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      Immunogenic evaluation of chimeric recombinant protein against ETEC, EHEC and Shigella

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          Abstract

          Diarrheal diseases still remain health problem worldwide and out of many bacteria responsible for, Shigella and pathogenic Escherichia cause the most diarrheas in the world. Shigellacause bacterial dysenteries and shigellosis through invasion where the most effective proteins for pathogenesis is Ipac. Critical virulence protein for ETEC infection is CFA/I with two subunits called cfab and cfae. . Attachment of EHEC is the main step of infection and the protein Intimin plays the key role in this function. Protection against the vast majority of responsible pathogens of diarrheas requires development of the combination vaccine against Shigella, ETEC and EHEC. In the present study, a multisubunitprotein (CII) containing immunologically significant parts of CfaB, IpaC and Intimin was designed. The chimeric gene (CII) was codon optimized and analyzed with different bioinformatic servers, then synthesized and expressed in E. coli. Mice, Guinea pig and, Caco-2 Cell line were used as challenge models for EHEC, shigella and ETEC respectively. The chimeric protein induced significant immune response and therefore could be a suitable vaccine candidate against these three pathogens.

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          Most cited references 40

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          Diarrhoea: why children are still dying and what can be done.

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            Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion.

            Shigella spp. are gram-negative pathogenic bacteria that evolved from harmless enterobacterial relatives and may cause devastating diarrhea upon ingestion. Research performed over the last 25 years revealed that a type III secretion system (T3SS) encoded on a large plasmid is a key virulence factor of Shigella flexneri. The T3SS determines the interactions of S. flexneri with intestinal cells by consecutively translocating two sets of effector proteins into the target cells. Thus, S. flexneri controls invasion into EC, intra- and intercellular spread, macrophage cell death, as well as host inflammatory responses. Some of the translocated effector proteins show novel biochemical activities by which they intercept host cell signal transduction pathways. An understanding of the molecular mechanisms underlying Shigella pathogenesis will foster the development of a safe and efficient vaccine, which, in parallel with improved hygiene, should curb infections by this widespread pathogen.
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              Design of the linkers which effectively separate domains of a bifunctional fusion protein.

               N Kamiya,  H Ueda,  R Arai (2001)
              With the aim of separating the domains of a bifunctional fusion protein, the ability of several lengths of helix-forming peptides to separate two weakly interacting beta-can domains was compared with that of flexible linkers or of a three alpha-helices bundle domain. We introduced helix-forming peptide linkers A(EAAAK)nA (n = 2-5) between two green fluorescent protein variants, EBFP and EGFP, and investigated their spectral properties. The fluorescence resonance energy transfer from EBFP to EGFP decreased as the length of the linkers increased. The circular dichroism spectra analysis suggested that the linkers form an alpha-helix and the alpha-helical contents increased as the length of the linkers increased. The results clearly suggested the ability of the helical linkers to control the distance and reduce the interference between the domains. This 'linker engineering' may open a way to the rational design of linkers which maximize the multiple functions of fusion proteins or de novo multi-domain proteins.
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                Author and article information

                Journal
                Mol Biol Res Commun
                Mol Biol Res Commun
                MBRC
                Molecular Biology Research Communications
                Shiraz University (Shiraz, Iran )
                2322-181X
                2345-2005
                September 2017
                : 6
                : 3
                : 101-112
                Affiliations
                [1 ]Department of Biology, Faculty of Basic Sciences, Shahed University, Tehran, Iran
                [2 ]Department of Biology, Faculty of Sciences, Imam Hossein University, Tehran, Iran
                [3 ]Applied Microbiology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
                Author notes
                [* ]Corresponding Author: Department of Biology, Faculty of Basic Sciences, Shahed University, Tehran, Iran Tel: +98- 21 51212600, Fax: +98- 21 51212601, E. mail: slmousavi@shahed.ac.ir
                Article
                10.22099/mbrc.2017.4081
                5640892

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License, ( http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                Categories
                Original Article

                chimeric vaccine, ipac, cfab, intimin

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