Detailed Information on Publication Record
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.Basic information
Original name
Novel bangle lectin from Photorhabdus asymbiotica: sugar-binding specificity, structure and interaction with host immune system
Name in Czech
Nový bangle-lektin z Photorhabdus asymbiotica: specifita vůči sacharidům, struktura a interakce s imunitním systémem hostitele
Authors
HOUSER, Josef (203 Czech Republic, belonging to the institution), Gita JANČAŘÍKOVÁ (203 Czech Republic, belonging to the institution), Gabriel DEMO (703 Slovakia, belonging to the institution), Pavel DOBEŠ (203 Czech Republic, belonging to the institution), Pavel HYRŠL (203 Czech Republic, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)
Edition
2017
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
RIV identification code
RIV/00216224:14740/17:00094888
Organization unit
Central European Institute of Technology
ISSN
Keywords (in Czech)
lektin Photorhabdus struktura imunita
Keywords in English
lectin Photorhabdus structure immunity
Tags
Změněno: 17/8/2017 14:21, Mgr. Josef Houser, Ph.D.
Abstract
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.
Links
| GA13-25401S, research and development project |
| ||
| LM2015043, research and development project |
| ||
| LQ1601, research and development project |
|