J 2011

LPS structure influences protein secretion in Salmonella enterica

CRHÁNOVÁ, Magdaléna; M. MALCOVA; Monika MAZGAJOVÁ; D. KARASOVA; A. SEBKOVA et al.

Základní údaje

Originální název

LPS structure influences protein secretion in Salmonella enterica

Autoři

CRHÁNOVÁ, Magdaléna; M. MALCOVA; Monika MAZGAJOVÁ; D. KARASOVA; A. SEBKOVA; A. FUCIKOVA; Zbyněk BORTLÍČEK; Lenka PILOUSOVÁ; K. KYROVA; M. DEKANOVA a I. RYCHLIK

Vydání

Veterinary Microbiology, Amsterdam, Elsevier, 2011, 0378-1135

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 3.327

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/11:00081770

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

Salmonella; LPS; rfaC; Protein secretion; Motility; SPI-1

Štítky

Změněno: 28. 4. 2016 12:49, Ing. Andrea Mikešková

Anotace

V originále

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. (C) 2011 Elsevier B.V. All rights reserved.