HOUSER, Josef, Gita JANČAŘÍKOVÁ, Gabriel DEMO, Pavel DOBEŠ, Pavel HYRŠL and Michaela WIMMEROVÁ. Novel bangle lectin from Photorhabdus asymbiotica: sugar-binding specificity, structure and interaction with host immune system. 2017. ISSN 1211-5894.
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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
Original language English
Type of outcome Conference abstract
Field of Study 10600 1.6 Biological sciences
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14740/17:00094888
Organization unit Central European Institute of Technology
ISSN 1211-5894
Keywords (in Czech) lektin Photorhabdus struktura imunita
Keywords in English lectin Photorhabdus structure immunity
Tags rivok
Changed by Changed by: Mgr. Josef Houser, Ph.D., učo 77781. Changed: 17/8/2017 14:21.
Abstract
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 projectName: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu
Investor: Czech Science Foundation
LM2015043, research and development projectName: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
LQ1601, research and development projectName: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR
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