Detailed Information on Publication Record
2014
Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies
KUMAR, Atul, Petra SÝKOROVÁ, Gabriel DEMO and Michaela WIMMEROVÁBasic information
Original name
Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies
Authors
KUMAR, Atul (356 India, belonging to the institution), Petra SÝKOROVÁ (203 Czech Republic, belonging to the institution), Gabriel DEMO (703 Slovakia, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)
Edition
Frontiers in Material and Life Sciences, Brno Czech Republic, 2014
Other information
Language
English
Type of outcome
Konferenční abstrakt
Field of Study
10600 1.6 Biological sciences
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
RIV identification code
RIV/00216224:14740/14:00074228
Organization unit
Central European Institute of Technology
ISBN
978-80-210-7159-9
Keywords (in Czech)
Lectin Photorhabdus luminisnce
Keywords in English
Lectin Insect pathogen Photorhabdus luminisnce
Tags
Reviewed
Změněno: 31/12/2014 17:29, Mgr. Gabriel Demo, Ph.D.
Abstract
V originále
Photorhabdus luminescence is Gram-negative bacilli, exhibit duel nature of lifecycle one, being pathogenic towards insect whereas other, symbiosis with entamo-pathogenic nematodes. The lectin gene was amplified from the genome of P. luminescence and cloned with polyhistidine tag. Expression and production of the lectin was optimized and further purified it using nickel affinity chromatography. The lectin was found to be tetramer of 160 kDa exhibiting 41 kDa monomers interconnected with disulphide bridge. Crystallization of the lectin was achieved after various screening kits and optimized further by hanging drop method. The crystal structure was solved at 1.8 A resolution. The lectin was found to be seven-bladed beta-propeller fold with possibly two different binding sites per monomer. One of the binding site was found to be fucose specific however other was also suggested to be saccharide specificity probably towards a saccharide with higher level of hydroxylation than L-fucopyranose. Lectin was found to exhibit binding ability to haemocytes from insect larvae however was not found to be lethal to Galleria mellonella insect larvae
Links
CZ.1.05/1.1.00/02.0068, interní kód MU |
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GA13-25401S, research and development project |
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