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#21859857   2011/10/14 Save this To Up

Ehrlichia chaffeensis TRP120 interacts with a diverse array of eukaryotic proteins involved in transcription, signaling, and cytoskeleton organization.

Ehrlichia chaffeensis is an obligately intracellular bacterium that exhibits tropism for mononuclear phagocytes and survives by evading host cell defense mechanisms. Recently, molecular interactions between E. chaffeensis 47-kDa tandem repeat (TR) protein (TRP47) and the eukaryotic host cell have been described. In this investigation, yeast (Saccharomyces cerevisiae) two-hybrid analysis demonstrated that E. chaffeensis-secreted tandem repeat protein 120 (TRP120) interacts with a diverse group of host cell proteins associated with major biological processes, including transcription and regulation, cell signaling, protein trafficking, and actin cytoskeleton organization. Twelve target proteins with the highest frequency of interaction with TRP120 were confirmed by cotransformation in yeast. Host targets, including human immunoglobulin lambda locus (IGL), cytochrome c oxidase subunit II (COX2), Golgi-associated gamma adaptin ear-containing ARF binding protein 1 (GGA1), polycomb group ring finger 5 (PCGF5), actin gamma 1 (ACTG1), and unc-13 homolog D (UNC13D; Caenorhabditis elegans), colocalized strongly with TRP120 in HeLa cells and with E. chaffeensis dense-cored morulae and areas adjacent to morulae in the host cytoplasm. The TR domain of TRP120 interacted only with PCGF5, indicating that distinct TRP120 domains contribute to specific host target interactions and that multiple domains are required to reconstitute TRP120 interactions with other host targets. Three previously defined molecular interactions between TRP47 and host proteins, PCGF5, IGLL1, and CAP1, were also associated with TRP120, demonstrating that molecular cross talk occurs between Ehrlichia TRPs and host targets. These findings further support the role of TRPs as effectors that reprogram the host cell.

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#20417300   2010/07/26 Save this To Up

Recombinant Mycobacterium bovis BCG expressing chimaeric protein of Ag85B and ESAT-6 enhances immunostimulatory activity of human macrophages.

Recombinant BCG strain that secretes the chimaeric protein of Ag85B and ESAT-6 has been demonstrated to augment Th1 immune response in C57BL/6 mice. In this paper, we studied the immunostimulatory activity of the recombinant BCG strains in vitro and found out that rBCG-A(N)-E-A(C) activated THP-1 cells and induced higher expression levels of CD86, CD80, CD40 and HLA-DR, especially increased the ratio of CD86/CD80. Likewise, rBCG-A(N)-E-A(C) infection was able to stimulate an increase in TNF-alpha production of macrophages. Moreover, rBCG-A(N)-E-A(C) up-regulated the expression of EFHD2, ACTB and ACTG1 in the macrophages and improved the ability of antigen presentation and the CD8(+) T-cells immune response. Taken together, this rBCG-A(N)-E-A(C) strain enhanced the immunostimulatory activity of human macrophages and could be a potential vaccine against Mycobacterium tuberculosis.

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