Chaperonin GroEL: A novel phylogenetically conserved protein with strong immunoreactivity of Avian Pathogenic Escherichia coli isolates from duck identified by immunoproteomics

Bao, Yinli; Zhai, Zhipeng; Wang, Shaohui; Ma, Jiale; Zhang, Wei; Lu, Chengping

doi:10.1016/j.vaccine.2013.04.042

Cited by 17 publications

(11 citation statements)

References 42 publications

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“…GroEL was described as a conserved and immunodominant protein in Brucella and avian pathogenic E. coli [ 52 , 53 ]. Besides its classical function as a chaperone, a role as adhesin- or invasin-mediating factor has been described for different pathogens such as Mollicutes , Salmonella Typhimurium, Mycobacterium bovis and E. coli [ 54 – 56 ].…”

Section: Discussionmentioning

confidence: 99%

Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

et al. 2015

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BackgroundEnteropathogenic Escherichia coli (EPEC) is distinguished mainly by the presence of EPEC adherence factor plasmid (pEAF) in typical EPEC (tEPEC) and its absence in atypical EPEC (aEPEC). The initial adherence to the intestinal mucosa is complex and mediated by adhesins other than bundle-forming pilus, which is not produced by aEPEC. Extracellular matrix (ECM) proteins of eukaryotic cells are commonly recognized by bacterial adhesins. Therefore, binding to ECM proteins may facilitate colonization, invasion and/or signaling by intestinal pathogens. Previous studies from our group demonstrated that aEPEC O26:H11 (strain BA2103) showed high binding activity to fibronectin, not shared by its counterpart, aEPEC O26:HNM.ResultsIn the present study, using mass spectrometry after fibronectin-associated immunoprecipitation, two proteins, flagellin (50 kDa) and GroEL (52 kDa), were identified and BA2103 binding ability to fibronectin was inhibited in the presence of anti-H11 and anti-GroEL sera, but not by either naïve rabbit or other unrelated sera. It was also observed that the presence of purified flagellin inhibits adhesion of BA2103 to cellular fibronectin in a dose-dependent manner. Additionally, BA2103 GroEL is similar to the same protein of uropathogenic E. coli.ConclusionsOur results suggest that flagellin may play a role in the in vitro interaction of BA2103 with cellular fibronectin, and GroEL can be an accessory protein in this process.Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-015-0612-4) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

et al. 2015

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“…It is well established that autophagy also functions as a protective mechanism for the clearance of intracellular pathogens through innate and adaptive immunity (Bao et al . ). During bacterial infection, lysosomes encapsulate bacteria that invade the host cell and destroy them (Huett et al .…”

Section: Introductionmentioning

confidence: 97%

“…S. Typhimurium is a facultative intracellular bacterium that can colonize host cells and escape from components of the host immune system. Autophagy is an important catabolic process by which a cell degrades unnecessary or dysfunctional components, such as misfolded proteins, denatured organelles and damaged nucleic acids (Bao et al 2013). Under various stress conditions, autophagy allows the orderly degradation and recycling of cellular components, maintaining cellular homeostasis (Lin et al 2011).…”

Section: Introductionmentioning

confidence: 99%

“…Under various stress conditions, autophagy allows the orderly degradation and recycling of cellular components, maintaining cellular homeostasis (Lin et al 2011). It is well established that autophagy also functions as a protective mechanism for the clearance of intracellular pathogens through innate and adaptive immunity (Bao et al 2013). During bacterial infection, lysosomes encapsulate bacteria that invade the host cell and destroy them (Huett et al 2009).…”

Section: Introductionmentioning

confidence: 99%

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Infection with sodA mutant of S. Typhimurium leads to up‐regulation of autophagy in Raw264·7 macrophages

Wang

Liu

Zhang

et al. 2019

Lett Appl Microbiol

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Salmonella enterica serovar Typhimurium (S. Typhimurium) inhabits a wide range of hosts, including poultry, and causes acute gastroenteritis in humans that may result in death. Superoxide dismutase (SOD) is an important antioxidant enzyme present in nearly all living cells exposed to oxygen. Recently, we reported the novel roles of SOD in serum resistance and biofilm formation in S. Typhimurium. This study was designed to explore the effect of infection with sodA mutant of S. Typhimurium on the autophagic response of macrophages. Murine macrophage cell line RAW264·7 was infected with wild‐type (LSM52), a sodA deletion mutant (LSM52ΔsodA) and complemented strain (LSM52CΔsodA). We found that sodA deletion triggered remarkable autophagic responses in infected cells, shown as higher concentrations of LC3‐II or Beclin‐1 than those infected with the wild‐type or complemented strain during the first hour post‐infection in S. Typhimurium. Consistent with these results, the number of viable bacteria in cells infected with the sodA mutant was significantly lower than those infected with wild‐type or complemented strains at 1 h, 2 h and 3 h post‐infection in S. Typhimurium. All results indicated that infection with sodA mutant of S. Typhimurium leads to up‐regulation of autophagy in Raw264·7 macrophages. Significance and Impact of the Study Autophagy plays an important role in Salmonella infection although the role of autophagy in Salmonella infection remains unclear. This study was designed to explore the effect of sodA on the autophagic response of macrophage. We found that infection with sodA mutant of Salmonella Typhimurium could lead to up‐regulation of autophagy in Raw264·7 macrophages.

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“…Thus, identification of S. agalactiae surface proteins associated with bacterial infection and a greater understanding of their roles in pathogenicity are required. The pre-absorbed immunoproteomics method (PAIM) was successfully established as a useful tool for identifying bacterial surface proteins in our previous study [12,13] and has been applied in Escherichia coli [14] and Campylobacter jejuni [15]. This technique involves the separation of proteins by two-dimensional electrophoresis (2-DE) and Western blotting with untreated (hyperimmune rabbit serum) and “pre-absorbed” serum, which is produced from untreated serum using a modified cross-absorption process to remove bacterial surface antigen-specific antibodies.…”

Section: Introductionmentioning

confidence: 99%

Identification of a virulence-related surface protein XF in piscine Streptococcus agalactiaeby pre-absorbed immunoproteomics

et al. 2014

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BackgroundSince 2009, large-scale Streptococcus agalactiae infections have broken out in cultured tilapia farms in China, resulting in considerable economic losses. Screening of the surface proteins is required to identify virulence factors or protective antigens involved in piscine S.agalactiae infections in tilapia. Pre-absorbed immunoproteomics method (PAIM) is a useful method previously established in our laboratory for identifying bacterial surface proteins.ResultsA serine-rich repeat protein family 1 (Srr-1), designated XF, was identified by PAIM in piscine S. agalactiae isolate GD201008-001. To investigate the role of XF in the pathogenesis of piscine S. agalactiae, an isogenic xf mutant strain (Δxf) and a complemented strain (CΔxf) were successfully constructed. The Δxf mutant and CΔxf showed no significant differences in growth characteristics and adherence to HEp-2 cells compared with the wild-type strain. However the 50% lethal dose of Δxf was increased (4-fold) compared with that of the parental strain in a zebrafish infection model.ConclusionsThe findings demonstrated that XF is a virulence-related, highly immunoreactive surface protein and is involved in the pathogenicity of S. agalactiae infections in fish.Electronic supplementary materialThe online version of this article (doi:10.1186/s12917-014-0259-7) contains supplementary material, which is available to authorized users.

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Chaperonin GroEL: A novel phylogenetically conserved protein with strong immunoreactivity of Avian Pathogenic Escherichia coli isolates from duck identified by immunoproteomics

Cited by 17 publications

References 42 publications

Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectin

Infection with sodA mutant of S. Typhimurium leads to up‐regulation of autophagy in Raw264·7 macrophages

Identification of a virulence-related surface protein XF in piscine Streptococcus agalactiaeby pre-absorbed immunoproteomics

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