Recombinant 56-Kilodalton Major Outer Membrane Protein Antigen of
            <i>Orientia tsutsugamushi</i>
            Shanxi and Its Antigenicity

Chen, Weijun; Niu, Dongsheng; Zhang, Xueying; Chen, Mei‐Ling; Cui, Hong; Wan, Wei; Wen, Bin; Chen, Xiangrui

doi:10.1128/iai.71.8.4772-4779.2003

Cited by 29 publications

(23 citation statements)

References 18 publications

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“…Then protein expression was induced with 1 mM isopropylb-D-thiogalactopyranoside (IPTG) for an additional 3 h at 37°C. After growth, the recombinant bacteria were centrifuged at 5000 · g for 10 min and the recombinant antigen was purified from the insoluble inclusion bodies by affinity chromatography using a 10 mL HisBind resin column (Qiagen) according to the method of Chen et al (2003). An elution buffer (300 mM NaCl, 40 mM NaH 2 PO 4 , pH 8.0) containing 400 mM of imidazole was utilized to wash the His-tagged proteins from the resin column.…”

Section: Expression and Purification Of Recombinant B Schroederi Bs-mentioning

confidence: 99%

Sequence Analysis of theBs-Ag1Gene ofBaylisascaris schroederifrom the Giant Panda and an Evaluation of the Efficacy of a RecombinantBaylisascaris schroederi Bs-Ag1Antigen in Mice

Chen

Wang

et al. 2012

DNA and Cell Biology

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The Baylisascaris schroederi infection rate among wild giant pandas may reach over 50% or even 100%, making it one of the leading causes of death from primary or secondary infection in wild populations. Until now, little was known about how protective immunity to B. schroederi infection could be achieved. The present study was conducted to evaluate the immunogenicity and protective efficacy of recombinant Bs-Ag1 from B. schroederi, by cloning the full-length Bs-Ag1 gene of B. schroederi and expressing it in a heterologous host, Escherichia coli BL21. In mice vaccinated with rBs-Ag1 coupled with Freund's complete adjuvant (FCA), there was a significant reduction (69.2%) in the recovery of challenged B. schroederi L3 compared with either nonvaccinated controls or mice vaccinated with FCA alone. Our study supports the use of Bs-Ag1 as a potential candidate for vaccination against B. schroederi infection and provides basic data for further vaccination trials with mixtures of antigens (with Bs-Ag2 and Bs-Ag3) to B. schroederi.

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Section: Expression and Purification Of Recombinant B Schroederi Bs-mentioning

confidence: 99%

Sequence Analysis of theBs-Ag1Gene ofBaylisascaris schroederifrom the Giant Panda and an Evaluation of the Efficacy of a RecombinantBaylisascaris schroederi Bs-Ag1Antigen in Mice

Chen

Wang

et al. 2012

DNA and Cell Biology

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“…The result proves that the protein expressed is V. harveyi origin and antigenicity of the protein is maintained. Some recombinant OMP have been proved to have good antigenicity, e.g., in A. hydrophila, Orientia tsutsugamushi and Mannheimia haemolytica [24,27,28]. In the present study it is proved that recombinant OmpK also has good antigenicity in V. harveyi.…”

Section: Discussionmentioning

confidence: 53%

An outer membrane protein, OmpK, is an effective vaccine candidate for Vibrio harveyi in Orange-spotted grouper (Epinephelus coioides)

Li¹,

Bai²,

Shu-qin³

et al. 2008

Fish & Shellfish Immunology

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“…Isopropyl-beta-d-thiogalactopyranoside (IPTG) was then added at the final concentration of 1 mM and cells were incubated for a further 4 h at 37°C to induce recombinant SsTPx expression. The purity of the expressed protein was measured as previously described [29]. …”

Section: Methodsmentioning

confidence: 99%

Characterisation and analysis of thioredoxin peroxidase as a potential antigen for the serodiagnosis of sarcoptic mange in rabbits by dot-ELISA

Zhang

Zheng

et al. 2013

BMC Infect Dis

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BackgroundScabies caused by Sarcoptes scabiei is a widespread but a neglected tropical zoonosis. In this study, we characterised a S. scabiei thioredoxin peroxidase (SsTPx) and evaluated a recombinant SsTPx as a diagnostic antigen in rabbits.MethodsThe open reading frame of the gene encoding SsTPx-2 was amplified and the recombinant protein was expressed in Escherichia coli cells and purified. SsTPx was localized in mite tissue by immunolocalisation using the purified recombinant protein. Serodiagnosis assays were carried out in 203 New Zealand White rabbit serum samples by dot-ELISA.ResultThe open reading frame (489 bp) of the gene encodes an 18.11 kDa protein, which showed highly homology to that of Psoroptes cuniculi (98.77% identity) and belongs to the 2-Cys family of peroxiredoxins. SsTPx was mainly distributed in muscle tissues of mites, integument of the epidermis and the anterior end of S. scabiei. Although SsTPx cross-reactivity with psoroptic mites was observed, the SsTPx dot-ELISA showed excellent diagnostic ability, with 95.3% sensitivity and 93.8% specificity in mange-infected and uninfected groups.ConclusionsThis study showed that the purified SsTPx is a highly sensitive antigen for the diagnosis of mange infection by dot-ELISA. This technique is a rapid and convenient method that can be used worldwide for the clinical diagnosis of sarcoptic mange in rabbits, and is especially useful in developing regions.

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Recombinant 56-Kilodalton Major Outer Membrane Protein Antigen of Orientia tsutsugamushi Shanxi and Its Antigenicity

Cited by 29 publications

References 18 publications

Sequence Analysis of theBs-Ag1Gene ofBaylisascaris schroederifrom the Giant Panda and an Evaluation of the Efficacy of a RecombinantBaylisascaris schroederi Bs-Ag1Antigen in Mice

Sequence Analysis of theBs-Ag1Gene ofBaylisascaris schroederifrom the Giant Panda and an Evaluation of the Efficacy of a RecombinantBaylisascaris schroederi Bs-Ag1Antigen in Mice

An outer membrane protein, OmpK, is an effective vaccine candidate for Vibrio harveyi in Orange-spotted grouper (Epinephelus coioides)

Characterisation and analysis of thioredoxin peroxidase as a potential antigen for the serodiagnosis of sarcoptic mange in rabbits by dot-ELISA

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