Apolipoprotein A-I Exerts Bactericidal Activity against Yersinia enterocolitica Serotype O:3

Biedzka-Sarek, Marta; Metso, Jari; Kateifides, Andreas; Meri, Taru; Jokiranta, T. Sakari; Muszyński, Artur; Radziejewska‐Lebrecht, Joanna; Zannis, Vassilis I.; Skurnik, Mikael; Jauhiainen, Matti

doi:10.1074/jbc.m111.249482

Cited by 35 publications

(29 citation statements)

References 44 publications

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“…These results suggest that binding of ApoA-I is detrimental to pathogenesis of L. interrogans and that LruA contributes to pathogenesis by decreasing ApoA-I binding in the host. ApoA-I has been shown to exert a bactericidal effect in combination with complement on the Gramnegative bacterium Yersinia enterocolitica (25). The current study found no increase in serum sensitivity for the lruA mutants despite the higher ApoA-I binding observed for mutant M754, indicating that the loss of virulence in this strain is unlikely to be due to altered serum sensitivity.…”

Section: Discussioncontrasting

confidence: 35%

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Leptospiral LruA Is Required for Virulence and Modulates an Interaction with Mammalian Apolipoprotein AI

et al. 2013

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dLeptospirosis is a worldwide zoonosis caused by spirochetes of the genus Leptospira. While understanding of pathogenesis remains limited, the development of mutagenesis in Leptospira has provided a powerful tool for identifying novel virulence factors. LruA is a lipoprotein that has been implicated in leptospiral uveitis as a target of the immune response. In this study, two lruA mutants, M754 and M765, generated by transposon mutagenesis from Leptospira interrogans serovar Manilae, were characterized. In M754, the transposon inserted in the middle of lruA, resulting in no detectable expression of LruA. In M765

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Section: Discussioncontrasting

confidence: 35%

“…It has been reported that ApoA-I exerts a bactericidal effect on the Gram-negative bacterium Yersinia enterocolitica, potentiating killing by serum complement (25). As the lruA mutant M754 had altered levels of ApoA-I binding and M754, which bound more ApoA-I, was avirulent, the serum sensitivity of these strains was assessed.…”

Section: Resultsmentioning

confidence: 99%

Leptospiral LruA Is Required for Virulence and Modulates an Interaction with Mammalian Apolipoprotein AI

et al. 2013

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“…Nevertheless, pretreating with apoA-I and then washing it out still reduced the LPS-stimulated inflammatory response in multiple cell lines [15,16] . In addition, Marta et al have recently provided direct evidence that apoA-I does not directly interact with the bacteria [17] , suggesting that apoA-I-induced intercellular signaling may play a significant role in initiating its antiinflammatory function. We have previously reported that apoA-I inhibits the mRNA expression of various proinflammatory cytokines via activation of STAT3 and that apoA-I upregulates the cytokine mRNA-destabilizing protein tristetraprolin (TTP) in both THP-1 macrophages and human primary macrophages [18] .…”

Section: Introductionmentioning

confidence: 99%

Apolipoprotein A-I inhibits LPS-induced atherosclerosis in ApoE−/− mice possibly via activated STAT3-mediated upregulation of tristetraprolin

Yin

Tang

Tu³

et al. 2013

Acta Pharmacol Sin

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Aim: To investigate the effects of the major component of high-density lipoprotein apolipoprotein A-I (apoA-I) on the development of atherosclerosis in LPS-challenged ApoE -/-mice and the underlying mechanisms. Methods: Male ApoE-KO mice were daily injected with LPS (25 μg, sc) or PBS for 4 weeks. The LPS-challenged mice were intravenously injected with rAAV-apoA-I-GFP or rAAV-GFP. After the animals were killed, blood, livers and aortas were collected for biochemical and histological analyses. For ex vivo experiments, the abdominal cavity macrophages were harvested from each treatment group of mice, and cultured with autologous serum, then treated with LPS. Results: Chronic administration of LPS in ApoE -/-mice significantly increased the expression of inflammatory cytokines (TNF-α, IL-1β, IL-6, and MCP-1), increased infiltration of inflammatory cells, and enhanced the development of atherosclerosis. In LPS-challenged mice injected with rAAV-apoA-I-GFP, viral particles and human apoA-I were detected in the livers, total plasma human apoA-I levels were grammatically increased; HDL-cholesterol level was significantly increased, TG and TC were slightly increased. Furthermore, overexpression of apoA-I significantly suppressed the expression of proinflammatory cytokines, reduced the infiltration of inflammatory cells, and decreased the extent of atherosclerotic lesions. Moreover, overexpression of apoA-I significantly increased the expression of the cytokine mRNA-destabilizing protein tristetraprolin (TTP), and phosphorylation of JAK2 and STAT3 in aortas. In ex vivo mouse macrophages, the serum from mice overexpressing apoA-I significantly increased the expression of TTP, accompanied by accelerated decay of mRNAs of the inflammatory cytokines. Conclusion: ApoA-I potently suppresses LPS-induced atherosclerosis by inhibiting the inflammatory response possibly via activation of STAT3 and upregulation of TTP.

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“…Expression of the apoA-I[E223A/K226A] mutant in apoA-I Ϫ / Ϫ mice caused small alterations in the apoA-I structure and the HDL phenotype, suggesting that these residues also contribute to the effi cient formation of HDL. In addition to the drastic effect of the L218A/L219A/ V221A/L222A mutations on the biogenesis of HDL, the mutants also inhibited the ability of lipid-free apoA-I to promote transendothelial transport ( 20 ), as well as its bactericidal activity against Gram-negative bacteria ( 21 ), indicating the importance of the 218-222 residues for the functions of apoA-I.…”

Section: Abca1-dependent Cholesterol Effl Ux and Lcat Assays Abca1-mentioning

confidence: 99%

Role of the hydrophobic and charged residues in the 218–226 region of apoA-I in the biogenesis of HDL

Fotakis

Kateifides

Gkolfinopoulou

et al. 2013

Journal of Lipid Research

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Apolipoprotein A-I Exerts Bactericidal Activity against Yersinia enterocolitica Serotype O:3

Cited by 35 publications

References 44 publications

Leptospiral LruA Is Required for Virulence and Modulates an Interaction with Mammalian Apolipoprotein AI

Leptospiral LruA Is Required for Virulence and Modulates an Interaction with Mammalian Apolipoprotein AI

Apolipoprotein A-I inhibits LPS-induced atherosclerosis in ApoE−/− mice possibly via activated STAT3-mediated upregulation of tristetraprolin

Role of the hydrophobic and charged residues in the 218–226 region of apoA-I in the biogenesis of HDL

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