免疫学期刊(英文)Pub Date : 2012-03-01Epub Date: 2011-12-30DOI: 10.4236/oji.2012.21004
Yu Qiao, Brian M Gray, Mohammed H Sofi, Laura D Bauler, Kathryn A Eaton, Mary X D O'Riordan, Cheong-Hee Chang
{"title":"Innate-like CD4 T cells selected by thymocytes suppress adaptive immune responses against bacterial infections.","authors":"Yu Qiao, Brian M Gray, Mohammed H Sofi, Laura D Bauler, Kathryn A Eaton, Mary X D O'Riordan, Cheong-Hee Chang","doi":"10.4236/oji.2012.21004","DOIUrl":"https://doi.org/10.4236/oji.2012.21004","url":null,"abstract":"<p><p>We have reported a new innate-like CD4 T cell population that expresses cell surface makers of effector/memory cells and produce Th1 and Th2 cytokines immediately upon activation. Unlike conventional CD4 T cells that are selected by thymic epithelial cells, these CD4 T cells, named T-CD4 T cells, are selected by MHC class II expressing thymocytes. Previously, we showed that the presence of T-CD4 T cells protected mice from airway inflammation suggesting an immune regulatory role of T-CD4 T cells. To further understand the function of T-CD4 T cells, we investigated immune responses mediated by T-CD4 T cells during bacterial infection because the generation of antigen specific CD4 T cells contributes to clearance of infection and for the development of immune memory. The current study shows a suppressive effect of T-CD4 T cells on both CD8 and CD4 T cell-mediated immune responses during Listeria and Helicobacter infections. In the mouse model of Listeria monocytogenes infection, T-CD4 T cells resulted in decreasedfrequency of Listeria-specific CD8 T cells and the killing activity of them. Furthermore, mice with T-CD4 T cells developed poor immune memory, demonstrated by reduced expansion of antigen-specific T cells and high bacterial burden upon re-infection. Similarly, the presence of T-CD4 T cells suppressed the generation of antigen-specific CD4 T cells in Helicobacter pylori infected mice. Thus, our studies reveal a novel function of T-CD4 T cells in suppressing anti-bacterial immunity.</p>","PeriodicalId":70343,"journal":{"name":"免疫学期刊(英文)","volume":"2 1","pages":"25-39"},"PeriodicalIF":0.0,"publicationDate":"2012-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3525959/pdf/nihms-427504.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31144952","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
免疫学期刊(英文)Pub Date : 2011-06-01Epub Date: 2011-06-30DOI: 10.4236/oji.2011.11001
Suely S Kashino, Antonio Campos-Neto
{"title":"Successful expression and purification of DPPD using a codon optimized synthetic gene.","authors":"Suely S Kashino, Antonio Campos-Neto","doi":"10.4236/oji.2011.11001","DOIUrl":"https://doi.org/10.4236/oji.2011.11001","url":null,"abstract":"<p><p>DPPD (Rv0061) is a difficult to express protein of Mycobacterium tuberculosis that elicits strong and specific delayed type hypersensitivity reactions in humans infected with M. tuberculosis. Therefore e DPPD is a molecule that can improve the specificity of the tuberculin skin test, which is widely used as an aid for the diagnosis of tuberculosis. However, a pitfall of our initial studies was that the DPPD molecule used to perform the skin tests was engineered as fusion molecule with another Mycobacterium protein. This approach was used because no expression of DPPD could be achieved either as a single molecule or as a fusion protein using a variety of commercially available expression systems. Here, we report the production and purification of rDPPD using a synthetic gene engineered to contain E. coli codon bias. The gene was cloned into pET14b expression vector, which was subsequently used to transform Rosetta 2(DE3) pLysS or BL-21(DE3)pLysS host cells. The recombinant protein was over-expressed after induction with IPTG and its purification was easily achieved at levels of 5 - 10 mg/l of bacterial broth cultures. The purified protein was confirmed to be DPPD by Mass Spectroscopy sequencing analysis. Moreover, purified rDPPD stimulated peripheral blood mononuclear cells of PPD positive blood donors to produce high levels of IFN-γ, thus confirming that this molecule is biologically active. Because of the DPPD gene is restricted to the tuberculosis-complex organisms of Mycobacterium genus, this highly purified molecule should be useful for the identification of individuals sensitized with tubercle bacilli.</p>","PeriodicalId":70343,"journal":{"name":"免疫学期刊(英文)","volume":"1 1","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"2011-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3527103/pdf/nihms377636.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31143920","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}