Effects of a HP0859 (rfaD) knockout mutation on lipopolysaccharide structure of Helicobacter pylori 26695 and the bacterial adhesion on AGS cells

Chang, Po-Chun; Wang, Chun-Jen; You, Chung-Kai; Kao, Mou-Chieh

doi:10.1016/j.bbrc.2011.01.060

Cited by 23 publications

(35 citation statements)

References 21 publications

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“…In addition, the author found that the LPS of P. multocida significantly increased the number of bacteria adhering to the epithelium when this molecule was applied 30 minutes before or simultaneously with exposure to the microorganism. A similar effect has been described for the LPS of other Gram negative bacteria, such as Salmonella enterica [19] and Helicobacter pylori [20].…”

Section: Veterinary Medicine Internationalsupporting

confidence: 75%

Interaction ofBordetella bronchisepticaand Its Lipopolysaccharide withIn VitroCulture of Respiratory Nasal Epithelium

Gallego

Middleton

Martínez

et al. 2013

Veterinary Medicine International

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The nasal septa of fetal rabbits at 26 days of gestation were harvested by cesarean section of the does while under anesthesia and then exposed to Bordetella bronchiseptica or its lipopolysaccharide (LPS) for periods of 2 and 4 hours. A total of 240 explants were used. The tissues were examined using the Hematoxylin & Eosin technique. Then, semithin sections (0.5 μm) were stained with toluidine blue and examined with indirect immunoperoxidase (IPI) and lectin histochemistry. The most frequent and statistically significant findings were as follows: (1) cell death and increased goblet cell activity when exposed to bacteria and (2) cell death, cytoplasmic vacuolation and infiltration of polymorphonuclear leukocytes when exposed to LPS. The lesions induced by the bacterium were more severe than with LPS alone, except for the cytoplasmic vacuolation in epithelial cells. IPI stained the ciliated border of the epithelium with the bacterium more intensely, while LPS lectin histochemistry preferentially labeled the cytoplasm of goblet cell. These data indicate that B. bronchiseptica and its LPS may have an affinity for specific glycoproteins that would act as adhesion receptors in both locations.

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Section: Veterinary Medicine Internationalsupporting

confidence: 75%

Interaction ofBordetella bronchisepticaand Its Lipopolysaccharide withIn VitroCulture of Respiratory Nasal Epithelium

Gallego

Middleton

Martínez

et al. 2013

Veterinary Medicine International

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“…In addition, 3‐deoxy‐ d ‐manno‐octulosonic acid (Kdo) hydrolase genes (HP0579 and HP0580) were shown to affect the expression of O‐antigen Lewis epitopes [46]. Finally, an ADP‐ l ‐glycero‐ d ‐manno‐heptose‐6‐epimerase ortholog (HP0859) was characterized [47]. ΔHP0859 mutants exhibited severe truncation of LPS, decreased growth rate, higher susceptibility to novobiocin, and failed to induce the AGS elongation phenotype.…”

Section: Bacterial Factors and Induction Of Intracellular Signaling Pmentioning

confidence: 99%

Pathogenesis of Helicobacter pylori Infection

Backert

Clyne

2011

Helicobacter

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Helicobacter pylori infections and clinical outcome are dependent on sophisticated interactions between the bacteria and its host. Crucial bacterial factors associated with pathogenicity comprise a type IV secretion system encoded by the cag pathogenicity island, the effector protein CagA, the vacuolating cytotoxin (VacA), peptidoglycan, lipopolysaccharide (LPS), γ‐glutamyl transpeptidase (GGT), protease HtrA, and the adhesins BabA, SabA, and others. The high number of these factors and allelic variation of the involved genes generates a highly complex scenario and reveals the difficulties in testing the contribution of each individual factor. Much effort has been put into identifying the molecular mechanisms associated with H. pylori‐associated pathogenesis using human primary tissues, Mongolian gerbils, transgenic, knockout, and other mice as well as in vitro cell model systems. Interactions between bacterial factors and host signal transduction pathways seem to be critical for mediating the induction of pathogenic downstream processes and disease development. In this review article, we discuss the most recent progress in this research field.

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“…The donor of l - d -heptose is ADP- l - d -heptose, which is converted from ADP- d - d -heptose by enzyme ADP- l - glycero - d - manno -heptose-6-epimerase RfaD [19,20] (Figure 1a). ADP- d - d -heptose could not be efficiently consumed by WaaC [1,16,18,20,21]. Therefore, there are two ways to accumulate Kdo 2 -lipid A in vivo ; one is inactivating the gene, rfaC , encoding the enzyme, WaaC, and the other is inactivating the gene, rfaD , encoding the enzyme, RfaD (Figure 1b).…”

Section: Introductionmentioning

confidence: 99%

Construction and Characterization of an Escherichia coli Mutant Producing Kdo2-Lipid A

Wang

et al. 2014

Marine Drugs

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3-deoxy-d-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and it is believed to stimulate the innate immune system through the TLR4/MD2 complex. Therefore, Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Kdo2-lipid A has not been chemically synthesized to date and could only be isolated from an Escherichia coli mutant strain, WBB06. WBB06 cells grow slowly and have to grow in the presence of tetracycline. In this study, a novel E. coli mutant strain, WJW00, that could synthesize Kdo2-lipid A was constructed by deleting the rfaD gene from the genome of E. coli W3110. The rfaD gene encodes ADP-l-glycero-d-manno-heptose-6-epimerase RfaD. Based on the analysis by SDS-PAGE, thin layer chromatography (TLC) and electrospray ionization mass spectrometry (ESI/MS), WJW00 could produce similar levels of Kdo2-lipid A to WBB06. WJW00 cells grow much better than WBB06 cells and do not need to add any antibiotics during growth. Compared with the wild-type strain, W3110, WJW00 showed increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability. Therefore, WJW00 could be a more suitable strain than WBB06 for producing Kdo2-lipid A and a good base strain for developing lipid A adjuvants.

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Effects of a HP0859 (rfaD) knockout mutation on lipopolysaccharide structure of Helicobacter pylori 26695 and the bacterial adhesion on AGS cells

Cited by 23 publications

References 21 publications

Interaction ofBordetella bronchisepticaand Its Lipopolysaccharide withIn VitroCulture of Respiratory Nasal Epithelium

Interaction ofBordetella bronchisepticaand Its Lipopolysaccharide withIn VitroCulture of Respiratory Nasal Epithelium

Pathogenesis of Helicobacter pylori Infection

Construction and Characterization of an Escherichia coli Mutant Producing Kdo2-Lipid A

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