Abstract
Lectin is an important protein in medical and pharmacological applications. Impurities in lectin derived from natural sources and the generation of inactive proteins by recombinant technology are major obstacles for the use of lectins. Expressing recombinant lectin with a tandem repeat structure can potentially overcome these problems, but few studies have systematically examined this possibility. This was investigated in the present study using three distinct forms of recombinant mannose-binding lectin from Bryopsis plumosa (BPL2)—i.e., the monomer (rD1BPL2), as well as the dimer (rD2BPL2), and tetramer (rD4BPL2) arranged as tandem repeats. The concentration of the inducer molecule isopropyl β-D-1-thiogalactopyranoside and the induction time had no effect on the efficiency of the expression of each construct. Of the tested constructs, only rD4BPL2 showed hemagglutination activity towards horse erythrocytes; the activity of towards the former was 64 times higher than that of native BPL2. Recombinant and native BPL2 showed differences in carbohydrate specificity; the activity of rD4BPL2 was inhibited by the glycoprotein fetuin, whereas that of native BPL2 was also inhibited by d-mannose. Our results indicate that expression as tandem repeat sequences can increase the efficiency of lectin production on a large scale using a bacterial expression system.
Highlights
Lectins are antibody-like proteins that bind to carbohydrates [1] via two or more sugar-binding sites [2]
An active form of rBPL2 was successfully generated from a construct with artificial tandem repeats of the lectin sequence
The tetramer potently induced hemagglutination of erythrocytes to a degree that was comparable to native BPL2
Summary
Lectins are antibody-like proteins that bind to carbohydrates [1] via two or more sugar-binding sites [2]. Lectins can agglutinate erythrocytes by binding the surface carbohydrates of red blood cells [1], and they are referred to as agglutinin or hemagglutinin. Owing to this property, lectins can serve as pharmacological agents and as a diagnostic and therapeutic tool [3,4,5]. Lectins can serve as pharmacological agents and as a diagnostic and therapeutic tool [3,4,5] They are used in combination with fluorophores to characterize cell-surface carbohydrates [6]. Lectins have been used in combination with a microarray approach to analyze the bacterial glycome [11]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
