2003
DOI: 10.1128/jb.185.19.5901-5905.2003
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Global Regulation of the Salmonella enterica Serovar Typhimurium Major Porin, OmpD

Abstract: The OmpD porin is the most abundant outer membrane protein in Salmonella enterica serovar Typhimurium and represents about 1% of total cell protein. Unlike the case with the less abundant OmpC and OmpF porins, the stoichiometry of OmpD in the outer membrane does not change in response to changes in osmolarity. The abundance of OmpD increases in response to anaerobiosis and decreases in response to low pH, conditions encountered by serovar Typhimurium during the infection of its murine host. By constructing an … Show more

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Cited by 49 publications
(47 citation statements)
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“…Salmonella OMP fraction was purifed by the method of Santiviago et al (2003) and analyzed by polyacrylamide gel electrophoresis as described previosuly (Bossi and Figueroa-Bossi 2007).…”
Section: Omp Preparationmentioning
confidence: 99%
“…Salmonella OMP fraction was purifed by the method of Santiviago et al (2003) and analyzed by polyacrylamide gel electrophoresis as described previosuly (Bossi and Figueroa-Bossi 2007).…”
Section: Omp Preparationmentioning
confidence: 99%
“…OmpD is a trimeric porin with homology to OmpF and OmpC (9, 15) whose expression is enhanced by anaerobiosis and suppressed by low pH, whereas OmpF and OmpC expression is sensitive to changes in osmolarity (16). OmpD has an unclear role in infection whereas loss of OmpR is attenuating (17,18).…”
Section: Discussionmentioning
confidence: 99%
“…OmpD is one of the most abundant outer membrane proteins of S. enterica serovar Typhimurium and is regulated by a multiplicity of environmental factors, including anaerobiosis, lower pH, and catabolite repression (33). As shown in showed a 4-fold elevation in resistance to ceftriaxone compared to strain 01-4; however, there was no difference in MIC value when ompC was deleted to give strain 01-4(⌬ompC).…”
Section: Discussionmentioning
confidence: 99%