Characterization of the Protein Tyrosine Phosphatase LmPRL-1 Secreted by Leishmania major via the Exosome Pathway
Similar to other intracellular pathogens, parasites are known to evade the antimicrobial effector functions of host immune cells. To date, however, only a few virulence factors have been described for , one of the causative agents of cutaneous leishmaniasis. Here, we have characterized the expressio...
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| Veröffentlicht in: | Infection and immunity 2017-08, Vol.85 (8) |
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| container_title | Infection and immunity |
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| creator | Leitherer, Sabine Clos, Joachim Liebler-Tenorio, Elisabeth M Schleicher, Ulrike Bogdan, Christian Soulat, Didier |
| description | Similar to other intracellular pathogens,
parasites are known to evade the antimicrobial effector functions of host immune cells. To date, however, only a few virulence factors have been described for
, one of the causative agents of cutaneous leishmaniasis. Here, we have characterized the expression and function of an
phosphatase, which we termed LmPRL-1. This enzyme shows a strong structural similarity to the human phosphatases of regenerating liver (PRL-1, -2, and -3) that regulate the proliferation, differentiation, and motility of cells. The biochemical characterization of the
phosphatase revealed that the enzyme is redox sensitive. When analyzing the subcellular localization of LmPRL-1 in promastigotes, amastigotes, and infected macrophages, we found that the phosphatase was predominantly expressed and secreted by promastigotes via the exosome route. Finally, we observed that ectopic expression of LmPRL-1 in
led to an increased number of parasites in macrophages. From these data, we conclude that the
phosphatase LmPRL-1 contributes to the intracellular survival of the parasites in macrophages. |
| doi_str_mv | 10.1128/IAI.00084-17 |
| format | Article |
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parasites are known to evade the antimicrobial effector functions of host immune cells. To date, however, only a few virulence factors have been described for
, one of the causative agents of cutaneous leishmaniasis. Here, we have characterized the expression and function of an
phosphatase, which we termed LmPRL-1. This enzyme shows a strong structural similarity to the human phosphatases of regenerating liver (PRL-1, -2, and -3) that regulate the proliferation, differentiation, and motility of cells. The biochemical characterization of the
phosphatase revealed that the enzyme is redox sensitive. When analyzing the subcellular localization of LmPRL-1 in promastigotes, amastigotes, and infected macrophages, we found that the phosphatase was predominantly expressed and secreted by promastigotes via the exosome route. Finally, we observed that ectopic expression of LmPRL-1 in
led to an increased number of parasites in macrophages. From these data, we conclude that the
phosphatase LmPRL-1 contributes to the intracellular survival of the parasites in macrophages.</description><identifier>ISSN: 0019-9567</identifier><identifier>EISSN: 1098-5522</identifier><identifier>DOI: 10.1128/IAI.00084-17</identifier><identifier>PMID: 28507071</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Animals ; Biological Transport ; Cell Cycle Proteins - chemistry ; Exosomes - metabolism ; Fungal and Parasitic Infections ; Humans ; Kinetics ; Leishmania major - enzymology ; Leishmania major - genetics ; Macrophages - parasitology ; Membrane Proteins - chemistry ; Mice ; Neoplasm Proteins - chemistry ; Oxidation-Reduction ; Phylogeny ; Protein Tyrosine Phosphatases - chemistry ; Protein Tyrosine Phosphatases - genetics ; Protein Tyrosine Phosphatases - metabolism ; Virulence ; Virulence Factors</subject><ispartof>Infection and immunity, 2017-08, Vol.85 (8)</ispartof><rights>Copyright © 2017 American Society for Microbiology.</rights><rights>Copyright © 2017 American Society for Microbiology. 2017 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c384t-69e92ae896927c055cebce41ffc43d0b712d26d8463336a2faba38ef2376d49d3</citedby><cites>FETCH-LOGICAL-c384t-69e92ae896927c055cebce41ffc43d0b712d26d8463336a2faba38ef2376d49d3</cites><orcidid>0000-0002-2300-0631 ; 0000-0002-3688-5846</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5520432/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5520432/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,3188,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28507071$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Adams, John H.</contributor><creatorcontrib>Leitherer, Sabine</creatorcontrib><creatorcontrib>Clos, Joachim</creatorcontrib><creatorcontrib>Liebler-Tenorio, Elisabeth M</creatorcontrib><creatorcontrib>Schleicher, Ulrike</creatorcontrib><creatorcontrib>Bogdan, Christian</creatorcontrib><creatorcontrib>Soulat, Didier</creatorcontrib><title>Characterization of the Protein Tyrosine Phosphatase LmPRL-1 Secreted by Leishmania major via the Exosome Pathway</title><title>Infection and immunity</title><addtitle>Infect Immun</addtitle><description>Similar to other intracellular pathogens,
parasites are known to evade the antimicrobial effector functions of host immune cells. To date, however, only a few virulence factors have been described for
, one of the causative agents of cutaneous leishmaniasis. Here, we have characterized the expression and function of an
phosphatase, which we termed LmPRL-1. This enzyme shows a strong structural similarity to the human phosphatases of regenerating liver (PRL-1, -2, and -3) that regulate the proliferation, differentiation, and motility of cells. The biochemical characterization of the
phosphatase revealed that the enzyme is redox sensitive. When analyzing the subcellular localization of LmPRL-1 in promastigotes, amastigotes, and infected macrophages, we found that the phosphatase was predominantly expressed and secreted by promastigotes via the exosome route. Finally, we observed that ectopic expression of LmPRL-1 in
led to an increased number of parasites in macrophages. From these data, we conclude that the
phosphatase LmPRL-1 contributes to the intracellular survival of the parasites in macrophages.</description><subject>Animals</subject><subject>Biological Transport</subject><subject>Cell Cycle Proteins - chemistry</subject><subject>Exosomes - metabolism</subject><subject>Fungal and Parasitic Infections</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Leishmania major - enzymology</subject><subject>Leishmania major - genetics</subject><subject>Macrophages - parasitology</subject><subject>Membrane Proteins - chemistry</subject><subject>Mice</subject><subject>Neoplasm Proteins - chemistry</subject><subject>Oxidation-Reduction</subject><subject>Phylogeny</subject><subject>Protein Tyrosine Phosphatases - chemistry</subject><subject>Protein Tyrosine Phosphatases - genetics</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Virulence</subject><subject>Virulence Factors</subject><issn>0019-9567</issn><issn>1098-5522</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU1v1DAQhi0Eokvhxhn5yIEUfyWxL0jVqsBKkaignK2JMyGuNvHW9rYsvx4vLRWc5uvVM6N5CXnN2RnnQr_fnG_OGGNaVbx9QlacGV3VtRBPyYoxbipTN-0JeZHSdSmVUvo5ORG6Zi1r-YrcrCeI4DJG_wuyDwsNI80T0ssYMvqFXh1iSH4pjSmk3QQZEtJuvvzaVZx-Qxcx40D7A-3Qp2mGxQOd4TpEeluyI-niZ0hhLgDI0x0cXpJnI2wTvnqIp-T7x4ur9eeq-_Jpsz7vKie1ylVj0AhAbRojWsfq2mHvUPFxdEoOrG-5GEQzaNVIKRsQI_QgNY5Cts2gzCBPyYd77m7fzzg4XHKErd1FP0M82ADe_j9Z_GR_hFtbnseUFAXw9gEQw80eU7azTw63W1gw7JPl2hjFVMPaIn13L3XlWSni-LiGM3t0yRaX7B-XLD_K3_x72qP4ry3yN2wGjyo</recordid><startdate>20170801</startdate><enddate>20170801</enddate><creator>Leitherer, Sabine</creator><creator>Clos, Joachim</creator><creator>Liebler-Tenorio, Elisabeth M</creator><creator>Schleicher, Ulrike</creator><creator>Bogdan, Christian</creator><creator>Soulat, Didier</creator><general>American Society for Microbiology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2300-0631</orcidid><orcidid>https://orcid.org/0000-0002-3688-5846</orcidid></search><sort><creationdate>20170801</creationdate><title>Characterization of the Protein Tyrosine Phosphatase LmPRL-1 Secreted by Leishmania major via the Exosome Pathway</title><author>Leitherer, Sabine ; Clos, Joachim ; Liebler-Tenorio, Elisabeth M ; Schleicher, Ulrike ; Bogdan, Christian ; Soulat, Didier</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c384t-69e92ae896927c055cebce41ffc43d0b712d26d8463336a2faba38ef2376d49d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Biological Transport</topic><topic>Cell Cycle Proteins - chemistry</topic><topic>Exosomes - metabolism</topic><topic>Fungal and Parasitic Infections</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Leishmania major - enzymology</topic><topic>Leishmania major - genetics</topic><topic>Macrophages - parasitology</topic><topic>Membrane Proteins - chemistry</topic><topic>Mice</topic><topic>Neoplasm Proteins - chemistry</topic><topic>Oxidation-Reduction</topic><topic>Phylogeny</topic><topic>Protein Tyrosine Phosphatases - chemistry</topic><topic>Protein Tyrosine Phosphatases - genetics</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>Virulence</topic><topic>Virulence Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leitherer, Sabine</creatorcontrib><creatorcontrib>Clos, Joachim</creatorcontrib><creatorcontrib>Liebler-Tenorio, Elisabeth M</creatorcontrib><creatorcontrib>Schleicher, Ulrike</creatorcontrib><creatorcontrib>Bogdan, Christian</creatorcontrib><creatorcontrib>Soulat, Didier</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Infection and immunity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leitherer, Sabine</au><au>Clos, Joachim</au><au>Liebler-Tenorio, Elisabeth M</au><au>Schleicher, Ulrike</au><au>Bogdan, Christian</au><au>Soulat, Didier</au><au>Adams, John H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the Protein Tyrosine Phosphatase LmPRL-1 Secreted by Leishmania major via the Exosome Pathway</atitle><jtitle>Infection and immunity</jtitle><addtitle>Infect Immun</addtitle><date>2017-08-01</date><risdate>2017</risdate><volume>85</volume><issue>8</issue><issn>0019-9567</issn><eissn>1098-5522</eissn><abstract>Similar to other intracellular pathogens,
parasites are known to evade the antimicrobial effector functions of host immune cells. To date, however, only a few virulence factors have been described for
, one of the causative agents of cutaneous leishmaniasis. Here, we have characterized the expression and function of an
phosphatase, which we termed LmPRL-1. This enzyme shows a strong structural similarity to the human phosphatases of regenerating liver (PRL-1, -2, and -3) that regulate the proliferation, differentiation, and motility of cells. The biochemical characterization of the
phosphatase revealed that the enzyme is redox sensitive. When analyzing the subcellular localization of LmPRL-1 in promastigotes, amastigotes, and infected macrophages, we found that the phosphatase was predominantly expressed and secreted by promastigotes via the exosome route. Finally, we observed that ectopic expression of LmPRL-1 in
led to an increased number of parasites in macrophages. From these data, we conclude that the
phosphatase LmPRL-1 contributes to the intracellular survival of the parasites in macrophages.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>28507071</pmid><doi>10.1128/IAI.00084-17</doi><orcidid>https://orcid.org/0000-0002-2300-0631</orcidid><orcidid>https://orcid.org/0000-0002-3688-5846</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Biological Transport Cell Cycle Proteins - chemistry Exosomes - metabolism Fungal and Parasitic Infections Humans Kinetics Leishmania major - enzymology Leishmania major - genetics Macrophages - parasitology Membrane Proteins - chemistry Mice Neoplasm Proteins - chemistry Oxidation-Reduction Phylogeny Protein Tyrosine Phosphatases - chemistry Protein Tyrosine Phosphatases - genetics Protein Tyrosine Phosphatases - metabolism Virulence Virulence Factors |
| title | Characterization of the Protein Tyrosine Phosphatase LmPRL-1 Secreted by Leishmania major via the Exosome Pathway |
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