MATIAŠOVIC, Ján, Hana ŠTEPÁNOVÁ, Jiří VOLF, Lukáš KUBALA, Petra OVESNÁ, Ivan RYCHLÍK and Martin FALDYNA. Influence of the lipopolysaccharide structure of Salmonella enterica serovar Enteritidis on interactions with pig neutrophils. Veterinary Microbiology. 2011, vol. 150, 1-2, p. 167-172. ISSN 0378-1135. Available from: https://dx.doi.org/10.1016/j.vetmic.2011.01.007.
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Basic information
Original name Influence of the lipopolysaccharide structure of Salmonella enterica serovar Enteritidis on interactions with pig neutrophils
Authors MATIAŠOVIC, Ján (703 Slovakia, guarantor), Hana ŠTEPÁNOVÁ (203 Czech Republic), Jiří VOLF (203 Czech Republic), Lukáš KUBALA (203 Czech Republic), Petra OVESNÁ (203 Czech Republic, belonging to the institution), Ivan RYCHLÍK (203 Czech Republic) and Martin FALDYNA (203 Czech Republic).
Edition Veterinary Microbiology, 2011, 0378-1135.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Netherlands
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.327
RIV identification code RIV/00216224:14110/11:00053445
Organization unit Faculty of Medicine
Doi http://dx.doi.org/10.1016/j.vetmic.2011.01.007
UT WoS 000290696500022
Keywords in English Salmonella; Pig; Pathogen-associated molecular patterns; Lipopolysaccharide; Neutrophil
Tags International impact
Changed by Changed by: Mgr. Michal Petr, učo 65024. Changed: 11/4/2012 15:54.
Abstract
The key process for immune response development is the recognition of bacteria by the immune system of the host based on the sensing of pathogen-associated molecular patterns (PAMP). One of the most important PAMP is the lipopolysaccharide (LPS) molecule, a complex molecule present in the outer membrane of Gram negative bacteria. In this study we were interested in how different parts of the LPS of Salmonella enterica serovar Enteritidis are recognized by porcine neutrophils. To this aim, we constructed S. Enteritidis mutants with rfaL and rfaC genes disabled in the attachment of the O-antigen and in the synthesis of the inner oligosaccharide core of LPS, respectively.We found that in the absence of serum, both the rfa mutants associated with neutrophils and stimulated them for reactive oxygen species (ROS) production significantly more than the wild-type strain. Addition of polymyxin B, which neutralized lipid A, the endotoxic moiety of LPS, effectively decreased the association of the wild-type strain and the rfaC mutant with neutrophils, but not the rfaL mutant. This indicates that the oligosaccharide core newly exposed on the surface in the rfaL mutant, protected from interaction in the wild-type strain by the O-antigen but completely absent in the rfaC mutant, may represent a new ligand for porcine neutrophils that cannot be neutralized by polymyxin B.
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