About: The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan     Goto   Sponge   Distinct   Permalink

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Description
  • Plant pathogens, as animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment and invasion. The bacterium Ralstonia solanacearum which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, RSL, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to áFuc1-2Gal and áFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for áFuc1-2Gal containing oligosaccharides (KD 2.5 10-7 M for 2-fucosyllactose). RSL has been crystallised with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose.
  • Plant pathogens, as animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment and invasion. The bacterium Ralstonia solanacearum which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, RSL, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to áFuc1-2Gal and áFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for áFuc1-2Gal containing oligosaccharides (KD 2.5 10-7 M for 2-fucosyllactose). RSL has been crystallised with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. (en)
Title
  • The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan
  • The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan (en)
skos:prefLabel
  • The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan
  • The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan (en)
skos:notation
  • RIV/00216224:14310/05:00013768!RIV10-MSM-14310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LN00A016), Z(MSM0021622413)
http://linked.open...iv/cisloPeriodika
  • 30
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 522200
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/05:00013768
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • lectin; Ralstonia solanacearum; crystal structure; propeller; SPR (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [3994287A681C]
http://linked.open...i/riv/nazevZdroje
  • Journal of Biological Chemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 280
http://linked.open...iv/tvurceVysledku
  • Imberty, Anne
  • Kostlánová, Nikola
  • Wimmerová, Michaela
  • Gilboa-Garber, Nechama
  • Lahmann, Martina
  • Mitchell, Edward
  • Lortat-Jacob, Hugues
  • Chambat, Gerard
  • Oscarson, Stefan
http://linked.open...n/vavai/riv/zamer
issn
  • 0021-9258
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
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