Using proteomics to identify host cell interaction partners for VgrG and IglJ

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F20%3A00556188" target="_blank" >RIV/60162694:G44__/20:00556188 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11160/20:10417508

Výsledek na webu

<a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7471685/" target="_blank" >https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7471685/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-020-71641-3" target="_blank" >10.1038/s41598-020-71641-3</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Using proteomics to identify host cell interaction partners for VgrG and IglJ

Popis výsledku v původním jazyce

Francisella tularensis is a highly virulent intracellular bacterium and the causative agent of tularemia. The disease is characterized by the suboptimal innate immune response and consequently by the impaired adaptive immunity. The virulence of this pathogen depends on proteins encoded by a genomic island termed the Francisella Pathogenicity Island (FPI). However, the precise biological roles of most of the FPI-encoded proteins remain to be clarified. In this study, we employed stable isotope labeling by amino acids in cell culture (SILAC) in combination with affinity protein purification coupled with liquid chromatography-mass spectrometry to identify potential protein-effector binding pairs for two FPI virulence effectors IglJ and VgrG. Our results may indicate that while the IglJ protein interactions primarily affect mitochondria, the VgrG interactions affect phagosome and/or autophagosome biogenesis via targeting components of the host's exocyst complex.

Název v anglickém jazyce

Using proteomics to identify host cell interaction partners for VgrG and IglJ

Popis výsledku anglicky

Francisella tularensis is a highly virulent intracellular bacterium and the causative agent of tularemia. The disease is characterized by the suboptimal innate immune response and consequently by the impaired adaptive immunity. The virulence of this pathogen depends on proteins encoded by a genomic island termed the Francisella Pathogenicity Island (FPI). However, the precise biological roles of most of the FPI-encoded proteins remain to be clarified. In this study, we employed stable isotope labeling by amino acids in cell culture (SILAC) in combination with affinity protein purification coupled with liquid chromatography-mass spectrometry to identify potential protein-effector binding pairs for two FPI virulence effectors IglJ and VgrG. Our results may indicate that while the IglJ protein interactions primarily affect mitochondria, the VgrG interactions affect phagosome and/or autophagosome biogenesis via targeting components of the host's exocyst complex.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10700 - Other natural sciences

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

Scientific Reports

ISSN

2045-2322

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

9

Strana od-do

14612

Kód UT WoS článku

000571229700104

EID výsledku v databázi Scopus

2-s2.0-85090166789