Protective immunity induced in mice by detoxified salmonella lipopolysaccharide

Ding, Han-Jen; Nakoneczna, Irene; Hsu, H. S.

doi:10.1099/00222615-31-2-95

Cited by 37 publications

(21 citation statements)

References 20 publications

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“…Ester-linked fatty acids in lipid A may be important in this protease recognition LPS, as a derivative unable to activate the proPO system (LPSdex) has been depleted of ester-linked fatty acids (Seid & Sado#, 1981). Deacylated LPS has been shown to be up to 1000-fold less active than untreated LPS in causing Limulus amoebocyte lysate to gel (Seid & Sado#, 1981;Ding et al, 1990). These observations with deacylated LPS are similar to the lack of activation found in the P. clarkii proPO system by LPSdex reported here.…”

Section: Discussionsupporting

confidence: 77%

Phenoloxidase specific activity in the red swamp crayfishProcambarus clarkii

Cárdenas¹,

Dankert²

1997

Fish & Shellfish Immunology

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The prophenoloxidase (proPO) system is considered an important mechanism of innate defence in arthropods. This enzymatic cascade has been studied in crustaceans such as the crayfishes Astacus astacus and Pacifastacus leniusculus and is located inside the haemocytes. An initial characterisation of this system in the commercially important red swamp crayfish Procambarus clarkii is described. The P. clarkii proPO system was activated by trypsin and also by zymosan A. This activation was calcium ion dependent. The calcium ion concentration also a#ected the background activation of the system and at 5 mM was highest as measured by the ability of phenoloxidase to oxidise L-3,4-dihydroxyphenylalanine. The e#ect of calcium ions appears to be related to the activation of an endogenous serine protease, but other calcium ion-dependent factors can also a#ect proPO activation. Lipopolysaccharides (LPS), glycolipids found in the outer leaflet of the outer membrane of Gram-negative bacteria, were also able to activate the proPO system in P. clarkii after a significant lag time of 25 to 30 min. However, LPS derivatives (deacylated LPS, lipid A and -D-GlcNAc-[1<6]-D-GlcNAc) were not able to activate the enzymatic cascade in P. clarkii. Activation of the proPO system in other crayfishes by LPS has been shown to be mediated by serine protease-like enzymes. The observed e#ect of LPS and LPS derivatives on the activation of the P. clarkii proPO system suggests that a protease activity triggered by these molecules may be mediated through the recognition of a ''complete'' LPS molecule (polysaccharide and lipid A). The intermolecular recognition of LPS by a putative endogenous serine protease zymogen might explain the lag time observed in proPO activation. Academic Press Limited

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Section: Discussionsupporting

confidence: 77%

Phenoloxidase specific activity in the red swamp crayfishProcambarus clarkii

Cárdenas¹,

Dankert²

1997

Fish & Shellfish Immunology

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“…Detoxified LPS is generated by mild alkaline hydrolysis of LPS removing the fatty acid side chains from lipid A, which are responsible for the toxic activity of LPS (41). Previous reports have indicated that LPS molecules with various deacylated forms of lipid A are capable of antagonizing biological responses to intact LPS by interacting with host cells (42,43).…”

Section: Discussionmentioning

confidence: 99%

Bacterial Invasion Augments Epithelial Cytokine Responses to Escherichia coli Through a Lipopolysaccharide-Dependent Mechanism

Schilling

Mulvey

Vincent

et al. 2001

The Journal of Immunology

226

213

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One mechanism of initiating innate host defenses against uropathogenic Escherichia coli (UPEC) is the production of cytokines by bladder epithelial cells; however, the means by which these cells recognize bacterial pathogens is poorly understood. Type 1 pili, expressed by the majority of UPEC, have been shown to have a critical role in inducing the expression of IL-6 in bladder epithelial cells after exposure to E. coli. In this study, we demonstrate that type 1 pili are not sufficient to activate IL-6 production by bladder epithelial cells. Instead, it was shown that bacterial invasion mediated by type 1 pili augments bladder epithelial responses to E. coli via an LPS-dependent mechanism, leading to the production of IL-6. RNA transcripts for the LPSR Toll-like receptor 4 (TLR4) was detected in cultured bladder epithelial cells. The in vivo role of TLR4 was assessed using C3H/HeJ mice, which express a dominant negative form of TLR4. After infection with UPEC, C3H/HeJ mice have large foci of intracellular bacteria that persist within the bladder epithelium in the absence of any notable inflammatory response. These results indicate that LPS is required for bacterial invasion to enhance host responses to E. coli within the bladder.

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“…However, an ideal vaccine candidate should not be limited to these immunization routes. Moreover, a general reduction of endotoxicity to minimize adverse effects might be necessary for a safe application of the OMV vaccine candidate in humans, as highlighted by a variety of other vaccine candidates containing LPS (47)(48)(49)(50)(51)(52)(53)(54)(55). For example, the Neisseria meningitidis OMV vaccines, used to control outbreaks in Scandinavia and New Zealand, include an additional step to remove most of the LPS by detergent extraction (56,57).…”

mentioning

confidence: 99%

Lipopolysaccharide Modifications of a Cholera Vaccine Candidate Based on Outer Membrane Vesicles Reduce Endotoxicity and Reveal the Major Protective Antigen

et al. 2013

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The causative agent of the life-threatening gastrointestinal infectious disease cholera is the Gram-negative, facultative human pathogen Vibrio cholerae. We recently started to investigate the potential of outer membrane vesicles (OMVs) derived from V. cholerae as an alternative approach for a vaccine candidate against cholera and successfully demonstrated the induction of a long-lasting, high-titer, protective immune response upon immunization with OMVs using the mouse model. In this study, we present immunization data using lipopolysaccharide (LPS)-modified OMVs derived from V. cholerae, which allowed us to improve and identify the major protective antigen of the vaccine candidate. Our results indicate that reduction of endotoxicity can be achieved without diminishing the immunogenic potential of the vaccine candidate by genetic modification of lipid A. Although the protective potential of anti-LPS antibodies has been suggested many times, this is the first comprehensive study that uses defined LPS mutants to characterize the LPS-directed immune response of a cholera vaccine candidate in more detail. Our results pinpoint the O antigen to be the essential immunogenic structure and provide a protective mechanism based on inhibition of motility, which prevents a successful colonization. In a detailed analysis using defined antisera, we can demonstrate that only anti-O antigen antibodies, but not antibodies directed against the major flagellar subunit FlaA or the most abundant outer membrane protein, OmpU, are capable of effectively blocking the motility by binding to the sheathed flagellum and provide protection in a passive immunization assay.

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Protective immunity induced in mice by detoxified salmonella lipopolysaccharide

Cited by 37 publications

References 20 publications

Phenoloxidase specific activity in the red swamp crayfishProcambarus clarkii

Phenoloxidase specific activity in the red swamp crayfishProcambarus clarkii

Bacterial Invasion Augments Epithelial Cytokine Responses to Escherichia coli Through a Lipopolysaccharide-Dependent Mechanism

Lipopolysaccharide Modifications of a Cholera Vaccine Candidate Based on Outer Membrane Vesicles Reduce Endotoxicity and Reveal the Major Protective Antigen

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