Purification and Characterization of a Lectin with High Hemagglutination Property Isolated from <Emphasis Type="Italic">Allium altaicum</Emphasis> |
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| Authors: | Santosh Kumar Upadhyay Sharad Saurabh Rahul Singh Preeti Rai Neeraj Kumar Dubey K Chandrashekar Kuldeep Singh Negi Rakesh Tuli P K Singh |
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| Institution: | (1) Council of Scientific and Industrial Research, National Botanical Research Institute, Rana Pratap Marg, Lucknow, Uttar Pradesh, 226001, India;(2) Department of Biotechnology, National Agri-Food Biotechnology Institute, C-127, Phase VIII, Industrial Area, SAS Nagar, Mohali, Punjab, 160071, India;(3) National Bureau of Plant Genetic Resources, Regional Station, Bhowali, Nainital, Uttarakhand, 263132, India; |
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| Abstract: | A lectin was purified from the leaves of Allium altaicum and corresponding gene was cloned. The lectin namely Allium altaicum agglutinin (AAA) was ~24 kDa homodimeric protein and similar to a typical garlic leaf lectin. It was synthesized as 177 amino
acid residues pre-proprotein, which consisted of 28 and 43 amino acid long N and C-terminal signal peptides, respectively.
The plant expressed this protein more in scapes and flowers in comparison to the bulbs and leaves. Hemagglutination activity
(with rabbit erythrocytes) was 1,428 fold higher as compared to Allium sativum leaf agglutinin (ASAL) although, the insecticidal activity against cotton aphid (Aphis gossypii) was relatively low. Glycan array revealed that AAA had higher affinity towards GlcAb1-3Galb as compared to ASAL. Homology
analysis showed 57–94% similarity with other Allium lectins. The mature protein was expressed in E. coli as a fusion with SUMO peptide in soluble and biologically active form. Recombinant protein retained high hemagglutination activity. |
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