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
UT WoS
Klíčová slova anglicky
Salmonella; LPS; rfaC; Protein secretion; Motility; SPI-1
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.