Detailed Information on Publication Record
2017
Characterization of novel bangle lectin from Photorhabdus asymbiotica with dual sugar-binding specificity and its effect on host immunity
JANČAŘÍKOVÁ, Gita, Josef HOUSER, Pavel DOBEŠ, Gabriel DEMO, Pavel HYRŠL et. al.Basic information
Original name
Characterization of novel bangle lectin from Photorhabdus asymbiotica with dual sugar-binding specificity and its effect on host immunity
Authors
JANČAŘÍKOVÁ, Gita (203 Czech Republic, belonging to the institution), Josef HOUSER (203 Czech Republic, belonging to the institution), Pavel DOBEŠ (203 Czech Republic, belonging to the institution), Gabriel DEMO (703 Slovakia, 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
PLoS Pathogens, San Francisco, Public Library of Science, 2017, 1553-7366
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 6.158
RIV identification code
RIV/00216224:14310/17:00094886
Organization unit
Faculty of Science
UT WoS
000408758400037
Keywords in English
Lectins; blood; insects; blood groups; carbohydrates; immune response; sedimenation; nematode infections
Tags
International impact, Reviewed
Změněno: 25/11/2018 12:12, prof. RNDr. Michaela Wimmerová, Ph.D.
Abstract
V originále
Photorhabdus asymbiotica is one of the three recognized species of the Photorhabdus genus, which consists of gram-negative bioluminescent bacteria belonging to the family Morganellaceae. These bacteria live in a symbiotic relationship with nematodes from the genus Heterorhabditis, together forming a complex that is highly pathogenic for insects. Unlike other Photorhabdus species, which are strictly entomopathogenic, P. asymbiotica is unique in its ability to act as an emerging human pathogen. Analysis of the P. asymbiotica genome identified a novel fucose-binding lectin designated PHL with a strong sequence similarity to the recently described P. luminescens lectin PLL. Recombinant PHL exhibited high affinity for fucosylated carbohydrates and the unusual disaccharide 3,6-O-Me2-GlcBeta1± 4(2,3-O-Me2)RhaAlpha-O-(p-C6H4)-OCH2CH2NH2 from Mycobacterium leprae. Based on its crystal structure, PHL forms a seven-bladed beta-propeller assembling into a homo-dimer with an inter-subunit disulfide bridge. Investigating complexes with different ligands revealed the existence of two sets of binding sites per monomer - the first type prefers L-fucose and its derivatives, whereas the second type can bind D-galactose. Based on the sequence analysis, PHL could contain up to twelve binding sites per monomer. PHL was shown to interact with all types of red blood cells and insect haemocytes. Interestingly, PHL inhibited the production of reactive oxygen species induced by zymosan A in human blood and antimicrobial activity both in human blood, serum and insect haemolymph. Concurrently, PHL increased the constitutive level of oxidants in the blood and induced melanisation in haemolymph. Our 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 |
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GA15-17670S, research and development project |
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LM2015043, research and development project |
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LQ1601, research and development project |
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