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  • 1
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    Delivery of epitopes by the Salmonella type III secretion system for vaccine development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-24
    Description: Avirulent strains of Salmonella typhimurium are being considered as antigen delivery vectors. During its intracellular stage in the host, S. typhimurium resides within a membrane-bound compartment and is not an efficient inducer of class I-restricted immune responses. Viral epitopes were successfully delivered to the host-cell cytosol by using the type III protein secretion system of S. typhimurium. This resulted in class I-restricted immune responses that protected vaccinated animals against lethal infection. This approach may allow the efficient use of S. typhimurium as an antigen delivery system to control infections by pathogens that require this type of immune response for protection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russmann, H -- Shams, H -- Poblete, F -- Fu, Y -- Galan, J E -- Donis, R O -- New York, N.Y. -- Science. 1998 Jul 24;281(5376):565-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, School of Medicine, State University of New York at Stony Brook, Stony Brook, NY 11794-5222, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9677200" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigens, Viral/immunology/metabolism ; Bacterial Proteins/genetics/*metabolism ; Cytosol/*immunology ; Endoplasmic Reticulum/immunology/metabolism ; Epitopes/*immunology ; Histocompatibility Antigens Class I/immunology ; Hybridomas ; Lymphocytic Choriomeningitis/prevention & control ; Lymphocytic choriomeningitis virus/immunology ; Mice ; Mice, Inbred C57BL ; Nucleoproteins/immunology/metabolism ; Peptide Fragments/immunology/metabolism ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Recombinant Fusion Proteins/immunology/metabolism ; *Salmonella typhimurium/metabolism/pathogenicity ; T-Lymphocytes/immunology ; T-Lymphocytes, Cytotoxic/immunology ; Tumor Cells, Cultured ; Vaccines, Synthetic/*administration & dosage/immunology ; Viral Core Proteins/immunology/metabolism ; Viral Vaccines/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Structure and function of the Salmonella Typhi chimaeric A(2)B(5) typhoid toxin (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-07-12
    Description: Salmonella enterica serovar Typhi (S. Typhi) differs from most other salmonellae in that it causes a life-threatening systemic infection known as typhoid fever. The molecular bases for its unique clinical presentation are unknown. Here we find that the systemic administration of typhoid toxin, a unique virulence factor of S. Typhi, reproduces many of the acute symptoms of typhoid fever in an animal model. We identify specific carbohydrate moieties on specific surface glycoproteins that serve as receptors for typhoid toxin, which explains its broad cell target specificity. We present the atomic structure of typhoid toxin, which shows an unprecedented A2B5 organization with two covalently linked A subunits non-covalently associated to a pentameric B subunit. The structure provides insight into the toxin's receptor-binding specificity and delivery mechanisms and reveals how the activities of two powerful toxins have been co-opted into a single, unique toxin that can induce many of the symptoms characteristic of typhoid fever. These findings may lead to the development of potentially life-saving therapeutics against typhoid fever.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4144355/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4144355/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, Jeongmin -- Gao, Xiang -- Galan, Jorge E -- AI079022/AI/NIAID NIH HHS/ -- GM098791/GM/NIGMS NIH HHS/ -- R01 AI114618/AI/NIAID NIH HHS/ -- R24 GM098791/GM/NIGMS NIH HHS/ -- U54-AI057158/AI/NIAID NIH HHS/ -- England -- Nature. 2013 Jul 18;499(7458):350-4. doi: 10.1038/nature12377. Epub 2013 Jul 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23842500" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Endotoxins/*chemistry/metabolism/toxicity ; Membrane Glycoproteins/metabolism ; Mice ; Models, Molecular ; Molecular Sequence Data ; Protein Subunits/chemistry/metabolism ; Salmonella typhi/*pathogenicity ; Sialoglycoproteins/chemistry ; Structure-Activity Relationship ; Typhoid Fever/microbiology ; Virulence Factors/*chemistry/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    A Rab32-dependent pathway contributes to Salmonella typhi host restriction (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-11-20
    Description: Unlike other Salmonellae, the intracellular bacterial human pathogen Salmonella Typhi exhibits strict host specificity. The molecular bases for this restriction are unknown. Here we found that the expression of a single type III secretion system effector protein from broad-host Salmonella Typhimurium allowed Salmonella Typhi to survive and replicate within macrophages and tissues from mice, a nonpermissive host. This effector proteolytically targeted Rab32, which controls traffic to lysosome-related organelles in conjunction with components of the biogenesis of lysosome-related organelle complexes (BLOCs). RNA interference-mediated depletion of Rab32 or of an essential component of a BLOC complex was sufficient to allow S. Typhi to survive within mouse macrophages. Furthermore, S. Typhi was able to survive in macrophages from mice defective in BLOC components.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3693731/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3693731/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spano, Stefania -- Galan, Jorge E -- AI055472/AI/NIAID NIH HHS/ -- AI079022/AI/NIAID NIH HHS/ -- R01 AI055472/AI/NIAID NIH HHS/ -- R01 AI079022/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 16;338(6109):960-3. doi: 10.1126/science.1229224.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbial Pathogenesis, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23162001" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Secretion Systems/genetics/*physiology ; COS Cells ; Cercopithecus aethiops ; *Host-Pathogen Interactions ; Humans ; Lysosomes/metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Phylogeny ; RNA Interference ; Salmonella typhi/genetics/*physiology ; rab GTP-Binding Proteins/classification/genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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