled production of high amounts of soluble recombinant lectins.
authors: Department of Biology, Kongju National University, Kongju 314-701, Korea. jwhan@kongju.ac.kr.|Marine Biodiversity Institute of Korea, Seocheon 427-100, Korea. jwhan@kongju.ac.kr.
authors: Jong Won
authors: JW
authors: Han
authors: Department of Biology, Kongju National University, Kongju 314-701, Korea. mgjung@kongju.ac.kr.
authors: Min Gui
authors: MG
authors: Jung
authors: Department of Biology, Kongju National University, Kongju 314-701, Korea. tlasud@kongju.ac.kr.
authors: Eun Young
authors: EY
authors: Shim
authors: Department of Biology, Kongju National University, Kongju 314-701, Korea. matthew80@kongju.ac.kr.
authors: Jun Bo
authors: JB
authors: Shim
authors: Department of Biology, Kongju National University, Kongju 314-701, Korea. ghkim@kongju.ac.kr.
authors: Young Min
authors: YM
authors: Kim
authors: Department of Biology, Kongju National University, Kongju 314-701, Korea.
authors: Gwang Hoon
authors: GH
authors: Kim
mesh_terms: D001212:Asialoglycoproteins / Q000378:metabolism*; D001665:Binding Sites; D016503:Drug Delivery Systems; D060748:Fetuins / Q000378:metabolism*; D015870:Gene Expression; D006386:Hemagglutination Tests; D016366:Open Reading Frames; D010140:Pacific Ocean; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D037121:Plant Lectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D015202:Protein Engineering; D054730:Protein Interaction Domains and Motifs; D055550:Protein Stability; D011786:Quality Control; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D056910:Republic of Korea; D000461:Rhodophyta / Q000737:chemistry* / Q000254:growth & development; D012624:Seaweed / Q000737:chemistry* / Q000254:growth & development; D012995:Solubility; D020080:Tandem Repeat Sequences; D013696:Temperature
chemical_list: D001212:Asialoglycoproteins; D060748:Fetuins; D010446:Peptide Fragments; D037121:Plant Lectins; D011994:Recombinant Proteins; C017029:asialofetuin