Cooperation of both, the FKBP N-like and the DSBA-like, domains is necessary for the correct function of FTS 1067 protein involved in Francisella tularensis virulence and pathogenesis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F15%3A43875427" target="_blank" >RIV/60162694:G44__/15:43875427 - isvavai.cz</a>

Výsledek na webu

<a href="http://femspd.oxfordjournals.org/content/73/6/ftv030" target="_blank" >http://femspd.oxfordjournals.org/content/73/6/ftv030</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/femspd/ftv030" target="_blank" >10.1093/femspd/ftv030</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Cooperation of both, the FKBP N-like and the DSBA-like, domains is necessary for the correct function of FTS 1067 protein involved in Francisella tularensis virulence and pathogenesis

Popis výsledku v původním jazyce

Francisella tularensis the etiological agent of tularaemia is one of the most infectious human pathogen known. Our knowledge about its key virulence factors has increased recently but it still remains a lot to explore. One of the described essential virulence factors is membrane lipoprotein FTS 1067 (nomenclature of F. tularensis subsp. holarctica strain FSC200) with homology to the protein family of disulphide oxidoreductases DsbA. Lipoprotein consists of two different domains: the C-terminal DsbA Com1-like domain (DSBA-like) and the N-terminal FKBP-type peptidyl-prolyl cis/trans isomerases (FKBP N-like). To uncover the biological role of these domains, we created bacterial strain with deletion of the DSBA-like domain. This defect in gene coding for lipoprotein FTS 1067 led to high in vivo attenuation associated with the ability to induce host protective immunity. Analyses performed with the truncated recombinant protein showed that the absence of DSBA-like domain revealed the loss of

Název v anglickém jazyce

Cooperation of both, the FKBP N-like and the DSBA-like, domains is necessary for the correct function of FTS 1067 protein involved in Francisella tularensis virulence and pathogenesis

Popis výsledku anglicky

Francisella tularensis the etiological agent of tularaemia is one of the most infectious human pathogen known. Our knowledge about its key virulence factors has increased recently but it still remains a lot to explore. One of the described essential virulence factors is membrane lipoprotein FTS 1067 (nomenclature of F. tularensis subsp. holarctica strain FSC200) with homology to the protein family of disulphide oxidoreductases DsbA. Lipoprotein consists of two different domains: the C-terminal DsbA Com1-like domain (DSBA-like) and the N-terminal FKBP-type peptidyl-prolyl cis/trans isomerases (FKBP N-like). To uncover the biological role of these domains, we created bacterial strain with deletion of the DSBA-like domain. This defect in gene coding for lipoprotein FTS 1067 led to high in vivo attenuation associated with the ability to induce host protective immunity. Analyses performed with the truncated recombinant protein showed that the absence of DSBA-like domain revealed the loss of

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

—

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Pathogens and Disease

ISSN

2049-632X

e-ISSN

—

Svazek periodika

73

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

12

Strana od-do

"Article Number: UNSP ftv030"

Kód UT WoS článku

000362574300002

EID výsledku v databázi Scopus

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