Relationship of Triamine-Biocide Tolerance of Salmonella enterica Serovar Senftenberg to Antimicrobial Susceptibility, Serum Resistance and Outer Membrane Proteins

ABSTRACT Mutant 7F2 of Salmonella enterica serovar Typhimurium has a transposon inserted in the regulator gene baeR of a two-component system and showed a more-than-fourfold reduction in resistance to ceftriaxone. Complementation analysis suggested an association among the outer membrane proteins OmpW and STM3031, ceftriaxone resistance, and baeR.

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Detection of virulence genes and investigation of the immunogenicity of outer membrane proteins of Salmonella enterica

Journal of Applied Biology & Biotechnology ◽

10.7324/jabb.2019.70511 ◽

2019 ◽

Vol 7 (5) ◽

pp. 62-73

Keyword(s):

Membrane Proteins ◽

Outer Membrane ◽

Salmonella Enterica ◽

Virulence Genes ◽

Outer Membrane Proteins

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The mechanisms of complement activation in normal bovine serum and normal horse serum against Yersinia enterocolitica O:9 strains with different outer membrane proteins content

Polish Journal of Veterinary Sciences ◽

10.1515/pjvs-2016-0013 ◽

2016 ◽

Vol 19 (1) ◽

pp. 99-107 ◽

Cited By ~ 2

Author(s):

K. Miętka ◽

K. Brzostek ◽

K. Guz-Regner ◽

G. Bugla-Płoskońska

Keyword(s):

Membrane Proteins ◽

Outer Membrane ◽

Yersinia Enterocolitica ◽

Bactericidal Activity ◽

Complement Activation ◽

Alternative Pathway ◽

Outer Membrane Proteins ◽

Serum Resistance ◽

Main Role ◽

Wild Type

AbstractYersinia enterocolitica is a common zoonotic pathogen and facultative intracellular bacterium which can survive within blood cells. Cattle and horses are considered a reservoir of Y. enterocolitica which often causes several serious syndromes associated with yersiniosis such as abortions, premature births or infertility. The aim of our investigation was to determine the vitality of Y. enterocolitica O:9 strains (Ye9) in bovine and horse sera (NBS and NHrS) and explain the role of outer membrane proteins (OMPs) in serum resistance of these bacteria. Our previous studies demonstrated moderate human serum (NHS) resistance of the wild type Ye9 strain, whereas mutants lacking YadA, Ail or OmpC remained sensitive to the bactericidal activity of NHS. The present study showed that the wild type of Ye9 strain was resistant to the bactericidal activity of both NHrS and NBS, while Ye9 mutants lacking the YadA, Ail and OmpC proteins were sensitive to NHrS and NBS as well as to NHS. The mechanisms of complement activation against Ye9 strains lacking Ail and YadA were distinguished, i.e. activation of the classical/lectin pathways decisive in the bactericidal mechanism of complement activation of NBS, parallel activation of the classical/lectin and alternative pathways of NHrS. In this research the mechanism of independent activation of the classical/lectin or the alternative pathway of NBS and NHrS against Ye9 lacking OmpC porin was also established. The results indicate that serum resistance of Ye9 is multifactorial, in which extracellular structures, i.e. outer membrane proteins (OMPs) such as Ail, OmpC or YadA, play the main role.

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