LPS structure influences protein secretion in Salmonella enterica

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F11%3A00052915" target="_blank" >RIV/00216224:14110/11:00052915 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00027162:_____/11:#0000747 RIV/00216224:14310/11:00081770

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.vetmic.2011.04.018" target="_blank" >http://dx.doi.org/10.1016/j.vetmic.2011.04.018</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.vetmic.2011.04.018" target="_blank" >10.1016/j.vetmic.2011.04.018</a>

Jazyk výsledku

angličtina

Název v původním jazyce

LPS structure influences protein secretion in Salmonella enterica

Popis výsledku v původním jazyce

In this study we have compared protein secretion in the wild type of S. Typhimurium and the rfaC mutant. We found out that the rfaC mutant was defective in protein secretion. In addition, the rfaC mutant was defective in its invasion into an IPEC-J2 porcine epithelial cell line and also in motility in semisolid agar. Consistent with this, reduced flagella numbers were observed in the rfaC mutant. In the rfaC mutant, there were no defects in flagellin expression as detected by western blot and immune electron microscopy which demonstrated equal amounts of flagellin in the cytoplasm of both the rfaC mutant and the wild-type S. Typhimurium. However, in the wild-type strain only, the flagellin was assembled to spatially restricted areas on the inner side of cytoplasmic membrane. The oligosaccharide core of LPS is therefore required for the assembly of flagella and T3SS secretion machinery followed by protein secretion.

Název v anglickém jazyce

LPS structure influences protein secretion in Salmonella enterica

Popis výsledku anglicky

In this study we have compared protein secretion in the wild type of S. Typhimurium and the rfaC mutant. We found out that the rfaC mutant was defective in protein secretion. In addition, the rfaC mutant was defective in its invasion into an IPEC-J2 porcine epithelial cell line and also in motility in semisolid agar. Consistent with this, reduced flagella numbers were observed in the rfaC mutant. In the rfaC mutant, there were no defects in flagellin expression as detected by western blot and immune electron microscopy which demonstrated equal amounts of flagellin in the cytoplasm of both the rfaC mutant and the wild-type S. Typhimurium. However, in the wild-type strain only, the flagellin was assembled to spatially restricted areas on the inner side of cytoplasmic membrane. The oligosaccharide core of LPS is therefore required for the assembly of flagella and T3SS secretion machinery followed by protein secretion.

Druh

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

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

—

Projekt

<a href="/cs/project/ED0006%2F01%2F01" target="_blank" >ED0006/01/01: Centrum pro aplikovanou mikrobiologii a imunologii ve veterinární medicíne</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Veterinary Microbiology

ISSN

0378-1135

e-ISSN

—

Svazek periodika

152

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

IE - Irsko

Počet stran výsledku

7

Strana od-do

131-137

Kód UT WoS článku

000294095000015

EID výsledku v databázi Scopus

—