Differential
            <i>In Vivo</i>
            Gene Expression of Major Leptospira Proteins in Resistant or Susceptible Animal Models

Matsui, Mariko; Soupé, Marie-Estelle; Bécam, Jérôme; Goarant, Cyrille

doi:10.1128/aem.00911-12

Cited by 28 publications

(27 citation statements)

References 21 publications

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“…Their results indicated that the lipl32 expression in hamsters was significantly higher than in mice. 20 This result may correlate with the present data in which the responses of hamster LipL32 -specific CD4 + T cells were higher than those of the mouse model. Although the response of hamster CD4 + T cells was dramatically increased in in vitro re-stimulation with rLipL32, lower levels of IFN-γ and IL-4 producing CD4 + T cells were detected.…”

Section: Discussionsupporting

confidence: 82%

Hamster IFN-γ+CD4+ and IL-4+CD4+ T cell responses against leptospires are significantly higher than those of mice

Nakornpakdee

Sermswan

Maneewatchararangsri

et al. 2018

Asian Pac J Allergy Immunol

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Section: Discussionsupporting

confidence: 82%

Hamster IFN-γ+CD4+ and IL-4+CD4+ T cell responses against leptospires are significantly higher than those of mice

Nakornpakdee

Sermswan

Maneewatchararangsri

et al. 2018

Asian Pac J Allergy Immunol

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“…Levels of lipL41 transcript (Matsui et al, 2012) and LipL41 protein (Cullen et al, 2002; Nally et al, 2001b) are remarkably unaffected by temperature, osmolarity and other environmental factors. The stability of LipL41 expression is useful as a control when studying the effects of growth conditions on the expression of other genes and proteins.…”

Section: Outer Membrane Proteins (Omps)mentioning

confidence: 99%

The Leptospiral Outer Membrane

Haake

Zückert

2014

Current Topics in Microbiology and Immunology

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The outer membrane (OM) is the front line of leptospiral interactions with their environment and the mammalian host. Unlike most invasive spirochetes, pathogenic leptospires must be able survive in both free-living and host-adapted states. As organisms move from one set of environmental conditions to another, the OM must cope with a series of conflicting challenges. For example, the OM must be porous enough to allow nutrient uptake, yet robust enough to defend the cell against noxious substances. In the host, the OM presents a surface decorated with adhesins and receptors for attaching to, and acquiring, desirable host molecules such as the complement regulator, Factor H. On the other hand, the OM must enable leptospires to evade detection by the host’s immune system on their way from sites of invasion through the bloodstream to the protected niche of the proximal tubule. The picture that is emerging of the leptospiral OM is that, while it shares many of the characteristics of the OMs of spirochetes and Gram-negative bacteria, it is also unique and different in ways that make it of general interest to microbiologists. For example, unlike most other pathogenic spirochetes, the leptospiral OM is rich in lipopolysaccharide (LPS). Leptospiral LPS is similar to that of Gram-negative bacteria but has a number of unique structural features that may explain why it is not recognized by the LPS-specific Toll-like receptor 4 of humans. As in other spirochetes, lipoproteins are major components of the leptospiral OM, though their roles are poorly understood. The functions of transmembrane OMPs in many cases are better understood thanks to homologies with their Gram-negative counterparts and the emergence of improved genetic techniques. This chapter will review recent discoveries involving the leptospiral OM and its role in leptospiral physiology and pathogenesis. Readers are referred to earlier, excellent summaries related to this subject (Adler and de la Peña Moctezuma, 2010; Cullen et al., 2004; Haake, 2000; Haake and Matsunaga, 2010; Ko et al., 2009; Raja and Natarajaseenivasan, 2013; Zuerner et al., 2000).

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“…The gene transcript 528 ZENG ET AL. levels were normalized to the level of L. interrogans 16S, as described previously (Matsui et al, 2012).…”

Section: Rna Extraction and Real-time Pcr Detectionmentioning

confidence: 99%

Extracellular Proteome Analysis ofLeptospira interrogansserovar Lai

Zeng

Zhang

Zhu

et al. 2013

OMICS: A Journal of Integrative Biology

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Leptospirosis is one of the most important zoonoses. Leptospira interrogans serovar Lai is a pathogenic spirochete that is responsible for leptospirosis. Extracellular proteins play an important role in the pathogenicity of this bacterium. In this study, L. interrogans serovar Lai was grown in protein-free medium; the supernatant was collected and subsequently analyzed as the extracellular proteome. A total of 66 proteins with more than two unique peptides were detected by MS/MS, and 33 of these were predicted to be extracellular proteins by a combination of bioinformatics analyses, including Psortb, cello, SoSuiGramN and SignalP. Comparisons of the transcriptional levels of these 33 genes between in vivo and in vitro conditions revealed that 15 genes were upregulated and two genes were downregulated in vivo compared to in vitro. A BLAST search for the components of secretion system at the genomic and proteomic levels revealed the presence of the complete type I secretion system and type II secretion system in this strain. Moreover, this strain also exhibits complete Sec translocase and Tat translocase systems. The extracellular proteome analysis of L. interrogans will supplement the previously generated whole proteome data and provide more information for studying the functions of specific proteins in the infection process and for selecting candidate molecules for vaccines or diagnostic tools for leptospirosis.

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Differential In Vivo Gene Expression of Major Leptospira Proteins in Resistant or Susceptible Animal Models

Cited by 28 publications

References 21 publications

Hamster IFN-γ+CD4+ and IL-4+CD4+ T cell responses against leptospires are significantly higher than those of mice

Hamster IFN-γ+CD4+ and IL-4+CD4+ T cell responses against leptospires are significantly higher than those of mice

The Leptospiral Outer Membrane

Extracellular Proteome Analysis ofLeptospira interrogansserovar Lai

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