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Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus
Effectors translocated into the host cell by Salmonella enterica serovar Typhimurium are critical for bacterial virulence. For many effectors, the mechanisms of their interactions with host pathways are not yet understood. We have recently found an interaction between the SPI-2 effector SseL and oxy...
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| Published in: | Microbes and infection 2012-02, Vol.14 (2), p.148-154 |
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| Main Authors: | , , , , |
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| cited_by | cdi_FETCH-LOGICAL-c391t-a05bc835b236fafa908c5696d44d50061e2f6a2d260222b74f6d541efa4114733 |
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| cites | cdi_FETCH-LOGICAL-c391t-a05bc835b236fafa908c5696d44d50061e2f6a2d260222b74f6d541efa4114733 |
| container_end_page | 154 |
| container_issue | 2 |
| container_start_page | 148 |
| container_title | Microbes and infection |
| container_volume | 14 |
| creator | Auweter, Sigrid D. Yu, Hong B. Arena, Ellen T. Guttman, Julian A. Finlay, B. Brett |
| description | Effectors translocated into the host cell by
Salmonella enterica serovar Typhimurium are critical for bacterial virulence. For many effectors, the mechanisms of their interactions with host pathways are not yet understood. We have recently found an interaction between the SPI-2 effector SseL and oxysterol-binding protein (OSBP). We show here that SseL binds the N-terminus of OSBP and that
S. Typhimurium infection results in redistribution of OSBP. We furthermore demonstrate that OSBP is required for efficient replication of intracellular
S. Typhimurium. This suggests that
S. Typhimurium hijacks OSBP-dependent pathways to benefit its intracellular life-style, possibly by SseL- and OSBP-mediated manipulation of host lipid metabolism. |
| doi_str_mv | 10.1016/j.micinf.2011.09.003 |
| format | article |
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Salmonella enterica serovar Typhimurium are critical for bacterial virulence. For many effectors, the mechanisms of their interactions with host pathways are not yet understood. We have recently found an interaction between the SPI-2 effector SseL and oxysterol-binding protein (OSBP). We show here that SseL binds the N-terminus of OSBP and that
S. Typhimurium infection results in redistribution of OSBP. We furthermore demonstrate that OSBP is required for efficient replication of intracellular
S. Typhimurium. This suggests that
S. Typhimurium hijacks OSBP-dependent pathways to benefit its intracellular life-style, possibly by SseL- and OSBP-mediated manipulation of host lipid metabolism.</description><identifier>ISSN: 1286-4579</identifier><identifier>EISSN: 1769-714X</identifier><identifier>DOI: 10.1016/j.micinf.2011.09.003</identifier><identifier>PMID: 21988961</identifier><language>eng</language><publisher>Kidlington: Elsevier Masson SAS</publisher><subject>Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Cell Line ; DNA, Complementary - genetics ; Endopeptidases - genetics ; Endopeptidases - metabolism ; Epithelial Cells - microbiology ; Female ; Fundamental and applied biological sciences. Psychology ; HeLa Cells ; Host-Pathogen Interactions ; Humans ; Intracellular Space - microbiology ; Membrane Proteins - metabolism ; Microbiology ; Miscellaneous ; OSBP ; Oxysterol-binding protein ; Protein Binding ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Protein Transport ; Receptors, Steroid - metabolism ; Salmonella enterica serovar Typhimurium ; Salmonella Infections - microbiology ; Salmonella typhimurium - pathogenicity ; Salmonella typhimurium - physiology ; SPI-2 ; SseL ; Type three secretion</subject><ispartof>Microbes and infection, 2012-02, Vol.14 (2), p.148-154</ispartof><rights>2011 Institut Pasteur</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-a05bc835b236fafa908c5696d44d50061e2f6a2d260222b74f6d541efa4114733</citedby><cites>FETCH-LOGICAL-c391t-a05bc835b236fafa908c5696d44d50061e2f6a2d260222b74f6d541efa4114733</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25466652$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21988961$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Auweter, Sigrid D.</creatorcontrib><creatorcontrib>Yu, Hong B.</creatorcontrib><creatorcontrib>Arena, Ellen T.</creatorcontrib><creatorcontrib>Guttman, Julian A.</creatorcontrib><creatorcontrib>Finlay, B. Brett</creatorcontrib><title>Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus</title><title>Microbes and infection</title><addtitle>Microbes Infect</addtitle><description>Effectors translocated into the host cell by
Salmonella enterica serovar Typhimurium are critical for bacterial virulence. For many effectors, the mechanisms of their interactions with host pathways are not yet understood. We have recently found an interaction between the SPI-2 effector SseL and oxysterol-binding protein (OSBP). We show here that SseL binds the N-terminus of OSBP and that
S. Typhimurium infection results in redistribution of OSBP. We furthermore demonstrate that OSBP is required for efficient replication of intracellular
S. Typhimurium. This suggests that
S. Typhimurium hijacks OSBP-dependent pathways to benefit its intracellular life-style, possibly by SseL- and OSBP-mediated manipulation of host lipid metabolism.</description><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>DNA, Complementary - genetics</subject><subject>Endopeptidases - genetics</subject><subject>Endopeptidases - metabolism</subject><subject>Epithelial Cells - microbiology</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HeLa Cells</subject><subject>Host-Pathogen Interactions</subject><subject>Humans</subject><subject>Intracellular Space - microbiology</subject><subject>Membrane Proteins - metabolism</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>OSBP</subject><subject>Oxysterol-binding protein</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Receptors, Steroid - metabolism</subject><subject>Salmonella enterica serovar Typhimurium</subject><subject>Salmonella Infections - microbiology</subject><subject>Salmonella typhimurium - pathogenicity</subject><subject>Salmonella typhimurium - physiology</subject><subject>SPI-2</subject><subject>SseL</subject><subject>Type three secretion</subject><issn>1286-4579</issn><issn>1769-714X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNp9kctu1DAYhS0EoqXwBgh5gyiLBNvxJd4gQcWl0oipNCCxsxznN_UocaZ2UrWPwRvj0QyXFSvb8nf-yzkIPaekpoTKN9t6DC5EXzNCaU10TUjzAJ1SJXWlKP_-sNxZKysulD5BT3LeEkKFkvwxOmFUt62W9BT9XN_d5xnSNFRdiH2IP_AuTTOEiM_Xm_dXrzHEaxsdZJxgNwRn5zBFPHkc4pysg2FYBpvwxg7jFMvLYht7vK-V8XwN_35sri4rhsF7cPNUJBlW-DZYHOaMv1RliDHEJT9Fj7wdMjw7nmfo28cPXy8-V6v1p8uLd6vKNZrOlSWic20jOtZIb73VpHVCatlz3gtCJAXmpWU9k4Qx1inuZS84BW85pVw1zRl6dahb9r1ZIM9mDHm_j40wLdloqoRSRVJIfiBdmnJO4M0uhdGme0OJ2WdhtuaQhdlnYYg2JYsie3FssHQj9H9Ev80vwMsjYLOzg0_F55D_coJLKQUr3NsDB8WO2wDJZBegZNKHVKw0_RT-P8kvzRKqXQ</recordid><startdate>20120201</startdate><enddate>20120201</enddate><creator>Auweter, Sigrid D.</creator><creator>Yu, Hong B.</creator><creator>Arena, Ellen T.</creator><creator>Guttman, Julian A.</creator><creator>Finlay, B. 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Brett</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-a05bc835b236fafa908c5696d44d50061e2f6a2d260222b74f6d541efa4114733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>DNA, Complementary - genetics</topic><topic>Endopeptidases - genetics</topic><topic>Endopeptidases - metabolism</topic><topic>Epithelial Cells - microbiology</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HeLa Cells</topic><topic>Host-Pathogen Interactions</topic><topic>Humans</topic><topic>Intracellular Space - microbiology</topic><topic>Membrane Proteins - metabolism</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>OSBP</topic><topic>Oxysterol-binding protein</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>Receptors, Steroid - metabolism</topic><topic>Salmonella enterica serovar Typhimurium</topic><topic>Salmonella Infections - microbiology</topic><topic>Salmonella typhimurium - pathogenicity</topic><topic>Salmonella typhimurium - physiology</topic><topic>SPI-2</topic><topic>SseL</topic><topic>Type three secretion</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Auweter, Sigrid D.</creatorcontrib><creatorcontrib>Yu, Hong B.</creatorcontrib><creatorcontrib>Arena, Ellen T.</creatorcontrib><creatorcontrib>Guttman, Julian A.</creatorcontrib><creatorcontrib>Finlay, B. 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Brett</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus</atitle><jtitle>Microbes and infection</jtitle><addtitle>Microbes Infect</addtitle><date>2012-02-01</date><risdate>2012</risdate><volume>14</volume><issue>2</issue><spage>148</spage><epage>154</epage><pages>148-154</pages><issn>1286-4579</issn><eissn>1769-714X</eissn><abstract>Effectors translocated into the host cell by
Salmonella enterica serovar Typhimurium are critical for bacterial virulence. For many effectors, the mechanisms of their interactions with host pathways are not yet understood. We have recently found an interaction between the SPI-2 effector SseL and oxysterol-binding protein (OSBP). We show here that SseL binds the N-terminus of OSBP and that
S. Typhimurium infection results in redistribution of OSBP. We furthermore demonstrate that OSBP is required for efficient replication of intracellular
S. Typhimurium. This suggests that
S. Typhimurium hijacks OSBP-dependent pathways to benefit its intracellular life-style, possibly by SseL- and OSBP-mediated manipulation of host lipid metabolism.</abstract><cop>Kidlington</cop><pub>Elsevier Masson SAS</pub><pmid>21988961</pmid><doi>10.1016/j.micinf.2011.09.003</doi><tpages>7</tpages></addata></record> |
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| ispartof | Microbes and infection, 2012-02, Vol.14 (2), p.148-154 |
| issn | 1286-4579 1769-714X |
| language | eng |
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| source | ScienceDirect Freedom Collection 2022-2024 |
| subjects | Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Cell Line DNA, Complementary - genetics Endopeptidases - genetics Endopeptidases - metabolism Epithelial Cells - microbiology Female Fundamental and applied biological sciences. Psychology HeLa Cells Host-Pathogen Interactions Humans Intracellular Space - microbiology Membrane Proteins - metabolism Microbiology Miscellaneous OSBP Oxysterol-binding protein Protein Binding Protein Interaction Mapping Protein Structure, Tertiary Protein Transport Receptors, Steroid - metabolism Salmonella enterica serovar Typhimurium Salmonella Infections - microbiology Salmonella typhimurium - pathogenicity Salmonella typhimurium - physiology SPI-2 SseL Type three secretion |
| title | Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus |
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