Identification of two substrates of FTS_ 1067 protein – an essential virulence factor of Francisella tularensis
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F17%3A43875741" target="_blank" >RIV/60162694:G44__/17:43875741 - isvavai.cz</a>
Výsledek na webu
<a href="http://akademiai.com/doi/abs/10.1556/030.63.2016.013" target="_blank" >http://akademiai.com/doi/abs/10.1556/030.63.2016.013</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1556/030.63.2016.013" target="_blank" >10.1556/030.63.2016.013</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Identification of two substrates of FTS_ 1067 protein – an essential virulence factor of Francisella tularensis
Popis výsledku v původním jazyce
Francisella tularensis is a highly virulent intracellular pathogen with the capacity to infect a variety of hosts including humans. One of the most important proteins involved in F. tularensis virulence and pathogenesis is the protein DsbA. This protein is annotated as a lipoprotein with disulfide oxidoreductase/isomerase activity. Therefore, its interactions with different substrates, including probable virulence factors, to assist in their proper folding are anticipated. We aimed to use the immunopurification approach to find DsbA (gene locus FTS_1067) interacting partners in F. tularensis subsp. holarctica strain FSC200 and compare the identified substrates with proteins which were found in our previous comparative proteome analysis. As a result of our work two FTS_1067 substrates, D-alanyl-D-alanine carboxypeptidase family protein and HlyD family secretion protein, were identified. Bacterial two-hybrid systems were further used to test their relevance in confirming FTS_1067 protein interactions.
Název v anglickém jazyce
Identification of two substrates of FTS_ 1067 protein – an essential virulence factor of Francisella tularensis
Popis výsledku anglicky
Francisella tularensis is a highly virulent intracellular pathogen with the capacity to infect a variety of hosts including humans. One of the most important proteins involved in F. tularensis virulence and pathogenesis is the protein DsbA. This protein is annotated as a lipoprotein with disulfide oxidoreductase/isomerase activity. Therefore, its interactions with different substrates, including probable virulence factors, to assist in their proper folding are anticipated. We aimed to use the immunopurification approach to find DsbA (gene locus FTS_1067) interacting partners in F. tularensis subsp. holarctica strain FSC200 and compare the identified substrates with proteins which were found in our previous comparative proteome analysis. As a result of our work two FTS_1067 substrates, D-alanyl-D-alanine carboxypeptidase family protein and HlyD family secretion protein, were identified. Bacterial two-hybrid systems were further used to test their relevance in confirming FTS_1067 protein interactions.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10606 - Microbiology
Návaznosti výsledku
Projekt
—
Návaznosti
S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Acta Microbiologica et Immunologica Hungarica
ISSN
1217-8950
e-ISSN
—
Svazek periodika
64
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
HU - Maďarsko
Počet stran výsledku
13
Strana od-do
37-49
Kód UT WoS článku
000398838400004
EID výsledku v databázi Scopus
2-s2.0-85016980207