Release of cytokines induced by Salmonella typhimurium porins

Galdiero, F; L'ero, G. Cipollaro De; Benedetto, N; Galdiero, Marilena; Tufano, Maria Antonietta

doi:10.1128/iai.61.1.155-161.1993

Cited by 106 publications

(57 citation statements)

References 48 publications

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“…The binding of S. typhimurium porins to human polymorphonuclear leukocytes induces a decreased oxidative burst in these cells as well as inhibits their migration in the presence of chemotactic agents [32]. Salmonella typhimurium porins bind to the membranes of polymorphonuclear leukocytes [33]; moreover, they incorporate into MÖ membranes [34]. Subcellular events in macrophages following attachment of the 44-kDa protein have not yet been characterized.…”

Section: -Kdamentioning

confidence: 99%

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

Negm

1998

FEMS Immunology and Medical Microbiology

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Murine peritoneal macrophages bind to Salmonella typhimurium in vitro in the absence of exogenous opsonins. We have identified an outer membrane protein of S. typhimurium that mediates this adhesion. Biotin-labeled macrophages were used to probe electroblotted envelope proteins of S. typhimurium that had been previously resolved by polyacrylamide electrophoresis under denaturing and reducing conditions. Macrophages bound to an outer membrane protein with an apparent molecular mass of 44 kDa. The protein was purified to homogeneity and free of detectable lipopolysaccharide. Limited microsequencing of this protein resulted in a 15-amino acid query sequence of A-E-V-Y-N-K-D-G-N-K-L-D-L-Y-G, which shares complete identity with a 15-mer of both the OmpD of S. typhimurium SH 7454 and the OmpC polypeptide of Escherichia coli K-12. Picomolar concentrations of this purified protein significantly inhibited the subsequent adherence of 35S-labeled S. typhimurium to macrophages in monolayers. We propose that this 44-kDa protein is involved in the recognition of S. typhimurium by macrophage during the initial stages of infection.

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Section: -Kdamentioning

confidence: 99%

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

Negm

1998

FEMS Immunology and Medical Microbiology

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“…Since the mid-1980s, a major OMP of Salmonella has been the subject of much investigation, and our earlier work has shown that porins afford protection against Salmonella infection [6][7][8][9]. Several workers have demonstrated porins to be important antigens, which elicit CMI responses through a delayed-type hypersensitivity reaction, interleukin-2 (IL-2) and interferon-g (IFN-g) production, and mitogenic effects on T and B cells [4,10]. Porins also activate the complement system and contribute to the pathogenesis of the bacterial infection [11,12].…”

Section: Introductionmentioning

confidence: 99%

Priming of T‐Cell Responses in Mice by Porins of Salmonella typhimurium

Gupta

1998

Scand J Immunol

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An imbalance in signals delivered to T cells via T-cell receptor and accessory molecules can lead to anergy, apoptosis, or both. In the present study we have demonstrated that Salmonella typhimurium infection in mice leads to a progressive loss of CD4 þ T helper (Th) cell population, abnormal T-cell death by apoptosis and loss of accessory molecules (B7 and intracellular adhesion molecule-1) on macrophages. Quantification of interleukin-2 (IL-2), interleukin-4 (IL-4) and interferon-g (IFN-g) secretion revealed a Th2-type of response in lymphocytes isolated from spleen. However, preimmunization of mice with porins resulted in an increased CD4þ Th cell population and accessory molecules on the surface of macrophages. Quantification of cytokines revealed a Th1-type of response. We conclude that preimmunization of mice with porins provides a microenvironment in which a well-balanced accessory molecule and cytokine network is established, which results in the prevention of cell death by apoptosis.

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“…The stimulation of CMI by porin immunization could be due to the amphiphilicity and amount of this protein, or to its intrinsic immunogenicity. Porins induce lymphocytes to secrete IL-2 and IFN-y ( [4,9] and not shown), and IFN-y can initiate macrophage effector activities in vitro. Certainly, the antigen-activated T cells could be involved at least as a source of IFN-y in this cascade, and presently, it is hypothesized that macrophages could be activated by soluble TNF-a and IFN-y secreted by Thl cells, secreted IFN-y and membranebound TNF-a and by cognate interactions [28].…”

Section: Discussionmentioning

confidence: 99%

Macrophage‐T cell interaction in murine salmonellosis: selective down‐regulation of ICAM‐1 and B7 molecules in infected macrophages and its probable role in cell‐mediated immunity

et al. 1996

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Vaccine development and understanding of cellular immune modulatory mechanisms in salmonella infections have been impeded due to the paucity of data on antigens capable of eliciting effective immune responses. The present study was done to evaluate the efficacy of five major purified salmonella antigens (porins, pili, flagella, outer membrane proteins and heat shock proteins) in modulating T cell-macrophage interactions which play a central role in resistance to and recovery from infection with several intracellular pathogens, including salmonella. The results showed that the T cells recovered 10 days post-immunization (D10 T cells) from mice immunized with porins and outer membrane proteins showed maximum proliferation in the presence of macrophages incubated with dead bacteria; however, this response was decreased when T cells were co-cultured with live Salmonella typhimurium-infected macrophages. Delayed-type hypersensitivity responses, as measured by increased footpad thickness at 24 h, though induced effectively by porins, pili and flagella, were completely abrogated when D10 T cells were pre-incubated with macrophages infected with live bacteria. The phagocytic and bactericidal ability of normal macrophages, when grown in presence of T cell supernatants, was not influenced by the immunizing agents, but T cell supernatants obtained from mice immunized with porins and heat-shock protein triggered increased bactericidal activity. Further, the expression of the co-stimulatory molecules ICAM-1 and B7 increased with increasing bacteria (dead):macrophage ratio, but this expression was down-regulated upon incubation with live bacteria.

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Release of cytokines induced by Salmonella typhimurium porins

Cited by 106 publications

References 48 publications

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

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

Priming of T‐Cell Responses in Mice by Porins of Salmonella typhimurium

Macrophage‐T cell interaction in murine salmonellosis: selective down‐regulation of ICAM‐1 and B7 molecules in infected macrophages and its probable role in cell‐mediated immunity

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