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.

Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3

“…Most plants and algae have a heterogeneous mixture of lectin isoforms with diverse biological activities; therefore, a lectin isolated from natural sources is typically not preferred for medical applications [ 14 , 15 ]. In addition, the inability to obtain large amounts of lectins from natural sources is a major hurdle for medical uses.…”

Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii

“…This may contribute to the stability of lectin's tertiary structure and may be a substitute for the advantages conferred through multimeric structures [18,34]. The tandem repeat structure of GCL was considered to be preferable for our purposes, as this is shared with other red algal lectins and may contribute to an increase in hemagglutination activity [18,23,34]. Furthermore, the isolated GCL amino acid sequence interestingly represented high similarity with bacterial lectins as shown in Supplementary Figure S4.…”

“…Similar to other red algal lectins that have short peptide (~30-mer) tandem repeat structures [18], GCL possessed a repeat structure in its primary structure. This may contribute to the stability of lectin's tertiary structure and may be a substitute for the advantages conferred through multimeric structures [18,34]. The tandem repeat structure of GCL was considered to be preferable for our purposes, as this is shared with other red algal lectins and may contribute to an increase in hemagglutination activity [18,23,34].…”

Karakterisasi Biokimia Lektin Makroalga Sargassum polycystum dan Turbinaria ornata/Biochemical Characterisation of Lectin Derived from Sargassum polycystum and Turbinaria ornata Macroalgae

“…Sementara itu, lektin S. polycystum yang mempunyai spesifisitas pengikatan terhadap fetuin berpotensi untuk dikembangkan sebagai protein penghantar obat (drug delivery protein). Fetuin yang diproduksi di liver dan dialirkan ke seluruh pembuluh darah merupakan bagian dari kelompok protein pembawa (carrier protein) yang memediasi transport berbagai substansi dalam pembuluh darah (Han et al, 2015).…”