2016
A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure
KUMAR, Atul, Petra SÝKOROVÁ, Gabriel DEMO, Pavel DOBEŠ, Pavel HYRŠL et. al.Základní údaje
Originální název
A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure
Autoři
KUMAR, Atul (356 Indie, domácí), Petra SÝKOROVÁ (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
The Journal of Biological Chemistry, Bethesda, American Society for Biochemistry and Molecular Biology, 2016, 0021-9258
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 4.125
Kód RIV
RIV/00216224:14740/16:00088341
Organizační jednotka
Středoevropský technologický institut
UT WoS
000388880100020
Klíčová slova anglicky
lectin; bacterial pathogen; host-pathogen interaction; crystal structure; structural biology; Photorhabdus luminescen; haemocytes; Galleria mellonella; nematodes; Heterorhabditis bacteriophora
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 14. 3. 2017 13:18, Mgr. Eva Špillingová
V originále
Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity toward insect larvae. Ahypothetical protein from P. luminescens was identified, purified from the native source, and characterized as an L-fucose-binding lectin, named P. luminescens lectin (PLL). Glycan array and biochemical characterization data revealed PLL to be specific toward L-fucose and the disaccharide glycan 3,6-O-Me-2-Glc beta 1-4(2,3-O-Me-2)Rha alpha-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homotetramer with an intersubunit disulfide bridge. The crystal structures of native and recombinant PLL revealed a seven-bladed beta-propeller fold creating seven putative fucose-binding sites per monomer. The crystal structure of the recombinant PLL.L-fucose complex confirmed that at least three sites were fucose-binding. Moreover, the crystal structures indicated that some of the other sites are masked either by the tetrameric nature of the lectin or by incorporation of the C terminus of the lectin into one of these sites. PLL exhibited an ability to bind to insect hemocytes and the cuticular surface of a nematode, H. bacteriophora.
Česky
Photorhabdus luminescens is known for its symbiosis with the entomopathogenic nematode Heterorhabditis bacteriophora and its pathogenicity toward insect larvae. Ahypothetical protein from P. luminescens was identified, purified from the native source, and characterized as an L-fucose-binding lectin, named P. luminescens lectin (PLL). Glycan array and biochemical characterization data revealed PLL to be specific toward L-fucose and the disaccharide glycan 3,6-O-Me-2-Glc beta 1-4(2,3-O-Me-2)Rha alpha-O-(p-C6H4)-OCH2CH2NH2. PLL was discovered to be a homotetramer with an intersubunit disulfide bridge. The crystal structures of native and recombinant PLL revealed a seven-bladed beta-propeller fold creating seven putative fucose-binding sites per monomer. The crystal structure of the recombinant PLL.L-fucose complex confirmed that at least three sites were fucose-binding. Moreover, the crystal structures indicated that some of the other sites are masked either by the tetrameric nature of the lectin or by incorporation of the C terminus of the lectin into one of these sites. PLL exhibited an ability to bind to insect hemocytes and the cuticular surface of a nematode, H. bacteriophora.
Návaznosti
| EE2.3.30.0009, projekt VaV |
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| GA13-25401S, projekt VaV |
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| LQ1601, projekt VaV |
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