Macrophages recognize and adhere to an OmpD-like protein of Salmonella typhimurium

Negm, R

doi:10.1016/s0928-8244(98)00011-x

Cited by 8 publications

(11 citation statements)

References 30 publications

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“…In contrast, earlier studies from our laboratory showed a 5-fold decrease in attachment of an ompC mutant to murine peritoneal macrophages compared with the wild-type strain (Negm and Pistole 1999). Our laboratory also showed that picomolar concentrations of an OmpD-like protein from Salmonella serovar Typhimurium inhibited attachment of this microorganism to murine peritoneal macrophages (Negm and Pistole 1998).…”

Section: Introductioncontrasting

confidence: 88%

“…There was no significant difference in binding for the 2 strains (p = 0.704, n = 4). murine peritoneal macrophages (Negm and Pistole 1998). They differ, however, from those of Meyer et al (1998), who found no significant difference in adherence of wild-type and ompD mutant Salmonella serovar Typhimurium to 407 cells, a human intestinal cell line.…”

Section: Discussioncontrasting

confidence: 68%

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OmpD but not OmpC is involved in adherence ofSalmonella entericaserovar Typhimurium to human cells

Hara-Kaonga¹,

Pistole²

2004

Can. J. Microbiol.

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Conflicting reports exist regarding the role of porins OmpC and OmpD in infections due to Salmonella enterica serovar Typhimurium. This study investigated the role of these porins in bacterial adherence to human macrophages and intestinal epithelial cells. ompC and ompD mutant strains were created by transposon mutagenesis using P22-mediated transduction of Tn10 and Tn5 insertions, respectively, into wild-type strain 14028. Fluorescein-labeled wild-type and mutant bacteria were incubated with host cells at various bacteria to cell ratios for 1 h at 37 degrees C and analyzed by flow cytometry. The mean fluorescence intensity of cells with associated wild-type and mutant bacteria was used to estimate the number of bacteria bound per host cell. Adherence was also measured by fluorescence microscopy. Neither assay showed a significant difference in binding of the ompC mutant and wild-type strains to the human cells. In contrast, the ompD mutant exhibited lowered binding to both cell types. Our findings suggest that OmpD but not OmpC is involved in the recognition of Salmonella serovar Typhimurium by human macrophages and intestinal epithelial cells.

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Section: Introductioncontrasting

confidence: 88%

Section: Discussioncontrasting

confidence: 68%

OmpD but not OmpC is involved in adherence ofSalmonella entericaserovar Typhimurium to human cells

Hara-Kaonga¹,

Pistole²

2004

Can. J. Microbiol.

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“…In S . Typhimurium, OmpC and OmpF porins are recognized by macrophages, participate in phagocytosis and trigger a signaling cascade which regulates the ROS response by the host and the phagolysosomal maturation [13], [14]. Furthermore, mutants in the S .…”

Section: Introductionmentioning

confidence: 99%

“…Other studies have shown that OmpD is involved in adherence and recognition of S . Typhimurium to human macrophages and intestinal epithelial cells, during the initial stages of infection [13], [20]. Moreover, studies based on the B1b cell antibody response showed that OmpD is a key factor in the humoral response in mice [21].…”

Section: Introductionmentioning

confidence: 99%

Participation of the Salmonella OmpD Porin in the Infection of RAW264.7 Macrophages and BALB/c Mice

et al. 2014

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Salmonella Typhimurium is the etiological agent of gastroenteritis in humans and enteric fever in mice. Inside these hosts, Salmonella must overcome hostile conditions to develop a successful infection, a process in which the levels of porins may be critical. Herein, the role of the Salmonella Typhimurium porin OmpD in the infection process was assessed for adherence, invasion and proliferation in RAW264.7 mouse macrophages and in BALB/c mice. In cultured macrophages, a ΔompD strain exhibited increased invasion and proliferation phenotypes as compared to its parental strain. In contrast, overexpression of ompD caused a reduction in bacterial proliferation but did not affect adherence or invasion. In the murine model, the ΔompD strain showed increased ability to survive and replicate in target organs of infection. The ompD transcript levels showed a down-regulation when Salmonella resided within cultured macrophages and when it colonized target organs in infected mice. Additionally, cultured macrophages infected with the ΔompD strain produced lower levels of reactive oxygen species, suggesting that down-regulation of ompD could favor replication of Salmonella inside macrophages and the subsequent systemic dissemination, by limiting the reactive oxygen species response of the host.

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“…The OmpD porin must play a critical role in the survival of S. typhimurium in certain environments, because OmpD facilitates the entry of some critical nutrients (Nikaido, 1996). Furthermore, OmpD may also play a critical role in the interactions between S. typhimurium and host cells, and is likely to be involved in the adhesion of S. typhimurium to murine macrophages (Negm & Pistole, 1998). The characterization of this important genomic difference between S. typhi and other Salmonella serovars that includes ompD is significant for the following three reasons.…”

Section: Discussionmentioning

confidence: 99%

A chromosomal region surrounding the ompD porin gene marks a genetic difference between Salmonella typhi and the majority of Salmonella serovars

et al. 2001

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In this work it is shown that the majority of Salmonella serovars most frequently associated with the systemic infection of vertebrate hosts produce a major outer-membrane porin, OmpD. However, OmpD is absent from the outer-membrane protein profiles of Salmonella typhi strain Ty2 and 26 clinical isolates of S. typhi examined by SDS-PAGE. To determine whether the ompD gene is present in S. typhi, primers internal to the ompD coding sequence were used to amplify the gene by PCR. With the exception of S. typhi strains, the ompD gene was amplified from the genomes of all Salmonella serovars tested. Consistently, a specific ompD probe did not hybridize with DNA isolated from the S. typhi strains. Taken together, these results demonstrate that S. typhi does not produce OmpD due to the absence of the ompD gene. Furthermore, it was investigated whether the deletion of ompD extended to smvA. This gene is adjacent to ompD in the Salmonella typhimurium chromosome and encodes a protein involved in the resistance to methyl viologen, a superoxide-generating agent. Although PCR failed to amplify the smvA gene from the S. typhi strain Ty2 genome, it was possible to amplify it from the chromosome of the clinical strains. On the other hand, hybridization analyses showed that the smvA gene is present in all the S. typhi strains tested. In contrast to the other Salmonella serovars, S. typhi strain Ty2 and the clinical isolates showed sensitivity to methyl viologen, suggesting that smvA gene is inactive in S. typhi. In conclusion, the ompD-smvA region is variable in structure among Salmonella serovars. It is hypothesized that the absence of ompD may suggest a role in host specificity.

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Macrophages recognize and adhere to an OmpD-like protein of Salmonella typhimurium

Cited by 8 publications

References 30 publications

OmpD but not OmpC is involved in adherence ofSalmonella entericaserovar Typhimurium to human cells

OmpD but not OmpC is involved in adherence ofSalmonella entericaserovar Typhimurium to human cells

Participation of the Salmonella OmpD Porin in the Infection of RAW264.7 Macrophages and BALB/c Mice

A chromosomal region surrounding the ompD porin gene marks a genetic difference between Salmonella typhi and the majority of Salmonella serovars

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