Unusual Entropy Driven Affinity of Chromobacterium violaceum
Lectin CV-IIL towards Fucose and Mannose

J 2006

Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose

POKORNÁ, Martina, Gianluca CIOCCI, Stephanie PERRET, Etienne REBUFFET, Nikola KOSTLÁNOVÁ et. al.

Základní údaje

Originální název

Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose

Název česky

Neobvykle entropicky rizena affinita lektinu z Chromobacterium violaceum k fukose a manose

Autoři

POKORNÁ, Martina (203 Česká republika), Gianluca CIOCCI (250 Francie), Stephanie PERRET (250 Francie), Etienne REBUFFET (250 Francie), Nikola KOSTLÁNOVÁ (203 Česká republika), Jan ADAM (203 Česká republika), Nechama GILBOA-GARBER (376 Izrael), Edward P. MITCHELL (826 Velká Británie a Severní Irsko), Anne IMBERTY (250 Francie) a Michaela WIMMEROVÁ (203 Česká republika, garant)

Vydání

Biochemistry, USA, American Chemical Society, 2006, 0006-2960

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

Impakt faktor

Impact factor: 3.633

Kód RIV

RIV/00216224:14310/06:00015708

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000238217100010

Klíčová slova anglicky

lectin; microcalorimetry; chromobacterium violaceum; pathogen

Štítky

Chromobacterium violaceum, lectin, microcalorimetry, pathogen

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 1. 2007 15:32, prof. RNDr. Michaela Wimmerová, Ph.D.

Anotace

ORIG CZ

V originále

The purple pigmented bacterium Chromobacterium Violaceum is a dominant component of tropical soil microbiota that can cause rare but fatal septicaemia in humans. Its sequenced genome provides insight into the abundant potential of this organism for biotechnological and pharmaceutical applications and allowed an ORF encoding a protein that is 60% identical to the fucose binding lectin (PA-IIL) from Pseudomonas aeruginosa and the mannose binding lectin (RS-IIL) from Ralstonia solanacearum to be identified. The lectin, CV-IIL, has recently been purified from C. Violaceum [Zinger-Yosovich, K., Sudakevitz, D., Imberty, A., Garber, N. C., and Gilboa-Garber, N. (2006) Microbiology 152, 457-463] and has been confirmed to be a tetramer with subunit size of 11.86 kDa and a binding preference for fucose. We describe here the cloning of CV-IIL and its expression as a recombinant protein. A complete structure-function characterization has been made in an effort to analyze the specificity and affinity of CV-IIL for fucose and mannose. Crystal structures of CV-IIL complexes with monosaccharides have yielded the molecular basis of the specificity. Each monomer contains two close calcium cations that mediate the binding of the monosaccharides, which occurs in different orientations for fucose and mannose. The thermodynamics of binding has been analyzed by titration microcalorimetry, giving dissociation constants of 1.7 and 19 íM for R-methyl fucoside and R-methyl mannoside, respectively. Further analysis demonstrated a strongly favorable entropy term that is unusual in carbohydrate binding. A comparison with both PA-IIL and RS-IIL, which have binding preferences for fucose and mannose, respectively, yielded insights into the monosaccharide specificity of this important class of soluble bacterial lectins.

Česky

Neobvykle entropicky rizena affinita lektinu z Chromobacterium violaceum k fukose a manose

Návaznosti

GD204/03/H016, projekt VaV

Název: Strukturní biofyzika makromolekul

Investor: Grantová agentura ČR, Strukturní biofyzika makromolekul

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

POKORNÁ, Martina, Gianluca CIOCCI, Stephanie PERRET, Etienne REBUFFET, Nikola KOSTLÁNOVÁ, Jan ADAM, Nechama GILBOA-GARBER, Edward P. MITCHELL, Anne IMBERTY a Michaela WIMMEROVÁ. Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose. Biochemistry. USA: American Chemical Society, 2006, roč. 45, č. 24, s. 7501-7510. ISSN 0006-2960.

@article{636664,
   author = {Pokorná, Martina and Ciocci, Gianluca and Perret, Stephanie and Rebuffet, Etienne and Kostlánová, Nikola and Adam, Jan and GilboaandGarber, Nechama and Mitchell, Edward P. and Imberty, Anne and Wimmerová, Michaela},
   article_location = {USA},
   article_number = {24},
   keywords = {lectin; microcalorimetry; chromobacterium violaceum; pathogen},
   language = {eng},
   issn = {0006-2960},
   journal = {Biochemistry},
   title = {Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose},
   volume = {45},
   year = {2006}
}

TY  - JOUR
ID  - 636664
AU  - Pokorná, Martina - Ciocci, Gianluca - Perret, Stephanie - Rebuffet, Etienne - Kostlánová, Nikola - Adam, Jan - Gilboa-Garber, Nechama - Mitchell, Edward P. - Imberty, Anne - Wimmerová, Michaela
PY  - 2006
TI  - Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose
JF  - Biochemistry
VL  - 45
IS  - 24
SP  - 7501-7510
EP  - 7501-7510
PB  - American Chemical Society
SN  - 00062960
KW  - lectin
KW  - microcalorimetry
KW  - chromobacterium violaceum
KW  - pathogen
N2  - The purple pigmented bacterium Chromobacterium Violaceum is a dominant component of tropical soil microbiota that can cause rare but fatal septicaemia in humans. Its sequenced genome provides insight into the abundant potential of this organism for biotechnological and pharmaceutical applications and allowed an ORF encoding a protein that is 60% identical to the fucose binding lectin (PA-IIL) from Pseudomonas aeruginosa and the mannose binding lectin (RS-IIL) from Ralstonia solanacearum to be identified. The lectin, CV-IIL, has recently been purified from C. Violaceum [Zinger-Yosovich, K., Sudakevitz, D., Imberty, A., Garber, N. C., and Gilboa-Garber, N. (2006) Microbiology 152, 457-463] and has been confirmed to be a tetramer with subunit size of 11.86 kDa and a binding preference for fucose. We describe here the cloning of CV-IIL and its expression as a recombinant protein. A complete structure-function characterization has been made in an effort to analyze the specificity and affinity of CV-IIL for fucose and mannose. Crystal structures of CV-IIL complexes with monosaccharides have yielded the molecular basis of the specificity. Each monomer contains two close calcium cations that mediate the binding of the monosaccharides, which occurs in different orientations for fucose and mannose. The thermodynamics of binding has been analyzed by titration microcalorimetry, giving dissociation constants of 1.7 and 19 íM for R-methyl fucoside and R-methyl mannoside, respectively. Further analysis demonstrated a strongly favorable entropy term that is unusual in carbohydrate binding. A comparison with both PA-IIL and RS-IIL, which have binding preferences for fucose and mannose, respectively, yielded insights into the monosaccharide specificity of this important class of soluble bacterial lectins.
ER  -

POKORNÁ, Martina, Gianluca CIOCCI, Stephanie PERRET, Etienne REBUFFET, Nikola KOSTLÁNOVÁ, Jan ADAM, Nechama GILBOA-GARBER, Edward P. MITCHELL, Anne IMBERTY a Michaela WIMMEROVÁ. Unusual Entropy Driven Affinity of Chromobacterium violaceum Lectin CV-IIL towards Fucose and Mannose. \textit{Biochemistry}. USA: American Chemical Society, 2006, roč.~45, č.~24, s.~7501-7510. ISSN~0006-2960.

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