The immunochemistry of <i>Salmonella</i> chemotype VI O-antigens. The structure of oligosaccharides from Salmonella group U (o 43) lipopolysaccharides

Lüderitz, Otto; Simmons, D. A. R.; Westphal, Götz A.

doi:10.1042/bj0970820

Cited by 48 publications

(22 citation statements)

References 4 publications

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“…Today, one can look back at the work of these pioneers in LPS chemistry and biology [185][186][187][188][189] with a great deal of respect and admiration. Although these studies on the pyrogenicity of LPS were primarily conducted in rabbits and sheep, 190,191 pioneers such as Sheldon Wolff and Sheldon Greisman used human subjects, mostly volunteers, to investigate the human febrile responses to intravenously injected LPS in humans.…”

Section: Pioneers In the Chemistry And Pyrogenicity Of Lpsmentioning

confidence: 99%

Infection, fever, and exogenous and endogenous pyrogens: some concepts have changed

Dinarello¹

2004

J. Endotoxin Res.

246

210

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For many years, it was thought that bacterial products caused fever via the intermediate production of a host-derived, fever-producing molecule, called endogenous pyrogen (EP). Bacterial products and other fever-producing substances were termed exogenous pyrogens. It was considered highly unlikely that exogenous pyrogens caused fever by acting directly on the hypothalamic thermoregulatory center since there were countless fever-producing microbial products, mostly large molecules, with no common physical structure. In vivo and in vitro, lipopolysaccharides (LPSs) and other microbial products induced EP, subsequently shown to be interleukin-1 (IL-1). The concept of the 'endogenous pyrogen' cause of fever gained considerable support when pure, recombinant IL-1 produced fever in humans and in animals at subnanomolar concentrations. Subsequently, recombinant tumor necrosis factor-alpha (TNF-alpha), IL-6 and other cytokines were also shown to cause fever and EPs are now termed pyrogenic cytokines. However, the concept was challenged when specific blockade of either IL-1 or TNF activity did not diminish the febrile response to LPS, to other microbial products or to natural infections in animals and in humans. During infection, fever could occur independently of IL-1 or TNF activity. The cytokine-like property of Toll-like receptor (TLR) signal transduction provides an explanation by which any microbial product can cause fever by engaging its specific TLR on the vascular network supplying the thermoregulatory center in the anterior hypothalamus. Since fever induced by IL-1, TNF-alpha, IL-6 or TLR ligands requires cyclooxygenase-2, production of prostaglandin E2 (PGE2) and activation of hypothalamic PGE2 receptors provides a unifying mechanism for fever by endogenous and exogenous pyrogens. Thus, fever is the result of either cytokine receptor or TLR triggering; in autoimmune diseases, fever is mostly cytokine mediated whereas both cytokine and TLR account for fever during infection.

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Section: Pioneers In the Chemistry And Pyrogenicity Of Lpsmentioning

confidence: 99%

Infection, fever, and exogenous and endogenous pyrogens: some concepts have changed

Dinarello¹

2004

J. Endotoxin Res.

246

210

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“…These enterobacteria may, thus, serve as an antigenic reservoir, continuously stimulating anti-Gal production. Structure analysis of carbohydrates in LPS of enterobacteria have demonstrated oligosaccharides with terminal e-galactosyl residues (termed e-galactosyl-like epitopes) on bacteria such as Salmonella [59], Klebsiella [9,15], E. coli [49,50] and Clostridia [43]. These epitopes contain galactosyl or glucosyl penultimate to the terminal e-galactosyl residues and are structurally different from the e-galactosyl epitope which has not been found in bacteria.…”

Section: Anti-gal and Infectious Agentsmentioning

confidence: 99%

Evolution and pathophysiology of the human natural anti-?-galactosyl IgG (anti-Gal) antibody

Galili

1993

Springer Semin Immunopathol

180

132

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Anti-Gal is a human natural antibody which interacts specifically with the mammalian carbohydrate structure Gal alpha 1-3Gal beta 1-4GlcNAc-R, termed, the alpha-galactosyl epitope. This antibody constitutes approximately 1% of circulating IgG in human serum and is produced, upon stimulation, by 1% of circulating B lymphocytes. Anti-Gal is also present as IgA antibodies in body secretions such as saliva, milk and colostrum. The antigenic source for the constant production of anti-Gal seems to be the alpha-galactosyl-like epitopes found on many bacteria of the gastrointestinal flora. Whereas anti-Gal is abundant in humans, apes and Old World monkeys, it is absent from New World monkeys, prosimians and nonprimate mammals. The latter group of species produces, however, large amounts of alpha-galactosyl epitopes (> 10(6) epitopes per cell). It is estimated that anti-Gal appeared in ancestral Old World primates less than 28 million years ago, possibly as a result of an evolutionary event which exerted a selective pressure for the suppression of alpha-galactosyl epitopes expression by inactivation of the gene for the enzyme alpha 1,3 galactosyltransferase. This also resulted in the loss of immune tolerance to the alpha-galactosyl epitope and the production of anti-Gal. The physiologic role of this antibody is not clear as yet. It may participate in the protection against gastrointestinal bacteria. In addition it seems to contribute to the removal of normal and pathologically senescent red cells by interacting with the few hundred cryptic alpha-galactosyl epitopes which are exposed de novo in the course of red cell aging, thereby opsonizing these cells for phagocytosis by reticuloendothelial macrophages. The alpha-galactosyl epitope has been found to be aberrantly expressed on human cells and the interaction of anti-Gal with such epitopes may result in autoimmune disease. Preliminary data suggest such a mechanism in Graves' disease. Anti-Gal has been found to interact with therapeutic recombinant proteins expressing alpha-galactosyl epitopes, but so far there is no indication that it affects the half-life in the circulation and the biologic activity. Detection of anti-Gal in the seminal fluid and in the cerebrospinal fluid may serve as a simple means for assessment of damage to the blood-genital tract barrier or the blood-brain barrier. Studies on the interaction of anti-Gal with aberrantly expressed alpha-galactosyl epitopes on human cells may elucidate the possible role of anti-Gal in human autoimmune diseases.

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“…However, the contemporaneous production of anti-Gal in humans, anthropoid apes, and Old World monkeys probably represents an ongoing immune response to Galal-+3Gal structures found on various gastrointestinal bacteria, including Salmonella, Klebsiella, and Escherichia coli (16)(17)(18). Our studies have indeed demonstrated a specific in vitro interaction of purified anti-Gal with these bacterial strains (unpublished data).…”

Section: Discussionmentioning

confidence: 99%

Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1----3Gal epitope in primates.

Galili¹,

Clark²,

Shohet³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

523

412

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The immunochemistry of Salmonella chemotype VI O-antigens. The structure of oligosaccharides from Salmonella group U (o 43) lipopolysaccharides

Cited by 48 publications

References 4 publications

Infection, fever, and exogenous and endogenous pyrogens: some concepts have changed

Infection, fever, and exogenous and endogenous pyrogens: some concepts have changed

Evolution and pathophysiology of the human natural anti-?-galactosyl IgG (anti-Gal) antibody

Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1----3Gal epitope in primates.

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