ArticleMarine drugs2015
Functional recombinants designed from a fetuin/asialofetuin-specific marine algal lectin, rhodobindin.
Article in Marine drugs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Exploring the Structural Diversity and Biotechnological Potential of the Rhodophyte Phycolectome.Marine drugs · 2024Review
- Anticancer Activity of Mannose-Specific Lectin, BPL2, from Marine Green AlgaMarine drugs · 2022Article
- Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga,Biomolecules · 2020Article
- Induction of Recombinant Lectin Expression by an Artificially Constructed Tandem Repeat Structure: A Case Study UsingBiomolecules · 2018Article
- Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3.Marine drugs · 2018Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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