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 and Michaela WIMMEROVÁ. A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure. The Journal of Biological Chemistry. Bethesda: American Society for Biochemistry and Molecular Biology, 2016, vol. 291, No 48, p. 25032-25049. ISSN 0021-9258. Available from: https://dx.doi.org/10.1074/jbc.M115.693473.

Basic information

• Original name: A Novel Fucose-Binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure
• Authors: KUMAR, Atul (356 India, belonging to the institution), Petra SÝKOROVÁ (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: The Journal of Biological Chemistry, Bethesda, American Society for Biochemistry and Molecular Biology, 2016, 0021-9258.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 4.125
• RIV identification code: RIV/00216224:14740/16:00088341
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1074/jbc.M115.693473
• UT WoS: 000388880100020
• Keywords in English: lectin; bacterial pathogen; host-pathogen interaction; crystal structure; structural biology; Photorhabdus luminescen; haemocytes; Galleria mellonella; nematodes; Heterorhabditis bacteriophora
• Tags: rivok
• Tags: International impact, Reviewed

Abstract

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.

Abstract (in Czech)

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.

Links

• EE2.3.30.0009, research and development project: Name: Zaměstnáním čerstvých absolventů doktorského studia k vědecké excelenci
• GA13-25401S, research and development project: Name: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu

Investor: Czech Science Foundation

• LQ1601, research and development project: Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR