Recombinant Lectin from insect pathogen Photorhabdus 
luminisnce: structural and functional studies

a 2014

Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies

KUMAR, Atul; Petra SÝKOROVÁ; Gabriel DEMO a Michaela WIMMEROVÁ

Základní údaje

Originální název

Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies

Autoři

KUMAR, Atul; Petra SÝKOROVÁ ; Gabriel DEMO a Michaela WIMMEROVÁ

Vydání

Frontiers in Material and Life Sciences, Brno Czech Republic, 2014

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10600 1.6 Biological sciences

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/14:00074228

Organizační jednotka

Středoevropský technologický institut

ISBN

978-80-210-7159-9

Klíčová slova česky

Lectin Photorhabdus luminisnce

Klíčová slova anglicky

Lectin Insect pathogen Photorhabdus luminisnce

Příznaky

Recenzováno

Změněno: 31. 12. 2014 17:29, Mgr. Gabriel Demo, Ph.D.

Anotace

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

Návaznosti

CZ.1.05/1.1.00/02.0068, interní kód MU

Název: CEITEC - středoevropský technologický institut (Akronym: CEITEC)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC - středoevropský technologický institut, 1.1 Evropská centra excelence

GA13-25401S, projekt VaV

Název: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu

Investor: Grantová agentura ČR, Studium proteinu z patogenu zapojených do rozpoznávání hostitelského organismu

Citovat

KUMAR, Atul; Petra SÝKOROVÁ; Gabriel DEMO a Michaela WIMMEROVÁ. Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies. In Frontiers in Material and Life Sciences, Brno Czech Republic. 2014. ISBN 978-80-210-7159-9.

@proceedings{1214483,
   author = {Kumar, Atul and Sýkorová, Petra and Demo, Gabriel and Wimmerová, Michaela},
   booktitle = {Frontiers in Material and Life Sciences, Brno Czech Republic},
   keywords = {Lectin Insect pathogen Photorhabdus luminisnce},
   language = {eng},
   isbn = {978-80-210-7159-9},
   title = {Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies},
   url = {http://www.ceitec.eu/ac2014-book-of-abstract/f32414},
   year = {2014}
}

TY  - CONF
ID  - 1214483
AU  - Kumar, Atul - Sýkorová, Petra - Demo, Gabriel - Wimmerová, Michaela
PY  - 2014
TI  - Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies
SN  - 9788021071599
KW  - Lectin Insect pathogen Photorhabdus luminisnce
UR  - http://www.ceitec.eu/ac2014-book-of-abstract/f32414
N2  - 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
ER  -

KUMAR, Atul; Petra SÝKOROVÁ; Gabriel DEMO a Michaela WIMMEROVÁ. Recombinant Lectin from insect pathogen Photorhabdus luminisnce: structural and functional studies. In \textit{Frontiers in Material and Life Sciences, Brno Czech Republic}. 2014. ISBN~978-80-210-7159-9.

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