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  • 1
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    Modulation of Rab GTPase function by a protein phosphocholine transferase (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-08-09
    Description: The intracellular pathogen Legionella pneumophila modulates the activity of host GTPases to direct the transport and assembly of the membrane-bound compartment in which it resides. In vitro studies have indicated that the Legionella protein DrrA post-translationally modifies the GTPase Rab1 by a process called AMPylation. Here we used mass spectrometry to investigate post-translational modifications to Rab1 that occur during infection of host cells by Legionella. Consistent with in vitro studies, DrrA-mediated AMPylation of a conserved tyrosine residue in the switch II region of Rab1 was detected during infection. In addition, a modification to an adjacent serine residue in Rab1 was discovered, which was independent of DrrA. The Legionella effector protein AnkX was required for this modification. Biochemical studies determined that AnkX directly mediates the covalent attachment of a phosphocholine moiety to Rab1. This phosphocholine transferase activity used CDP-choline as a substrate and required a conserved histidine residue located in the FIC domain of the AnkX protein. During infection, AnkX modified both Rab1 and Rab35, which explains how this protein modulates membrane transport through both the endocytic and exocytic pathways of the host cell. Thus, phosphocholination of Rab GTPases represents a mechanism by which bacterial FIC-domain-containing proteins can alter host-cell functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3206611/" 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/PMC3206611/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mukherjee, Shaeri -- Liu, Xiaoyun -- Arasaki, Kohei -- McDonough, Justin -- Galan, Jorge E -- Roy, Craig R -- F32 AI082927/AI/NIAID NIH HHS/ -- R01 AI041699/AI/NIAID NIH HHS/ -- R01 AI041699-16/AI/NIAID NIH HHS/ -- R01 AI064559/AI/NIAID NIH HHS/ -- R01 AI064559-05/AI/NIAID NIH HHS/ -- R01-AI048770/AI/NIAID NIH HHS/ -- R01-AI064559/AI/NIAID NIH HHS/ -- U54-AI057158/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Aug 7;477(7362):103-6. doi: 10.1038/nature10335.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, New Haven, Connecticut, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21822290" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/*metabolism ; COS Cells ; Cercopithecus aethiops ; Diacylglycerol Cholinephosphotransferase/*metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; HEK293 Cells ; Host-Pathogen Interactions/*physiology ; Humans ; Legionella pneumophila/*enzymology ; Legionnaires' Disease/*enzymology/physiopathology ; Mass Spectrometry ; Protein Processing, Post-Translational ; rab GTP-Binding Proteins/*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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  • 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 sorting platform determines the order of protein secretion in bacterial type III systems (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-05
    Description: Bacterial type III protein secretion systems deliver effector proteins into eukaryotic cells in order to modulate cellular processes. Central to the function of these protein-delivery machines is their ability to recognize and secrete substrates in a defined order. Here, we describe a mechanism by which a type III secretion system from the bacterial enteropathogen Salmonella enterica serovar Typhimurium can sort its substrates before secretion. This mechanism involves a cytoplasmic sorting platform that is sequentially loaded with the appropriate secreted proteins. The sequential loading of this platform, facilitated by customized chaperones, ensures the hierarchy in type III protein secretion. Given the presence of these machines in many important pathogens, these findings can serve as the bases for the development of novel antimicrobial strategies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859126/" 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/PMC3859126/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lara-Tejero, Maria -- Kato, Junya -- Wagner, Samuel -- Liu, Xiaoyun -- Galan, Jorge E -- AI30492/AI/NIAID NIH HHS/ -- R01 AI030492/AI/NIAID NIH HHS/ -- U54 AI0157158/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2011 Mar 4;331(6021):1188-91. doi: 10.1126/science.1201476. Epub 2011 Feb 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section 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/21292939" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Bacterial/chemistry/metabolism ; Bacterial Proteins/chemistry/*metabolism ; Bacterial Secretion Systems/*physiology ; Cytoplasm/metabolism ; Membrane Proteins/chemistry/*metabolism ; Molecular Chaperones/chemistry/*metabolism ; Molecular Sequence Data ; Multiprotein Complexes/metabolism ; Mutation ; Protein Binding ; Protein Transport ; Salmonella typhimurium/genetics/*metabolism/*pathogenicity
    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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  • 4
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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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  • 5
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    The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-12-30
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 6
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    Proteolytic targeting of Rab29 by an effector protein distinguishes the intracellular compartments of human-adapted and broad-host Salmonella (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-10-31
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 7
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    Proteolytic targeting of Rab29 by an effector protein distinguishes the intracellular compartments of human-adapted and broad-host Salmonella [Microbiology] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-11-09
    Description: Unlike broad-host Salmonella serovars, which cause self-limiting disease, Salmonella enterica serovar Typhi can infect only humans causing typhoid fever, a life-threatening systemic disease. The molecular bases for these differences are presently unknown. Here we show that the GTPase Rab29 (Rab7L1) distinguishes the intracellular vacuole of human-adapted and broad-host Salmonella serovars. A screen to identify host factors required for the export of typhoid toxin, which is exclusively encoded by the human-specific Salmonella enterica serovars Typhi (S. Typhi) and Paratyphi (S. Paratyphi) identified Rab29. We found that Rab29 is recruited to the S. Typhi-containing vacuole but not to vacuoles containing broad-host Salmonella. We observed that in cells infected with broad-host Salmonella Rab29 is specifically cleaved by the proteolytic activity of GtgE, a unique type III secretion effector protein that is absent from S. Typhi. An S. Typhi strain engineered to express GtgE and therefore able to cleave Rab29 exhibited increased intracellular replication in human macrophages. These findings indicate significant differences in the intracellular biology of human-adapted and broad-host Salmonella and show how subtle differences in the assortment of effector proteins encoded by highly related pathogens can have a major impact in their biology.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 8
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    Inner rod function in type III secretion [Microbiology] (2014)
    National Academy of Sciences
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    Publication Date: 2014-01-15
    Description: Type III secretion machines are essential for the biology of many bacteria that are pathogenic or symbiotic for animals, plants, or insects. They exert their function by delivering bacterial effector proteins into target eukaryotic cells. The core component of these machines is the needle complex, a multiprotein structure that spans...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    Structure of membrane ATP microcompartments [Chemistry] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-08-01
    Description: The type of metabolic compartmentalization that occurs in red blood cells differs from the types that exist in most eukaryotic cells, such as intracellular organelles. In red blood cells (ghosts), ATP is sequestered within the cytoskeletal–membrane complex. These pools of ATP are known to directly fuel both the Na+/K+ and Ca2+ pumps. ATP can be entrapped within these pools either by incubation with bulk ATP or by operation of the phosphoglycerate kinase and pyruvate kinase reactions to enzymatically generate ATP. When the pool is filled with nascent ATP, metabolic labeling of the Na+/K+ or Ca2+ pump phosphoproteins (ENa-P and ECa-P, respectively) from bulk [γ-32P]-ATP is prevented until the pool is emptied by various means. Importantly, the pool also can be filled with the fluorescent ATP analog trinitrophenol ATP, as well as with a photoactivatable ATP analog, 8-azido-ATP (N3-ATP). Using the fluorescent ATP, we show that ATP accumulates and then disappears from the membrane as the ATP pools are filled and subsequently emptied, respectively. By loading N3-ATP into the membrane pool, we demonstrate that membrane proteins that contribute to the pool’s architecture can be photolabeled. With the aid of an antibody to N3-ATP, we identify these labeled proteins by immunoblotting and characterize their derived peptides by mass spectrometry. These analyses show that the specific peptides that corral the entrapped ATP derive from sequences within β-spectrin, ankyrin, band 3, and GAPDH.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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