CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA

Result code in IS VaVaI

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Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA

Original language description

Four genes coding proteins homologous to lectin PA-IIL from Pseudomonas aeruginasa have been found in the genome of B. cenocepacia. One of them, named BclC, is a 28 kDa protein which is able to recognize D-mannosylated carbohydrates. This protein also exhibits partial sequence homology with the protein CV-IIL from the Chromobacterium violaceum. BclC has been cloned and prepared in recombinant form. Sequence analysis showed two distinct domains in the protein, N-terminal part that does not have any sequence homolog in genomic and protein databases, and C-terminal part that codes for lectin domain. Both domains were also cloned separately to simplify further structure-function characterization. Detailed functional studies using surface plasmon resonance(SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters.

Czech name

Charakterizace nového lektinu BclC z lidského podmíněného patogenu B. Cenocepacia

Czech description

Four genes coding proteins homologous to lectin PA-IIL from Pseudomonas aeruginasa have been found in the genome of B. cenocepacia. One of them, named BclC, is a 28 kDa protein which is able to recognize D-mannosylated carbohydrates. This protein also exhibits partial sequence homology with the protein CV-IIL from the Chromobacterium violaceum. BclC has been cloned and prepared in recombinant form. Sequence analysis showed two distinct domains in the protein, N-terminal part that does not have any sequence homolog in genomic and protein databases, and C-terminal part that codes for lectin domain. Both domains were also cloned separately to simplify further structure-function characterization. Detailed functional studies using surface plasmon resonance(SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters.

Type

D - Article in proceedings

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2008

Confidentiality

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

Article name in the collection

XII. Setkání biochemiků a molekulárních biologů

ISBN

978-80-210-4526-2

ISSN

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e-ISSN

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Number of pages

2

Pages from-to

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Publisher name

Masarykova univerzita

Place of publication

Brno

Event location

Brno

Event date

Jan 1, 2008

Type of event by nationality

EUR - Evropská akce

UT code for WoS article

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