Common pathways for receptor-mediated ingestion of Escherichia coli and LDL cholesterol by Entamoeba histolytica regulated in part by transmembrane kinase 39
[Display omitted] ► Entamoeba histolytica ingests low density lipoprotein (LDL) particles in a saturable manner. ► LDL particles are a competitive ligand for the ingestion of Escherichia coli bacteria. ► The adherence and ingestion of E. coli bacteria is regulated by transmembrane kinase 39. The sin...
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Veröffentlicht in: | International journal for parasitology 2012-04, Vol.42 (4), p.393-400 |
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► Entamoeba histolytica ingests low density lipoprotein (LDL) particles in a saturable manner. ► LDL particles are a competitive ligand for the ingestion of Escherichia coli bacteria. ► The adherence and ingestion of E. coli bacteria is regulated by transmembrane kinase 39.
The single-celled parasite, Entamoeba histolytica, is an enteric pathogen that ingests bacteria and host cells. Inhibition of phagocytosis renders the parasite avirulent. The ligand/receptor interactions that allow E. histolytica to phagocytose are not well understood. We hypothesised that E. histolytica trophozoites might accomplish ingestion through the utilisation of a scavenger receptor for cholesterol. Here we show that acetylated low density lipoprotein cholesterol was phagocytosed by amoebae via receptor-mediated mechanisms. Acetylated low density lipoprotein cholesterol competitively inhibited by 31±1.3% (P |
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► Entamoeba histolytica ingests low density lipoprotein (LDL) particles in a saturable manner. ► LDL particles are a competitive ligand for the ingestion of Escherichia coli bacteria. ► The adherence and ingestion of E. coli bacteria is regulated by transmembrane kinase 39.
The single-celled parasite, Entamoeba histolytica, is an enteric pathogen that ingests bacteria and host cells. Inhibition of phagocytosis renders the parasite avirulent. The ligand/receptor interactions that allow E. histolytica to phagocytose are not well understood. We hypothesised that E. histolytica trophozoites might accomplish ingestion through the utilisation of a scavenger receptor for cholesterol. Here we show that acetylated low density lipoprotein cholesterol was phagocytosed by amoebae via receptor-mediated mechanisms. Acetylated low density lipoprotein cholesterol competitively inhibited by 31±1.3% (P<0.005) the ingestion of Escherichia coli, but not erythrocytes and Jurkat T lymphocytes, suggesting a partially redundant phagocytic pathway for E. coli and cholesterol. Inducible expression of a signalling-dead dominant-negative version of E. histolytica transmembrane kinase 39 inhibited ingestion of E. coli by 55±3% (P<0.005) but not LDL particles. We concluded that ingestion of E. coli was regulated by TMK39 and partially shared the acetylated low density lipoprotein cholesterol uptake pathway.</description><identifier>ISSN: 0020-7519</identifier><identifier>EISSN: 1879-0135</identifier><identifier>DOI: 10.1016/j.ijpara.2012.02.009</identifier><identifier>PMID: 22619755</identifier><identifier>CODEN: IJPYBT</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Amoeba ; Bacteria ; Biological and medical sciences ; Cholesterol ; Cholesterol, LDL - metabolism ; Entamoeba histolytica ; Entamoeba histolytica - enzymology ; Entamoeba histolytica - metabolism ; Entamoeba histolytica - microbiology ; Entamoeba histolytica - physiology ; Erythrocytes ; Erythrocytes - metabolism ; Erythrocytes - microbiology ; Escherichia coli ; Escherichia coli - isolation & purification ; Fundamental and applied biological sciences. Psychology ; hosts ; Humans ; ingestion ; Jurkat Cells - metabolism ; Jurkat Cells - microbiology ; LDL receptor ; Life cycle. Host-agent relationship. Pathogenesis ; Lipoproteins ; Lipoproteins (low density) ; low density lipoprotein ; Lymphocytes T ; parasites ; Pathogens ; Phagocytes ; Phagocytosis ; Phosphotransferases - metabolism ; Protein Transport ; Protozoa ; receptors ; scavenger receptors ; T-lymphocytes ; Transmembrane kinase ; Trophozoites</subject><ispartof>International journal for parasitology, 2012-04, Vol.42 (4), p.393-400</ispartof><rights>2012 Australian Society for Parasitology Inc.</rights><rights>2015 INIST-CNRS</rights><rights>2012 Australian Society for Parasitology. Published by Elsevier Ltd. All rights reserved. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c625t-73a034b52f379bc4a468e84f3c0077cf39f489d626dddbc27781db85d2161d853</citedby><cites>FETCH-LOGICAL-c625t-73a034b52f379bc4a468e84f3c0077cf39f489d626dddbc27781db85d2161d853</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijpara.2012.02.009$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25845163$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22619755$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Christy, Nathaniel C.V.</creatorcontrib><creatorcontrib>Buss, Sarah N.</creatorcontrib><creatorcontrib>Petri, William A.</creatorcontrib><title>Common pathways for receptor-mediated ingestion of Escherichia coli and LDL cholesterol by Entamoeba histolytica regulated in part by transmembrane kinase 39</title><title>International journal for parasitology</title><addtitle>Int J Parasitol</addtitle><description>[Display omitted]
► Entamoeba histolytica ingests low density lipoprotein (LDL) particles in a saturable manner. ► LDL particles are a competitive ligand for the ingestion of Escherichia coli bacteria. ► The adherence and ingestion of E. coli bacteria is regulated by transmembrane kinase 39.
The single-celled parasite, Entamoeba histolytica, is an enteric pathogen that ingests bacteria and host cells. Inhibition of phagocytosis renders the parasite avirulent. The ligand/receptor interactions that allow E. histolytica to phagocytose are not well understood. We hypothesised that E. histolytica trophozoites might accomplish ingestion through the utilisation of a scavenger receptor for cholesterol. Here we show that acetylated low density lipoprotein cholesterol was phagocytosed by amoebae via receptor-mediated mechanisms. Acetylated low density lipoprotein cholesterol competitively inhibited by 31±1.3% (P<0.005) the ingestion of Escherichia coli, but not erythrocytes and Jurkat T lymphocytes, suggesting a partially redundant phagocytic pathway for E. coli and cholesterol. Inducible expression of a signalling-dead dominant-negative version of E. histolytica transmembrane kinase 39 inhibited ingestion of E. coli by 55±3% (P<0.005) but not LDL particles. We concluded that ingestion of E. coli was regulated by TMK39 and partially shared the acetylated low density lipoprotein cholesterol uptake pathway.</description><subject>Amoeba</subject><subject>Bacteria</subject><subject>Biological and medical sciences</subject><subject>Cholesterol</subject><subject>Cholesterol, LDL - metabolism</subject><subject>Entamoeba histolytica</subject><subject>Entamoeba histolytica - enzymology</subject><subject>Entamoeba histolytica - metabolism</subject><subject>Entamoeba histolytica - microbiology</subject><subject>Entamoeba histolytica - physiology</subject><subject>Erythrocytes</subject><subject>Erythrocytes - metabolism</subject><subject>Erythrocytes - microbiology</subject><subject>Escherichia coli</subject><subject>Escherichia coli - isolation & purification</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hosts</subject><subject>Humans</subject><subject>ingestion</subject><subject>Jurkat Cells - metabolism</subject><subject>Jurkat Cells - microbiology</subject><subject>LDL receptor</subject><subject>Life cycle. Host-agent relationship. Pathogenesis</subject><subject>Lipoproteins</subject><subject>Lipoproteins (low density)</subject><subject>low density lipoprotein</subject><subject>Lymphocytes T</subject><subject>parasites</subject><subject>Pathogens</subject><subject>Phagocytes</subject><subject>Phagocytosis</subject><subject>Phosphotransferases - metabolism</subject><subject>Protein Transport</subject><subject>Protozoa</subject><subject>receptors</subject><subject>scavenger receptors</subject><subject>T-lymphocytes</subject><subject>Transmembrane kinase</subject><subject>Trophozoites</subject><issn>0020-7519</issn><issn>1879-0135</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNksuO0zAUhiMEYsrAGyDkDRKbFF_iON4goVIuUiU2sLYc22lcnLjY7oz6MLwrp2qZgQ0gWToLf-c__7lU1XOClwST9vVu6Xd7nfSSYkKXGB6WD6oF6YSsMWH8YbXAmOJacCKvqic57zAmnDXN4-qK0pZIwfmi-rGK0xRntNdlvNXHjIaYUHLG7UtM9eSs18VZ5Oety8UDGAe0zmZ0yZvRa2Ri8EjPFm3ebZAZYwDMpRhQf0Truegpul6j0ecSw7F4o0F8ewgXUSibygktSc95clMP0aFvftbZISafVo8GHbJ7donX1df36y-rj_Xm84dPq7eb2rSUl1owjVnTczowIXvT6KbtXNcMzGAshBmYHJpO2pa21treUCE6YvuOW0paYjvOrqs3Z939oYeejZvBUFD75Cedjipqr_78mf2otvFGwTgllAaBVxeBFL8fYAZq8tm4EKCdeMiKNKctccbIv1HYkuAMLP4PSihhncCANmfUpJhzcsOdeYJPXKt26nwv6uREYXhYQtqL3xu_S_p1IAC8vAA6Gx0G2I_x-Z7jXcNJy-4n6GBNN94llY13s4EDgmsqykb_dyc_ATSE4r8</recordid><startdate>20120401</startdate><enddate>20120401</enddate><creator>Christy, Nathaniel C.V.</creator><creator>Buss, Sarah N.</creator><creator>Petri, William A.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope><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>7QL</scope><scope>C1K</scope><scope>M7N</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20120401</creationdate><title>Common pathways for receptor-mediated ingestion of Escherichia coli and LDL cholesterol by Entamoeba histolytica regulated in part by transmembrane kinase 39</title><author>Christy, Nathaniel C.V. ; Buss, Sarah N. ; Petri, William A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c625t-73a034b52f379bc4a468e84f3c0077cf39f489d626dddbc27781db85d2161d853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amoeba</topic><topic>Bacteria</topic><topic>Biological and medical sciences</topic><topic>Cholesterol</topic><topic>Cholesterol, LDL - metabolism</topic><topic>Entamoeba histolytica</topic><topic>Entamoeba histolytica - enzymology</topic><topic>Entamoeba histolytica - metabolism</topic><topic>Entamoeba histolytica - microbiology</topic><topic>Entamoeba histolytica - physiology</topic><topic>Erythrocytes</topic><topic>Erythrocytes - metabolism</topic><topic>Erythrocytes - microbiology</topic><topic>Escherichia coli</topic><topic>Escherichia coli - isolation & purification</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hosts</topic><topic>Humans</topic><topic>ingestion</topic><topic>Jurkat Cells - metabolism</topic><topic>Jurkat Cells - microbiology</topic><topic>LDL receptor</topic><topic>Life cycle. Host-agent relationship. Pathogenesis</topic><topic>Lipoproteins</topic><topic>Lipoproteins (low density)</topic><topic>low density lipoprotein</topic><topic>Lymphocytes T</topic><topic>parasites</topic><topic>Pathogens</topic><topic>Phagocytes</topic><topic>Phagocytosis</topic><topic>Phosphotransferases - metabolism</topic><topic>Protein Transport</topic><topic>Protozoa</topic><topic>receptors</topic><topic>scavenger receptors</topic><topic>T-lymphocytes</topic><topic>Transmembrane kinase</topic><topic>Trophozoites</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Christy, Nathaniel C.V.</creatorcontrib><creatorcontrib>Buss, Sarah N.</creatorcontrib><creatorcontrib>Petri, William A.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal for parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Christy, Nathaniel C.V.</au><au>Buss, Sarah N.</au><au>Petri, William A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Common pathways for receptor-mediated ingestion of Escherichia coli and LDL cholesterol by Entamoeba histolytica regulated in part by transmembrane kinase 39</atitle><jtitle>International journal for parasitology</jtitle><addtitle>Int J Parasitol</addtitle><date>2012-04-01</date><risdate>2012</risdate><volume>42</volume><issue>4</issue><spage>393</spage><epage>400</epage><pages>393-400</pages><issn>0020-7519</issn><eissn>1879-0135</eissn><coden>IJPYBT</coden><abstract>[Display omitted]
► Entamoeba histolytica ingests low density lipoprotein (LDL) particles in a saturable manner. ► LDL particles are a competitive ligand for the ingestion of Escherichia coli bacteria. ► The adherence and ingestion of E. coli bacteria is regulated by transmembrane kinase 39.
The single-celled parasite, Entamoeba histolytica, is an enteric pathogen that ingests bacteria and host cells. Inhibition of phagocytosis renders the parasite avirulent. The ligand/receptor interactions that allow E. histolytica to phagocytose are not well understood. We hypothesised that E. histolytica trophozoites might accomplish ingestion through the utilisation of a scavenger receptor for cholesterol. Here we show that acetylated low density lipoprotein cholesterol was phagocytosed by amoebae via receptor-mediated mechanisms. Acetylated low density lipoprotein cholesterol competitively inhibited by 31±1.3% (P<0.005) the ingestion of Escherichia coli, but not erythrocytes and Jurkat T lymphocytes, suggesting a partially redundant phagocytic pathway for E. coli and cholesterol. Inducible expression of a signalling-dead dominant-negative version of E. histolytica transmembrane kinase 39 inhibited ingestion of E. coli by 55±3% (P<0.005) but not LDL particles. We concluded that ingestion of E. coli was regulated by TMK39 and partially shared the acetylated low density lipoprotein cholesterol uptake pathway.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>22619755</pmid><doi>10.1016/j.ijpara.2012.02.009</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amoeba Bacteria Biological and medical sciences Cholesterol Cholesterol, LDL - metabolism Entamoeba histolytica Entamoeba histolytica - enzymology Entamoeba histolytica - metabolism Entamoeba histolytica - microbiology Entamoeba histolytica - physiology Erythrocytes Erythrocytes - metabolism Erythrocytes - microbiology Escherichia coli Escherichia coli - isolation & purification Fundamental and applied biological sciences. Psychology hosts Humans ingestion Jurkat Cells - metabolism Jurkat Cells - microbiology LDL receptor Life cycle. Host-agent relationship. Pathogenesis Lipoproteins Lipoproteins (low density) low density lipoprotein Lymphocytes T parasites Pathogens Phagocytes Phagocytosis Phosphotransferases - metabolism Protein Transport Protozoa receptors scavenger receptors T-lymphocytes Transmembrane kinase Trophozoites |
title | Common pathways for receptor-mediated ingestion of Escherichia coli and LDL cholesterol by Entamoeba histolytica regulated in part by transmembrane kinase 39 |
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