A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts
We demonstrate a functional role for the paraflagellar rod (PFR) in motility of Leishmania mexicana. The PFR is a complex cytoskeletal structure running parallel to the axoneme in the flagella of kinetoplastid protozoa. The PFR is composed of a latticework of protein filaments whose major constituen...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1997-12, Vol.90 (1), p.95-109 |
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| creator | Santrich, C Moore, L Sherwin, T Bastin, P Brokaw, C Gull, K LeBowitz, J.H |
| description | We demonstrate a functional role for the paraflagellar rod (PFR) in motility of
Leishmania mexicana. The PFR is a complex cytoskeletal structure running parallel to the axoneme in the flagella of kinetoplastid protozoa. The PFR is composed of a latticework of protein filaments whose major constituents are two related proteins (PFR-1 and PFR-2 in
Leishmania). The molecular details of their assembly into PFR filaments are unknown as is the biological function of the PFR. As an approach to understanding the structure and function of the PFR in
Leishmania, we made
L. mexicana null mutants of
PFR-2.
PFR-2 minus parasites grow and divide normally in culture and still express the PFR-1 protein. They lack most of the PFR structure demonstrating that the PFR-2 protein is an essential constituent of the PFR. Detailed ultrastructural analysis of the
PFR-2 null mutant reveals the presence of a residual inner substructure of the PFR which contains PFR-1 protein, indicating that PFR-1 can polymerize in the absence of PFR-2. The
PFR-2 null mutant displays pronounced changes in flagellar beat waveform and forward swimming velocity, compared to wild type parasites consistent with decreased internal elastic bending resistance in PFR-lacking flagella, and indicating a functional role for the PFR in the motility of
Leishmania. |
| doi_str_mv | 10.1016/S0166-6851(97)00149-7 |
| format | Article |
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Leishmania mexicana. The PFR is a complex cytoskeletal structure running parallel to the axoneme in the flagella of kinetoplastid protozoa. The PFR is composed of a latticework of protein filaments whose major constituents are two related proteins (PFR-1 and PFR-2 in
Leishmania). The molecular details of their assembly into PFR filaments are unknown as is the biological function of the PFR. As an approach to understanding the structure and function of the PFR in
Leishmania, we made
L. mexicana null mutants of
PFR-2.
PFR-2 minus parasites grow and divide normally in culture and still express the PFR-1 protein. They lack most of the PFR structure demonstrating that the PFR-2 protein is an essential constituent of the PFR. Detailed ultrastructural analysis of the
PFR-2 null mutant reveals the presence of a residual inner substructure of the PFR which contains PFR-1 protein, indicating that PFR-1 can polymerize in the absence of PFR-2. The
PFR-2 null mutant displays pronounced changes in flagellar beat waveform and forward swimming velocity, compared to wild type parasites consistent with decreased internal elastic bending resistance in PFR-lacking flagella, and indicating a functional role for the PFR in the motility of
Leishmania.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/S0166-6851(97)00149-7</identifier><identifier>PMID: 9497035</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Cytoskeleton ; Cytoskeleton - chemistry ; Cytoskeleton - physiology ; Cytoskeleton - ultrastructure ; Flagella ; Flagella - chemistry ; Flagella - physiology ; Flagella - ultrastructure ; Fluorescent Antibody Technique ; Gene Targeting ; Genes, Protozoan ; Leishmania ; Leishmania mexicana - genetics ; Leishmania mexicana - physiology ; Motility ; Movement ; Mutation ; Paraflagellar rod ; Phenotype ; Protozoan Proteins - genetics ; Protozoan Proteins - physiology ; Trypanosome</subject><ispartof>Molecular and biochemical parasitology, 1997-12, Vol.90 (1), p.95-109</ispartof><rights>1997 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-4fec90f433548108b77d2e8e639a83963782d3f7ce18779be4b6036ed723c1fe3</citedby><cites>FETCH-LOGICAL-c426t-4fec90f433548108b77d2e8e639a83963782d3f7ce18779be4b6036ed723c1fe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0166-6851(97)00149-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9497035$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Santrich, C</creatorcontrib><creatorcontrib>Moore, L</creatorcontrib><creatorcontrib>Sherwin, T</creatorcontrib><creatorcontrib>Bastin, P</creatorcontrib><creatorcontrib>Brokaw, C</creatorcontrib><creatorcontrib>Gull, K</creatorcontrib><creatorcontrib>LeBowitz, J.H</creatorcontrib><title>A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>We demonstrate a functional role for the paraflagellar rod (PFR) in motility of
Leishmania mexicana. The PFR is a complex cytoskeletal structure running parallel to the axoneme in the flagella of kinetoplastid protozoa. The PFR is composed of a latticework of protein filaments whose major constituents are two related proteins (PFR-1 and PFR-2 in
Leishmania). The molecular details of their assembly into PFR filaments are unknown as is the biological function of the PFR. As an approach to understanding the structure and function of the PFR in
Leishmania, we made
L. mexicana null mutants of
PFR-2.
PFR-2 minus parasites grow and divide normally in culture and still express the PFR-1 protein. They lack most of the PFR structure demonstrating that the PFR-2 protein is an essential constituent of the PFR. Detailed ultrastructural analysis of the
PFR-2 null mutant reveals the presence of a residual inner substructure of the PFR which contains PFR-1 protein, indicating that PFR-1 can polymerize in the absence of PFR-2. The
PFR-2 null mutant displays pronounced changes in flagellar beat waveform and forward swimming velocity, compared to wild type parasites consistent with decreased internal elastic bending resistance in PFR-lacking flagella, and indicating a functional role for the PFR in the motility of
Leishmania.</description><subject>Animals</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton - chemistry</subject><subject>Cytoskeleton - physiology</subject><subject>Cytoskeleton - ultrastructure</subject><subject>Flagella</subject><subject>Flagella - chemistry</subject><subject>Flagella - physiology</subject><subject>Flagella - ultrastructure</subject><subject>Fluorescent Antibody Technique</subject><subject>Gene Targeting</subject><subject>Genes, Protozoan</subject><subject>Leishmania</subject><subject>Leishmania mexicana - genetics</subject><subject>Leishmania mexicana - physiology</subject><subject>Motility</subject><subject>Movement</subject><subject>Mutation</subject><subject>Paraflagellar rod</subject><subject>Phenotype</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - physiology</subject><subject>Trypanosome</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtP3DAUha2qFR0oPwHJq6osQu3Y8WOFEOIljdQKytpynGtwSeLBdpDm35N5iC2bexfn3Mf5EDqh5IwSKn4_zEVUQjX0l5anhFCuK_kFLaiSdaV5rb6ixYflOzrM-T8hpJFCHKADzbUkrFkgf4GHWEIfyhr7aXQlxBH7mHB5BryyyfrePkHf24RT7HD0eAkhPw92DHar51Ag4wRvYHvocLvGf6_vqxo_wQj4ZYzuJU4l_0DfvO0zHO_7EXq8vvp3eVst_9zcXV4sK8drUSruwWniOWMNV5SoVsquBgWCaauYFkyqumNeOphTSt0CbwVhAjpZM0c9sCP0c7d3leLrBLmYIWS3-X-EOGVDBada1mo2NjujSzHnBN6sUhhsWhtKzIav2fI1G3hGS7Pla-Q8d7I_MLUDdB9Te6Czfr7TYU75FiCZ7AKMDrqQwBXTxfDJhXeaXopw</recordid><startdate>19971201</startdate><enddate>19971201</enddate><creator>Santrich, C</creator><creator>Moore, L</creator><creator>Sherwin, T</creator><creator>Bastin, P</creator><creator>Brokaw, C</creator><creator>Gull, K</creator><creator>LeBowitz, J.H</creator><general>Elsevier B.V</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19971201</creationdate><title>A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts</title><author>Santrich, C ; Moore, L ; Sherwin, T ; Bastin, P ; Brokaw, C ; Gull, K ; LeBowitz, J.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-4fec90f433548108b77d2e8e639a83963782d3f7ce18779be4b6036ed723c1fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Cytoskeleton</topic><topic>Cytoskeleton - chemistry</topic><topic>Cytoskeleton - physiology</topic><topic>Cytoskeleton - ultrastructure</topic><topic>Flagella</topic><topic>Flagella - chemistry</topic><topic>Flagella - physiology</topic><topic>Flagella - ultrastructure</topic><topic>Fluorescent Antibody Technique</topic><topic>Gene Targeting</topic><topic>Genes, Protozoan</topic><topic>Leishmania</topic><topic>Leishmania mexicana - genetics</topic><topic>Leishmania mexicana - physiology</topic><topic>Motility</topic><topic>Movement</topic><topic>Mutation</topic><topic>Paraflagellar rod</topic><topic>Phenotype</topic><topic>Protozoan Proteins - genetics</topic><topic>Protozoan Proteins - physiology</topic><topic>Trypanosome</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Santrich, C</creatorcontrib><creatorcontrib>Moore, L</creatorcontrib><creatorcontrib>Sherwin, T</creatorcontrib><creatorcontrib>Bastin, P</creatorcontrib><creatorcontrib>Brokaw, C</creatorcontrib><creatorcontrib>Gull, K</creatorcontrib><creatorcontrib>LeBowitz, J.H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Santrich, C</au><au>Moore, L</au><au>Sherwin, T</au><au>Bastin, P</au><au>Brokaw, C</au><au>Gull, K</au><au>LeBowitz, J.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1997-12-01</date><risdate>1997</risdate><volume>90</volume><issue>1</issue><spage>95</spage><epage>109</epage><pages>95-109</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><abstract>We demonstrate a functional role for the paraflagellar rod (PFR) in motility of
Leishmania mexicana. The PFR is a complex cytoskeletal structure running parallel to the axoneme in the flagella of kinetoplastid protozoa. The PFR is composed of a latticework of protein filaments whose major constituents are two related proteins (PFR-1 and PFR-2 in
Leishmania). The molecular details of their assembly into PFR filaments are unknown as is the biological function of the PFR. As an approach to understanding the structure and function of the PFR in
Leishmania, we made
L. mexicana null mutants of
PFR-2.
PFR-2 minus parasites grow and divide normally in culture and still express the PFR-1 protein. They lack most of the PFR structure demonstrating that the PFR-2 protein is an essential constituent of the PFR. Detailed ultrastructural analysis of the
PFR-2 null mutant reveals the presence of a residual inner substructure of the PFR which contains PFR-1 protein, indicating that PFR-1 can polymerize in the absence of PFR-2. The
PFR-2 null mutant displays pronounced changes in flagellar beat waveform and forward swimming velocity, compared to wild type parasites consistent with decreased internal elastic bending resistance in PFR-lacking flagella, and indicating a functional role for the PFR in the motility of
Leishmania.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>9497035</pmid><doi>10.1016/S0166-6851(97)00149-7</doi><tpages>15</tpages></addata></record> |
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| subjects | Animals Cytoskeleton Cytoskeleton - chemistry Cytoskeleton - physiology Cytoskeleton - ultrastructure Flagella Flagella - chemistry Flagella - physiology Flagella - ultrastructure Fluorescent Antibody Technique Gene Targeting Genes, Protozoan Leishmania Leishmania mexicana - genetics Leishmania mexicana - physiology Motility Movement Mutation Paraflagellar rod Phenotype Protozoan Proteins - genetics Protozoan Proteins - physiology Trypanosome |
| title | A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts |
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