2017
Novel bangle lectin from Photorhabdus asymbiotica: sugar-binding specificity, structure and interaction with host immune system
HOUSER, Josef, Gita JANČAŘÍKOVÁ, Gabriel DEMO, Pavel DOBEŠ, Pavel HYRŠL et. al.Základní údaje
Originální název
Novel bangle lectin from Photorhabdus asymbiotica: sugar-binding specificity, structure and interaction with host immune system
Název česky
Nový bangle-lektin z Photorhabdus asymbiotica: specifita vůči sacharidům, struktura a interakce s imunitním systémem hostitele
Autoři
HOUSER, Josef (203 Česká republika, domácí), Gita JANČAŘÍKOVÁ (203 Česká republika, domácí), Gabriel DEMO (703 Slovensko, domácí), Pavel DOBEŠ (203 Česká republika, domácí), Pavel HYRŠL (203 Česká republika, domácí) a Michaela WIMMEROVÁ (203 Česká republika, garant, domácí)
Vydání
2017
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
Kód RIV
RIV/00216224:14740/17:00094888
Organizační jednotka
Středoevropský technologický institut
ISSN
Klíčová slova česky
lektin Photorhabdus struktura imunita
Klíčová slova anglicky
lectin Photorhabdus structure immunity
Štítky
Změněno: 17. 8. 2017 14:21, Mgr. Josef Houser, Ph.D.
Anotace
V originále
Photorhabdus asymbiotica is gram-negative bioluminescent bacteria living in a symbiotic relationship with nematodes from the genus Heterorhabditis. Together with nematode it forms a complex that is highly pathogenic for insects. However, while other three recognized species of the Photorhabdus genus are strictly entomopathogenic, P. asymbiotica is unique in its ability to act as an emerging human pathogen as well. Analysis of the P. asymbiotica genome identified a novel lectin designated PHL. Recombinant protein was purified and characterized. It exhibited high affinity for fucosylated carbohydrates including saccharides from bacterial cell wall or human blood epitopes. It inhibits the production of reactive oxygen species in human blood and antimicrobial activity both in human blood, serum and insect haemolymph. The structure analysis of these complexes revealed an unusual organization of binding sites that was not observed in any other lectin so far. The presence of high number of binding sites per monomer together with protein dimerization enables high affinity of the lectin towards potential interacting surfaces, e.g. bacteria, immune cells or host epithelia. These results suggest that PHL might play a crucial role in the interaction of P. asymbiotica with both human and insect hosts.
Návaznosti
| GA13-25401S, projekt VaV |
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| LM2015043, projekt VaV |
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| LQ1601, projekt VaV |
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