Structure and specificity of lectin from bacterium Burkholderia pseudomallei

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F15%3A00080927" target="_blank" >RIV/00216224:14310/15:00080927 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Structure and specificity of lectin from bacterium Burkholderia pseudomallei

Popis výsledku v původním jazyce

A new lectin from B. pseudomallei was identified, which did not show any significant sequence similarity to the known proteins. The gene coding the lectin was cloned and protein expression and purification were successfully optimized. Surface plasmon resonance (SPR) and titration microcalorimetry (ITC) were used to characterize the interactions between the lectin and saccharides. Both methods revealed the lectin ability to bind D-mannose and mannosylated derivatives. The structure of the protein was solved using X-ray diffraction and showed a novel fold of bacterial lectins. The lectin is present as a monomer in solution as determined using analytical ultracentrifugation, which was also confirmed in the crystal structure. According to its structure andsequence, the protein belongs to a not yet described family of lectins.

Název v anglickém jazyce

Structure and specificity of lectin from bacterium Burkholderia pseudomallei

Popis výsledku anglicky

A new lectin from B. pseudomallei was identified, which did not show any significant sequence similarity to the known proteins. The gene coding the lectin was cloned and protein expression and purification were successfully optimized. Surface plasmon resonance (SPR) and titration microcalorimetry (ITC) were used to characterize the interactions between the lectin and saccharides. Both methods revealed the lectin ability to bind D-mannose and mannosylated derivatives. The structure of the protein was solved using X-ray diffraction and showed a novel fold of bacterial lectins. The lectin is present as a monomer in solution as determined using analytical ultracentrifugation, which was also confirmed in the crystal structure. According to its structure andsequence, the protein belongs to a not yet described family of lectins.

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů