1Genetic Engineering of Bacteria laboratory, Division of Bacteriology and Mycology, Indian Veterinary Research Institute, Izatnagar, India
2Centre of Excellence in Agriculture Biotechnology, Sardar Vallabhbhai Patel University of Agriculture and Technology, Meerut, Uttar Pradesh, India
3Department of Immunology and Defense Mechanism, Sardar Vallabhbhai Patel University of Agriculture and Technology, Meerut, Uttar Pradesh, India
4Department of Molecular Biology & Genetic Engineering, Sardar Vallabhbhai Patel University of Agriculture and Technology, Meerut, Uttar Pradesh, India
5Department of Plant Physiology, Institute of Agricultural Sciences, Banaras Hindu University, Varanasi, 221005, Uttar Pradesh, India
*Email: nehag0609@gmail.com
Online published on 15 March, 2014.
Lectins have always demonstrated their role in bearing insecticidal activity. They are although considered to be toxic for mammals but some studies have reported that the presence of mannose binding region is believed to impart non-toxic nature to lectins against mammals including humans. In the present investigation, the research was conducted to elucidate the relationship of lectin gene LECASAI with other previously cloned lectins having insecticidal activity and to ensure the presence of the conserved mannose binding region/site in LECASAI. In this study, we report isolation of LECASAI via PCR, Cloning, Characterization & Bioinformatics analysis of LECASAI isolated from Garlic (Allium sativum L.). The full length gene sequence of LECASAI obtained from sequencing consisted of 1029bp which was subjected to In-silico analysis in order to determine its ancestral relationship and the presence of the conserved mannose binding region within the sequence. Results from In-vitro analysis indicated a higher homology of LECASAI with those of insecticidal lectins and the presence of mannose binding region in LECASAI. This unique approach has not only helped us in understanding the relationship between these genes but may also enable us to obtain an insecticidal lectin carrying insecticidal activity to several insects pests (for which even Bt proteins have been reported to be ineffective), apart from being non-toxic for man, mammals and birds in the future.
Insect pests cause immense destruction and great losses to many of the important crop plants. Bt proteins have although proved as potential candidates against these pests but there are yet no Bt toxins effective against bugs, hoppers or aphids which feed on phloem sap.
Scientists have reported lectins to possess insecticidal properties against these insect pests but the toxic nature of lectins to man and animals left the researchers in a dilemma.
Studies are conducted on LECASAI lectin gene to determine its insecticidal activity and non-toxic nature for man, mammals and birds by elucidating the presence of mannose binding region within the gene sequence.
Bacillus thuringiensis, LECASAI, Allium sativum I lectin, Mannose Binding lectins
