Production of Ca-dependent high-affinity lectins with defined
specificity by mutagenesis of PA-IIL lectin

a 2011

Production of Ca-dependent high-affinity lectins with defined specificity by mutagenesis of PA-IIL lectin

POKORNÁ, Martina; Jan ADAM; Charles SABIN; Edward P. MITCHELL; Anne IMBERTY et. al.

Základní údaje

Originální název

Production of Ca-dependent high-affinity lectins with defined specificity by mutagenesis of PA-IIL lectin

Autoři

POKORNÁ, Martina (203 Česká republika, domácí); Jan ADAM (203 Česká republika, domácí); Charles SABIN (250 Francie); Edward P. MITCHELL (250 Francie); Anne IMBERTY (250 Francie); Jaroslav KOČA (203 Česká republika, domácí) a Michaela WIMMEROVÁ (203 Česká republika, garant, domácí)

Vydání

European Young Investigator Workshop, Carbohydrate Chemistry: From Synthesis to Applications, 2011

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10600 1.6 Biological sciences

Stát vydavatele

Francie

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14740/11:00050178

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

lectin; Pseudomonas aeruginosa; PA-IIL; mutagenesis

Štítky

rivok

Změněno: 4. 4. 2012 10:23, Mgr. Nikola Kostlánová, Ph.D.

Anotace

V originále

The bacterium Pseudomonas aeruginosa is a human opportunistic pathogen that can infect almost every human tissue in conditions of a lowered immunity barrier. The lectin PA IIL plays an important role in the bacteria’s virulence. It displays unusually high affinity for L fucose in the micromolar range. [1] This characteristic is correlated with the remarkable presence of two calcium ions in the binding site of the protein. In vitro mutagenesis was performed focusing on three single point mutants of PA-IIL in positions 22-23-24. The mutated amino acids belong to the “specificity-binding loop”. The structure of all mutants was determined by X-ray crystallography and their thermodynamic characterization was performed using isothermal titration calorimetry. The mutants were designed also by in silico methods, and the resulting structures were used for docking experiments. The in vitro mutagenesis in combination with computational methods allowed the key importance of amino acid 22 for the specificity of the lectin to be identified.

Návaznosti

GPP207/11/P185, projekt VaV

Název: Příprava lektinů s vysokou specifitou a afinitou

Investor: Grantová agentura ČR, Příprava lektinů s vysokou specifitou a afinitou

Citovat

POKORNÁ, Martina; Jan ADAM; Charles SABIN; Edward P. MITCHELL; Anne IMBERTY; Jaroslav KOČA a Michaela WIMMEROVÁ. Production of Ca-dependent high-affinity lectins with defined specificity by mutagenesis of PA-IIL lectin. In European Young Investigator Workshop, Carbohydrate Chemistry: From Synthesis to Applications. 2011.

@proceedings{959880,
   author = {Pokorná, Martina and Adam, Jan and Sabin, Charles and Mitchell, Edward P. and Imberty, Anne and Koča, Jaroslav and Wimmerová, Michaela},
   booktitle = {European Young Investigator Workshop, Carbohydrate Chemistry: From Synthesis to Applications},
   keywords = {lectin; Pseudomonas aeruginosa; PA-IIL; mutagenesis},
   language = {eng},
   title = {Production of Ca-dependent high-affinity lectins with defined specificity by mutagenesis of PA-IIL lectin},
   year = {2011}
}

TY  - CONF
ID  - 959880
AU  - Pokorná, Martina - Adam, Jan - Sabin, Charles - Mitchell, Edward P. - Imberty, Anne - Koča, Jaroslav - Wimmerová, Michaela
PY  - 2011
TI  - Production of Ca-dependent high-affinity lectins with defined specificity by mutagenesis of PA-IIL lectin
KW  - lectin
KW  - Pseudomonas aeruginosa
KW  - PA-IIL
KW  - mutagenesis
N2  - The bacterium Pseudomonas aeruginosa is a human opportunistic pathogen that can infect almost every human tissue in conditions of a lowered immunity barrier. The lectin PA IIL plays an important role in the bacteria’s virulence. It displays unusually high affinity for L fucose in the micromolar range. [1] This characteristic is correlated with the remarkable presence of two calcium ions in the binding site of the protein. In vitro mutagenesis was performed focusing on three single point mutants of PA-IIL in positions 22-23-24. The mutated amino acids belong to the “specificity-binding loop”. The structure of all mutants was determined by X-ray crystallography and their thermodynamic characterization was performed using isothermal titration calorimetry. The mutants were designed also by in silico methods, and the resulting structures were used for docking experiments. The in vitro mutagenesis in combination with computational methods allowed the key importance of amino acid 22 for the specificity of the lectin to be identified.
ER  -

POKORNÁ, Martina; Jan ADAM; Charles SABIN; Edward P. MITCHELL; Anne IMBERTY; Jaroslav KOČA a Michaela WIMMEROVÁ. Production of Ca-dependent high-affinity lectins with defined specificity by mutagenesis of PA-IIL lectin. In \textit{European Young Investigator Workshop, Carbohydrate Chemistry: From Synthesis to Applications}. 2011.

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