About: Lectins from human pathogens - structure, function, engineering

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Projekt, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	http://linked.opendata.cz/ontology/domain/vavai/Projekt
rdfs:seeAlso	http://www.isvav.cz/projectDetail.do?rowId=GA303/09/1168
Description	Recognition of glycoconjugates is an important event in host recognition by pathogenic organisms. Project is focused on structure-function characterisation of already identified proteins from opportunistic human pathogens and also proteins that will be identified by database search in newly sequenced genomes. Selected proteins will be cloned and expressed in recombinant form. Specificities and affininties of lectins will be studied by binding experiments using Surface Plasmon Resonance and microcalorimetry methods with oligosaccharides of biological interest, such as blood group antigenic determinants. Crystal structure determination of protein/carbohydrate complexes will be performed to understand a molecular basis of the interactions. Powerful combination of experimental and computational methods will be employed to understand crutial contributions for affinity and specificity of binding. In silico mutagenesis will help to select interesting lectin targets with modified binding properties. The present study has potential pharmaceutical implications since these inhibitors would be the basis for local anti-adhesion therapy. (en) Specifické rozpoznávání sacharidů na povrchu buněk hraje důležitou úlohu v rozlišení hostitele patogenními organismy. Projekt je zaměřen na strukturně-funkční charakterizaci dosud identifikovaných proteinů z podmíněných lidských patogenů a také proteinů, které budou nalezeny v nově sekvenovaných genomech. Vybrané proteiny budou klonovány a exprimovány v rekombinační podobě. Specifita a afinita lektinů s biologicky zajímavými oligosacharidy bude studována pomocí metod resonance povrchových plasmonů (SPR) a mikrokalorimetrie. Pro pochopení molekulární podstaty interakcí budou krystalovány a řešeny struktury protein/sacharidových komplexů. Pro porozumění jednotlivých příspěvků k afinitě a specifitě lektinů bude používána účinná kombinace experimentálních a výpočetních metod. In silico mutageneze umožní návrhy nových lektinů s modifikovanými vazebnými vlastnostmi. Projekt má potenciální farmaceutické implikace, protože inhibitory studovaných lektinů mohou sloužit jako základ antiadhezivní terapie.
Title	Lectins from human pathogens - structure, function, engineering (en) Lektiny z lidských patogenů - struktura, funkce, inženýrství
skos:notation	GA303/09/1168
http://linked.open...avai/cep/aktivita	Standard projects
http://linked.open...kovaStatniPodpora	http://linked.opendata.cz/resource/domain/vavai/projekt/GA303%2F09%2F1168/celkovaStatniPodpora
http://linked.open...ep/celkoveNaklady	http://linked.opendata.cz/resource/domain/vavai/projekt/GA303%2F09%2F1168/celkoveNaklady
http://linked.open...datumDodatniDoRIV	2014-01-30 (xsd:date)
http://linked.open...i/cep/druhSouteze	VS - Veřejná soutěž ve výzkumu a vývoji
http://linked.open...ep/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open.../cep/fazeProjektu	92536688
http://linked.open...ai/cep/hlavniObor	BO - Biofyzika
http://linked.open...hodnoceniProjektu	V - Vynikající výsledky (s mezinárodním významem apod.). Zároveň byly splněny cíle a předpokládané výsledky uvedené ve smlouvě / rozhodnutí o poskytnutí podpory.
http://linked.open...vai/cep/kategorie	ZV - Základní výzkum
http://linked.open.../cep/klicovaSlova	lectin; 3D-structure; biomolecular; interactions; docking; mutagenesis (en)
http://linked.open...ep/partnetrHlavni	Přírodovědecká fakulta
http://linked.open...inujicichPrijemcu	0 (xsd:int)
http://linked.open...cep/pocetPrijemcu	1 (xsd:int)
http://linked.open...ocetSpoluPrijemcu	0 (xsd:int)
http://linked.open.../pocetVysledkuRIV	52 (xsd:int)
http://linked.open...enychVysledkuVRIV	52 (xsd:int)
http://linked.open...lneniVMinulemRoce	2012-03-30 (xsd:date)
http://linked.open.../prideleniPodpory	http://linked.opendata.cz/resource/domain/vavai/cep/prideleniPodpory/303%2F09%2F1168
http://linked.open...iciPoslednihoRoku	2012
http://linked.open...atUdajeProjZameru	2013
http://linked.open.../vavai/cep/soutez	SGA02009GA-ST
http://linked.open...usZobrazovaneFaze	DUU
http://linked.open...ai/cep/typPojektu	P - Projekt výzkumu a vývoje financovaný ze státního rozpočtu
http://linked.open...ep/ukonceniReseni	2012-12-31 (xsd:date)
http://linked.open.../cep/vedlejsiObor	CE - Biochemie
http://linked.open...ep/zahajeniReseni	2009-01-01 (xsd:date)
http://linked.open...jektu+dodavatelem	Scientific contribution of the project was structural and functional characterization of several lectins. More than 10 lectin structures have been solved. The project significantly contributed to the student training. Major outputs comprise 9 papers in scinetific journals, 1 book chapter and 40 conference contributions. No imperfections in compliance of the rules and financial spending have arisen (en) Odborným přínosem projektu byla strukturní a funkční charakterizace některých lektinů z patogenních mikroorganismů. Bylo vyřešeno více než deset struktur lektinů. Projekt významně přispěl i k výchově studentů. Hlavními výstupy projektu je 9 publikací v mezinárodních časopisech, 1 kapitola v knize a 40 prezentací na konferencích. Nedostatky v dodržování pravidel a v čerpání financí se nevyskytly. (cs)
http://linked.open...tniCyklusProjektu	ZBBKU
http://linked.open.../cep/klicoveSlovo	lectin 3D-structure biomolecular docking interactions
is http://linked.open...vavai/riv/projekt of	Effect of pH on oligomeric form and activity of lectins Aspergillus fumigatus lectin – a new procedure for studying highly complex interactions of multivalent lectins with their ligands Function and structure studies of lectin from bioluminescent bacterium Photorhabdus luminescens The Five Bacterial Lectins: PA-IL, PA-IIL, RSL, RS-IIL and CV-IIL Interactions with Diverse Animal Cells and Glycoproteins. Fucose-binding lectin from human pathogen Aspergillus fumigatus Structure and function of lectins from Burkholderia cenocepacia - similar, yet different Structure and specificity of a blood group oligosaccharide specific lectin from Aspergillus fumigatus Bioinformatika v praxi - výuka předmětu na pomezí informatických a biologických věd Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide TRITON 4 : software for ligand-binding protein engineering Aspergillus fumigatus lectins - how to stay in touch Aspergillus fumigatus as a pathogen - role of surface interacting molecules CV-IIL lectin: another piece of the Chromobacterium violaceum puzzle Directed evolution of lectins from pathogenic bacteria Aspergillus fumigatus host-interacting proteins - potential therapeutic targets Structure and binding properties of Burkholderia cenocepacia lectin with dual specificity CV-IIL lectin : an ideal helper for understanding mutation-caused binding preference changes in the PA-IIL lectin family Role of LecA and LecB Lectins in Pseudomonas aeruginosa-Induced Lung Injury and Effect of Carbohydrate Ligands Proteiny Aspergillus fumigatus zapojené do interakce s hostitelem Recognition of selected monosaccharides by Pseudomonas aeruginosa Lectin II analyzed by molecular dynamics and free energy calculations A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens Thermodynamics behind CV-IIL binding of saccharides Thermodynamical analysis of the mutant CV-IIL lectins from Chromobacterium violaceum Virtual screening and in silico design of novel inhibitors of bacterial lectins High resolution structure of Aleuria aurantia lectin mutant reveals the principal of increased affinity Protein oligomerization in Aleuria aurantia lectin family - importance and difficulties Aspergillus fumigatus host-interacting proteins - potential therapeutic targets Aleuria aurantia lectin family - structural insight into differences of carbohydrate binding among related proteins Cloning and characterization of novel jacalin-related lectin from Aspergillus fumigatus Characterization of lectins from opportunistic pathogens by fluorescence microscopy Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes Identification and preparation of novel lectin from A. bisporus In Silico Engineering of Proteins that Recognize Small Molecules In Silico Mutagenesis and Docking Study of Ralstonia solanacearum RSL Lectin: Performance of Docking Software To Predict Saccharide Binding Lectins from Burkholderia cenocepacia - when two (three, four) do the same thing... Stacking Interactions between Carbohydrate and Protein Quantified by Combination of Theoretical and Experimental Methods Methods of directed evolution of PA-IIL lectin Structure and binding properties of Burkholderia cenocepacia lectin with dual specificity Characterization of lectins from opportunistic pathogens by surface plasmon resonance Burkholderia cenocepacia lectins – similar, however different potential virulence factors Calorimetric investigation of the mutant lectins from Chromobacterium violaceum Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity Nový lektin ze světélkující bakterie Photorhabdus luminescens Random mutagenesis of lectins and high-throughput screening of mutant libraries Structural insight into binding variability of Aspergillus fumigatus lectin Novel lectins from Aspergillus fumigatus Structure and functional approaches revealing the mysteries of Aspergillus fumigatus host-interacting proteins Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin Host cell recognition by carbohydrate-binding proteins from human pathogens Novel pH dependent lectin from bioluminescent bacterium Photorhabdus luminescens Lectins from Burkholderia cenocepacia - potential virulence factors Lectins from pathogens: mystery of life
is http://linked.open...vavai/cep/projekt of	http://linked.opendata.cz/resource/domain/vavai/cep/ucast/GA303%2F09%2F1168/2009/orjk%3A14310 http://linked.opendata.cz/resource/domain/vavai/cep/ucast/GA303%2F09%2F1168/2010/orjk%3A14310 http://linked.opendata.cz/resource/domain/vavai/cep/ucast/GA303%2F09%2F1168/2011/orjk%3A14310 http://linked.opendata.cz/resource/domain/vavai/cep/ucast/GA303%2F09%2F1168/2012/orjk%3A14310 http://linked.opendata.cz/resource/domain/vavai/cep/ucast/GA303%2F09%2F1168/2013/orjk%3A14310

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