Myeloperoxidase binds to and kills Entamoeba histolytica trophozoites
Summary During amebic invasion, neutrophils are a key component in either protecting against invading trophozoites or contributing to tissue damage. Upon degranulating or being lysed, neutrophils release toxic substances that can kill amebas as well as damage host tissue. In a previous study we iden...
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| Veröffentlicht in: | Parasite immunology 2011-05, Vol.33 (5), p.255-264 |
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| creator | PACHECO‐YÉPEZ, J. RIVERA‐AGUILAR, V. BARBOSA‐CABRERA, E. ROJAS HERNÁNDEZ, S. JARILLO‐LUNA, R. A. CAMPOS‐RODRÍGUEZ, R. |
| description | Summary
During amebic invasion, neutrophils are a key component in either protecting against invading trophozoites or contributing to tissue damage. Upon degranulating or being lysed, neutrophils release toxic substances that can kill amebas as well as damage host tissue. In a previous study we identified a protein from nonspecifically stimulated peritoneal exudates of hamster that has peroxidase and marked amebicidal activity. In the current study we analyzed the in vitro amebicidal effect of purified hamster myeloperoxidase (MPO). The results demonstrate that MPO must bind directly to the surface of Entamoeba histolytica trophozoites in order to carry out amebicidal activity by using the H2O2 produced by the amebas themselves. Myeloperoxidase‐incubated amebas showed important morphological and ultrastructural alterations that increased with incubation time. Changes included an increase of vacuoles in the cytoplasm, a decrease of glycogen, alterations of nuclear morphology and disturbances in the plasma membrane culminating in complete ameba destruction. |
| doi_str_mv | 10.1111/j.1365-3024.2010.01275.x |
| format | Article |
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During amebic invasion, neutrophils are a key component in either protecting against invading trophozoites or contributing to tissue damage. Upon degranulating or being lysed, neutrophils release toxic substances that can kill amebas as well as damage host tissue. In a previous study we identified a protein from nonspecifically stimulated peritoneal exudates of hamster that has peroxidase and marked amebicidal activity. In the current study we analyzed the in vitro amebicidal effect of purified hamster myeloperoxidase (MPO). The results demonstrate that MPO must bind directly to the surface of Entamoeba histolytica trophozoites in order to carry out amebicidal activity by using the H2O2 produced by the amebas themselves. Myeloperoxidase‐incubated amebas showed important morphological and ultrastructural alterations that increased with incubation time. Changes included an increase of vacuoles in the cytoplasm, a decrease of glycogen, alterations of nuclear morphology and disturbances in the plasma membrane culminating in complete ameba destruction.</description><identifier>ISSN: 0141-9838</identifier><identifier>EISSN: 1365-3024</identifier><identifier>DOI: 10.1111/j.1365-3024.2010.01275.x</identifier><identifier>PMID: 21204853</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>amebicidal activity ; Animals ; Antiprotozoal Agents - isolation & purification ; Antiprotozoal Agents - metabolism ; Antiprotozoal Agents - pharmacology ; Cell Survival ; Cricetinae ; E. histolytica ; Entamoeba histolytica ; Entamoeba histolytica - cytology ; Entamoeba histolytica - drug effects ; hydrogen peroxide ; Male ; Mesocricetus ; myeloperoxidase ; neutrophil ; Neutrophils - enzymology ; Peroxidase - isolation & purification ; Peroxidase - metabolism ; Peroxidase - pharmacology ; Protein Binding ; Trophozoites - cytology ; Trophozoites - drug effects</subject><ispartof>Parasite immunology, 2011-05, Vol.33 (5), p.255-264</ispartof><rights>2011 Blackwell Publishing Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3955-c36d21846015774f24e70d4be8697f6502444ac64dabd8407cefb66d5e24c35b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-3024.2010.01275.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-3024.2010.01275.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21204853$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>PACHECO‐YÉPEZ, J.</creatorcontrib><creatorcontrib>RIVERA‐AGUILAR, V.</creatorcontrib><creatorcontrib>BARBOSA‐CABRERA, E.</creatorcontrib><creatorcontrib>ROJAS HERNÁNDEZ, S.</creatorcontrib><creatorcontrib>JARILLO‐LUNA, R. A.</creatorcontrib><creatorcontrib>CAMPOS‐RODRÍGUEZ, R.</creatorcontrib><title>Myeloperoxidase binds to and kills Entamoeba histolytica trophozoites</title><title>Parasite immunology</title><addtitle>Parasite Immunol</addtitle><description>Summary
During amebic invasion, neutrophils are a key component in either protecting against invading trophozoites or contributing to tissue damage. Upon degranulating or being lysed, neutrophils release toxic substances that can kill amebas as well as damage host tissue. In a previous study we identified a protein from nonspecifically stimulated peritoneal exudates of hamster that has peroxidase and marked amebicidal activity. In the current study we analyzed the in vitro amebicidal effect of purified hamster myeloperoxidase (MPO). The results demonstrate that MPO must bind directly to the surface of Entamoeba histolytica trophozoites in order to carry out amebicidal activity by using the H2O2 produced by the amebas themselves. Myeloperoxidase‐incubated amebas showed important morphological and ultrastructural alterations that increased with incubation time. Changes included an increase of vacuoles in the cytoplasm, a decrease of glycogen, alterations of nuclear morphology and disturbances in the plasma membrane culminating in complete ameba destruction.</description><subject>amebicidal activity</subject><subject>Animals</subject><subject>Antiprotozoal Agents - isolation & purification</subject><subject>Antiprotozoal Agents - metabolism</subject><subject>Antiprotozoal Agents - pharmacology</subject><subject>Cell Survival</subject><subject>Cricetinae</subject><subject>E. histolytica</subject><subject>Entamoeba histolytica</subject><subject>Entamoeba histolytica - cytology</subject><subject>Entamoeba histolytica - drug effects</subject><subject>hydrogen peroxide</subject><subject>Male</subject><subject>Mesocricetus</subject><subject>myeloperoxidase</subject><subject>neutrophil</subject><subject>Neutrophils - enzymology</subject><subject>Peroxidase - isolation & purification</subject><subject>Peroxidase - metabolism</subject><subject>Peroxidase - pharmacology</subject><subject>Protein Binding</subject><subject>Trophozoites - cytology</subject><subject>Trophozoites - drug effects</subject><issn>0141-9838</issn><issn>1365-3024</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkD1PwzAQhi0EoqXwF1A2pgR_xxkYUFWgUisYYLac2FFdnDjEqWj49SQUOuPhfLp7773TA0CEYIKGd7tNEOEsJhDTBMOhChFOWbI_AdNj4xRMIaIozgQRE3ARwhZCRDAn52CCEYZUMDIFi3VvnG9M6_dWq2Ci3NY6RJ2PVK2jd-tciBZ1pypvchVtbOi86ztbqKhrfbPxX952JlyCs1K5YK5-_xl4e1i8zp_i1fPjcn6_iguSMTZErjESlEPE0pSWmJoUapobwbO05Gy4mlJVcKpVrgWFaWHKnHPNDKYFYTmZgZuDb9P6j50JnaxsKIxzqjZ-F6Tgg63IEB6U4qAsWh9Ca0rZtLZSbS8RlCNDuZUjKjmikiND-cNQ7ofR698lu7wy-jj4B20Q3B0En9aZ_t_G8mW5HjPyDbN2f7A</recordid><startdate>201105</startdate><enddate>201105</enddate><creator>PACHECO‐YÉPEZ, J.</creator><creator>RIVERA‐AGUILAR, V.</creator><creator>BARBOSA‐CABRERA, E.</creator><creator>ROJAS HERNÁNDEZ, S.</creator><creator>JARILLO‐LUNA, R. A.</creator><creator>CAMPOS‐RODRÍGUEZ, R.</creator><general>Blackwell Publishing Ltd</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>7T5</scope><scope>F1W</scope><scope>H94</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope></search><sort><creationdate>201105</creationdate><title>Myeloperoxidase binds to and kills Entamoeba histolytica trophozoites</title><author>PACHECO‐YÉPEZ, J. ; RIVERA‐AGUILAR, V. ; BARBOSA‐CABRERA, E. ; ROJAS HERNÁNDEZ, S. ; JARILLO‐LUNA, R. A. ; CAMPOS‐RODRÍGUEZ, R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3955-c36d21846015774f24e70d4be8697f6502444ac64dabd8407cefb66d5e24c35b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>amebicidal activity</topic><topic>Animals</topic><topic>Antiprotozoal Agents - isolation & purification</topic><topic>Antiprotozoal Agents - metabolism</topic><topic>Antiprotozoal Agents - pharmacology</topic><topic>Cell Survival</topic><topic>Cricetinae</topic><topic>E. histolytica</topic><topic>Entamoeba histolytica</topic><topic>Entamoeba histolytica - cytology</topic><topic>Entamoeba histolytica - drug effects</topic><topic>hydrogen peroxide</topic><topic>Male</topic><topic>Mesocricetus</topic><topic>myeloperoxidase</topic><topic>neutrophil</topic><topic>Neutrophils - enzymology</topic><topic>Peroxidase - isolation & purification</topic><topic>Peroxidase - metabolism</topic><topic>Peroxidase - pharmacology</topic><topic>Protein Binding</topic><topic>Trophozoites - cytology</topic><topic>Trophozoites - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>PACHECO‐YÉPEZ, J.</creatorcontrib><creatorcontrib>RIVERA‐AGUILAR, V.</creatorcontrib><creatorcontrib>BARBOSA‐CABRERA, E.</creatorcontrib><creatorcontrib>ROJAS HERNÁNDEZ, S.</creatorcontrib><creatorcontrib>JARILLO‐LUNA, R. A.</creatorcontrib><creatorcontrib>CAMPOS‐RODRÍGUEZ, R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Parasite immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>PACHECO‐YÉPEZ, J.</au><au>RIVERA‐AGUILAR, V.</au><au>BARBOSA‐CABRERA, E.</au><au>ROJAS HERNÁNDEZ, S.</au><au>JARILLO‐LUNA, R. A.</au><au>CAMPOS‐RODRÍGUEZ, R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Myeloperoxidase binds to and kills Entamoeba histolytica trophozoites</atitle><jtitle>Parasite immunology</jtitle><addtitle>Parasite Immunol</addtitle><date>2011-05</date><risdate>2011</risdate><volume>33</volume><issue>5</issue><spage>255</spage><epage>264</epage><pages>255-264</pages><issn>0141-9838</issn><eissn>1365-3024</eissn><abstract>Summary
During amebic invasion, neutrophils are a key component in either protecting against invading trophozoites or contributing to tissue damage. Upon degranulating or being lysed, neutrophils release toxic substances that can kill amebas as well as damage host tissue. In a previous study we identified a protein from nonspecifically stimulated peritoneal exudates of hamster that has peroxidase and marked amebicidal activity. In the current study we analyzed the in vitro amebicidal effect of purified hamster myeloperoxidase (MPO). The results demonstrate that MPO must bind directly to the surface of Entamoeba histolytica trophozoites in order to carry out amebicidal activity by using the H2O2 produced by the amebas themselves. Myeloperoxidase‐incubated amebas showed important morphological and ultrastructural alterations that increased with incubation time. Changes included an increase of vacuoles in the cytoplasm, a decrease of glycogen, alterations of nuclear morphology and disturbances in the plasma membrane culminating in complete ameba destruction.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>21204853</pmid><doi>10.1111/j.1365-3024.2010.01275.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | amebicidal activity Animals Antiprotozoal Agents - isolation & purification Antiprotozoal Agents - metabolism Antiprotozoal Agents - pharmacology Cell Survival Cricetinae E. histolytica Entamoeba histolytica Entamoeba histolytica - cytology Entamoeba histolytica - drug effects hydrogen peroxide Male Mesocricetus myeloperoxidase neutrophil Neutrophils - enzymology Peroxidase - isolation & purification Peroxidase - metabolism Peroxidase - pharmacology Protein Binding Trophozoites - cytology Trophozoites - drug effects |
| title | Myeloperoxidase binds to and kills Entamoeba histolytica trophozoites |
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