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Statements

Subject Item
n2:RIV%2F60162694%3AG44__%2F11%3A00002556%21RIV12-MO0-G44_____
rdf:type
n5:Vysledek skos:Concept
rdfs:seeAlso
http://dx.doi.org/10.1016/j.vetmic.2011.04.018
dcterms:description
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. 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.
dcterms:title
LPS structure influences protein secretion in Salmonella enteritica LPS structure influences protein secretion in Salmonella enteritica
skos:prefLabel
LPS structure influences protein secretion in Salmonella enteritica LPS structure influences protein secretion in Salmonella enteritica
skos:notation
RIV/60162694:G44__/11:00002556!RIV12-MO0-G44_____
n3:aktivita
n16:I n16:P n16:Z
n3:aktivity
I, P(ED0006/01/01), Z(MO0FVZ0000501), Z(MZE0002716202)
n3:cisloPeriodika
1-2
n3:dodaniDat
n14:2012
n3:domaciTvurceVysledku
n6:9773401
n3:druhVysledku
n12:J
n3:duvernostUdaju
n4:S
n3:entitaPredkladatele
n20:predkladatel
n3:idSjednocenehoVysledku
210052
n3:idVysledku
RIV/60162694:G44__/11:00002556
n3:jazykVysledku
n19:eng
n3:klicovaSlova
Salmonella; LPS; rfaC; protein secretion; motility; SPI-1
n3:klicoveSlovo
n11:rfaC n11:SPI-1 n11:LPS n11:protein%20secretion n11:motility n11:Salmonella
n3:kodStatuVydavatele
NL - Nizozemsko
n3:kontrolniKodProRIV
[C73D1CAC7D41]
n3:nazevZdroje
Veterinary Microbiology
n3:obor
n13:EE
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
11
n3:projekt
n18:ED0006%2F01%2F01
n3:rokUplatneniVysledku
n14:2011
n3:svazekPeriodika
152
n3:tvurceVysledku
Fučíková, Alena Malcova, Marcela Mazgajova, Monika Crhanova, Magdaléna Bortlicek, Zbyněk Rychlik, Ivan Kyrova, Kamila Karasová, Daniela Děkanová, Michela Šebková, Alena Pilousová, Lenka
n3:wos
000294095000015
n3:zamer
n9:MZE0002716202 n9:MO0FVZ0000501
s:issn
0378-1135
s:numberOfPages
7
n7:organizacniJednotka
G44