Identification and characterization of a surface-associated, subtilisin-like serine protease in Trichomonas vaginalis
Trichomonas vaginalis is a protozoan parasite causing trichomonosis, a sexually transmitted infection in humans. This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and character...
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description | Trichomonas vaginalis is a protozoan parasite causing trichomonosis, a sexually transmitted infection in humans. This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and characterize a putative subtilisin-like serine protease (SUB1). The sub1 gene encodes a 101-kDa protein. In silico analyses predict signal and pro-peptides at the N-terminus, and a transmembrane helix at the carboxy-terminal region. The sub1 gene was found as single copy by Southern analysis, albeit additional serine protease related genes are annotated in the T. vaginalis genome. The expression of sub1 could only be detected by RT-PCR and Ribonuclease Protection Assays, suggesting a low abundant mRNA. The sub1 gene transcription start site was correctly assigned by RPA. The transcript abundance was found to be modulated by the availability of iron in the growth medium. Antibodies raised to a specific SUB1 peptide recognized a single protein band (~82 kDa) in Western blots, possibly representing the mature form of the protein. Immunofluorescence showed SUB1 on the trichomonad surface, and in dispersed vesicles throughout the cytoplasm. A bioinformatic analysis of genes annotated as serine proteases in the T. vaginalis genome is also presented. To our knowledge this is the first putative serine protease experimentally described for T. vaginalis. |
doi_str_mv | 10.1017/S003118201000051X |
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This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and characterize a putative subtilisin-like serine protease (SUB1). The sub1 gene encodes a 101-kDa protein. In silico analyses predict signal and pro-peptides at the N-terminus, and a transmembrane helix at the carboxy-terminal region. The sub1 gene was found as single copy by Southern analysis, albeit additional serine protease related genes are annotated in the T. vaginalis genome. The expression of sub1 could only be detected by RT-PCR and Ribonuclease Protection Assays, suggesting a low abundant mRNA. The sub1 gene transcription start site was correctly assigned by RPA. The transcript abundance was found to be modulated by the availability of iron in the growth medium. Antibodies raised to a specific SUB1 peptide recognized a single protein band (~82 kDa) in Western blots, possibly representing the mature form of the protein. Immunofluorescence showed SUB1 on the trichomonad surface, and in dispersed vesicles throughout the cytoplasm. A bioinformatic analysis of genes annotated as serine proteases in the T. vaginalis genome is also presented. To our knowledge this is the first putative serine protease experimentally described for T. vaginalis.</description><identifier>ISSN: 0031-1820</identifier><identifier>EISSN: 1469-8161</identifier><identifier>DOI: 10.1017/S003118201000051X</identifier><identifier>PMID: 20602853</identifier><identifier>CODEN: PARAAE</identifier><language>eng</language><publisher>Cambridge, UK: Cambridge University Press</publisher><subject>Amino Acid Sequence ; Animals ; Antigens, Protozoan - chemistry ; Antigens, Protozoan - genetics ; Antigens, Protozoan - immunology ; Antigens, Protozoan - metabolism ; Base Sequence ; Biological and medical sciences ; cellular localization ; Cytotoxicity ; Female ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation ; General aspects ; General aspects and techniques. Study of several systematic groups. Models ; Humans ; Invertebrates ; Iron - metabolism ; Mice ; Models, Molecular ; Molecular Sequence Data ; Parasites ; Peptides ; Protozoan Proteins - chemistry ; Protozoan Proteins - genetics ; Protozoan Proteins - immunology ; Protozoan Proteins - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, DNA ; serine protease ; Serine Proteases - chemistry ; Serine Proteases - genetics ; Serine Proteases - immunology ; Serine Proteases - metabolism ; Sexually transmitted diseases ; STD ; subtilisin ; Subtilisin - chemistry ; Subtilisin - genetics ; Subtilisin - immunology ; Subtilisin - metabolism ; surface protein ; Trichomonas vaginalis ; Trichomonas vaginalis - enzymology ; Trichomonas vaginalis - genetics ; Trichomonas vaginalis - metabolism</subject><ispartof>Parasitology, 2010-09, Vol.137 (11), p.1621-1635</ispartof><rights>Copyright © Cambridge University Press 2010</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-4623a2789bcffbd4f7ca10655a038070db353b6ff16ebfc907a53147fbdf2e953</citedby><cites>FETCH-LOGICAL-c471t-4623a2789bcffbd4f7ca10655a038070db353b6ff16ebfc907a53147fbdf2e953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.cambridge.org/core/product/identifier/S003118201000051X/type/journal_article$$EHTML$$P50$$Gcambridge$$H</linktohtml><link.rule.ids>164,314,780,784,27924,27925,55628</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23361466$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20602853$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HERNÁNDEZ-ROMANO, PABLO</creatorcontrib><creatorcontrib>HERNÁNDEZ, ROBERTO</creatorcontrib><creatorcontrib>ARROYO, ROSSANA</creatorcontrib><creatorcontrib>ALDERETE, JOHN F.</creatorcontrib><creatorcontrib>LÓPEZ-VILLASEÑOR, IMELDA</creatorcontrib><title>Identification and characterization of a surface-associated, subtilisin-like serine protease in Trichomonas vaginalis</title><title>Parasitology</title><addtitle>Parasitology</addtitle><description>Trichomonas vaginalis is a protozoan parasite causing trichomonosis, a sexually transmitted infection in humans. This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and characterize a putative subtilisin-like serine protease (SUB1). The sub1 gene encodes a 101-kDa protein. In silico analyses predict signal and pro-peptides at the N-terminus, and a transmembrane helix at the carboxy-terminal region. The sub1 gene was found as single copy by Southern analysis, albeit additional serine protease related genes are annotated in the T. vaginalis genome. The expression of sub1 could only be detected by RT-PCR and Ribonuclease Protection Assays, suggesting a low abundant mRNA. The sub1 gene transcription start site was correctly assigned by RPA. The transcript abundance was found to be modulated by the availability of iron in the growth medium. Antibodies raised to a specific SUB1 peptide recognized a single protein band (~82 kDa) in Western blots, possibly representing the mature form of the protein. Immunofluorescence showed SUB1 on the trichomonad surface, and in dispersed vesicles throughout the cytoplasm. A bioinformatic analysis of genes annotated as serine proteases in the T. vaginalis genome is also presented. To our knowledge this is the first putative serine protease experimentally described for T. vaginalis.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, Protozoan - chemistry</subject><subject>Antigens, Protozoan - genetics</subject><subject>Antigens, Protozoan - immunology</subject><subject>Antigens, Protozoan - metabolism</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>cellular localization</subject><subject>Cytotoxicity</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>General aspects</subject><subject>General aspects and techniques. Study of several systematic groups. Models</subject><subject>Humans</subject><subject>Invertebrates</subject><subject>Iron - metabolism</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Parasites</subject><subject>Peptides</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - immunology</subject><subject>Protozoan Proteins - metabolism</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Sequence Analysis, DNA</subject><subject>serine protease</subject><subject>Serine Proteases - chemistry</subject><subject>Serine Proteases - genetics</subject><subject>Serine Proteases - immunology</subject><subject>Serine Proteases - metabolism</subject><subject>Sexually transmitted diseases</subject><subject>STD</subject><subject>subtilisin</subject><subject>Subtilisin - chemistry</subject><subject>Subtilisin - genetics</subject><subject>Subtilisin - immunology</subject><subject>Subtilisin - metabolism</subject><subject>surface protein</subject><subject>Trichomonas vaginalis</subject><subject>Trichomonas vaginalis - enzymology</subject><subject>Trichomonas vaginalis - genetics</subject><subject>Trichomonas vaginalis - metabolism</subject><issn>0031-1820</issn><issn>1469-8161</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNqF0U1rFTEUBuAgir1Wf4AbCYK4cTSZfM0spei10iJitd2FM5mkTTuT1CQj6q83l3ttQRGzCeQ8J5zkRegxJS8poerVJ0IYpV1LKKlL0LM7aEW57JuOSnoXrTblZlPfQw9yvqxGMtneR3stkaTtBFuh5XC0oXjnDRQfA4YwYnMBCUyxyf_cHkaHAeclOTC2gZyj8VDs-KKeDcVPPvvQTP7K4lx7gsXXKRYL2WIf8Eny5iLOMUDG3-DcB6j-IbrnYMr20W7fR5_fvjk5eNccfVgfHrw-agxXtDRctgxa1fWDcW4YuVMGKJFCAGEdUWQcmGCDdI5KOzjTEwWCUa6qda3tBdtHz7f31om-LjYXPfts7DRBsHHJuqNCMFE_479SCU5aynte5dM_5GVcUn3WBokaR0e6iugWmRRzTtbp6-RnSD80JXqTnf4ru9rzZHfxMsx2vOn4HVYFz3YAsoHJJQjG51vHmKzpy-qarfO52O83dUhXWiqmhJbrj5p_WR-_Pz4906fVs92wMA_Jj-f29kn_HvcXHf3Apw</recordid><startdate>20100901</startdate><enddate>20100901</enddate><creator>HERNÁNDEZ-ROMANO, PABLO</creator><creator>HERNÁNDEZ, ROBERTO</creator><creator>ARROYO, ROSSANA</creator><creator>ALDERETE, JOHN F.</creator><creator>LÓPEZ-VILLASEÑOR, IMELDA</creator><general>Cambridge University Press</general><scope>BSCLL</scope><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>3V.</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20100901</creationdate><title>Identification and characterization of a surface-associated, subtilisin-like serine protease in Trichomonas vaginalis</title><author>HERNÁNDEZ-ROMANO, PABLO ; HERNÁNDEZ, ROBERTO ; ARROYO, ROSSANA ; ALDERETE, JOHN F. ; LÓPEZ-VILLASEÑOR, IMELDA</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-4623a2789bcffbd4f7ca10655a038070db353b6ff16ebfc907a53147fbdf2e953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens, Protozoan - chemistry</topic><topic>Antigens, Protozoan - genetics</topic><topic>Antigens, Protozoan - immunology</topic><topic>Antigens, Protozoan - metabolism</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>cellular localization</topic><topic>Cytotoxicity</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation</topic><topic>General aspects</topic><topic>General aspects and techniques. Study of several systematic groups. Models</topic><topic>Humans</topic><topic>Invertebrates</topic><topic>Iron - metabolism</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Parasites</topic><topic>Peptides</topic><topic>Protozoan Proteins - chemistry</topic><topic>Protozoan Proteins - genetics</topic><topic>Protozoan Proteins - immunology</topic><topic>Protozoan Proteins - metabolism</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Sequence Analysis, DNA</topic><topic>serine protease</topic><topic>Serine Proteases - chemistry</topic><topic>Serine Proteases - genetics</topic><topic>Serine Proteases - immunology</topic><topic>Serine Proteases - metabolism</topic><topic>Sexually transmitted diseases</topic><topic>STD</topic><topic>subtilisin</topic><topic>Subtilisin - chemistry</topic><topic>Subtilisin - genetics</topic><topic>Subtilisin - immunology</topic><topic>Subtilisin - metabolism</topic><topic>surface protein</topic><topic>Trichomonas vaginalis</topic><topic>Trichomonas vaginalis - enzymology</topic><topic>Trichomonas vaginalis - genetics</topic><topic>Trichomonas vaginalis - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HERNÁNDEZ-ROMANO, PABLO</creatorcontrib><creatorcontrib>HERNÁNDEZ, ROBERTO</creatorcontrib><creatorcontrib>ARROYO, ROSSANA</creatorcontrib><creatorcontrib>ALDERETE, JOHN F.</creatorcontrib><creatorcontrib>LÓPEZ-VILLASEÑOR, IMELDA</creatorcontrib><collection>Istex</collection><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>ProQuest Central (Corporate)</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HERNÁNDEZ-ROMANO, PABLO</au><au>HERNÁNDEZ, ROBERTO</au><au>ARROYO, ROSSANA</au><au>ALDERETE, JOHN F.</au><au>LÓPEZ-VILLASEÑOR, IMELDA</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of a surface-associated, subtilisin-like serine protease in Trichomonas vaginalis</atitle><jtitle>Parasitology</jtitle><addtitle>Parasitology</addtitle><date>2010-09-01</date><risdate>2010</risdate><volume>137</volume><issue>11</issue><spage>1621</spage><epage>1635</epage><pages>1621-1635</pages><issn>0031-1820</issn><eissn>1469-8161</eissn><coden>PARAAE</coden><abstract>Trichomonas vaginalis is a protozoan parasite causing trichomonosis, a sexually transmitted infection in humans. This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and characterize a putative subtilisin-like serine protease (SUB1). The sub1 gene encodes a 101-kDa protein. In silico analyses predict signal and pro-peptides at the N-terminus, and a transmembrane helix at the carboxy-terminal region. The sub1 gene was found as single copy by Southern analysis, albeit additional serine protease related genes are annotated in the T. vaginalis genome. The expression of sub1 could only be detected by RT-PCR and Ribonuclease Protection Assays, suggesting a low abundant mRNA. The sub1 gene transcription start site was correctly assigned by RPA. The transcript abundance was found to be modulated by the availability of iron in the growth medium. Antibodies raised to a specific SUB1 peptide recognized a single protein band (~82 kDa) in Western blots, possibly representing the mature form of the protein. Immunofluorescence showed SUB1 on the trichomonad surface, and in dispersed vesicles throughout the cytoplasm. A bioinformatic analysis of genes annotated as serine proteases in the T. vaginalis genome is also presented. To our knowledge this is the first putative serine protease experimentally described for T. vaginalis.</abstract><cop>Cambridge, UK</cop><pub>Cambridge University Press</pub><pmid>20602853</pmid><doi>10.1017/S003118201000051X</doi><tpages>15</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Antigens, Protozoan - chemistry Antigens, Protozoan - genetics Antigens, Protozoan - immunology Antigens, Protozoan - metabolism Base Sequence Biological and medical sciences cellular localization Cytotoxicity Female Fundamental and applied biological sciences. Psychology Gene Expression Regulation General aspects General aspects and techniques. Study of several systematic groups. Models Humans Invertebrates Iron - metabolism Mice Models, Molecular Molecular Sequence Data Parasites Peptides Protozoan Proteins - chemistry Protozoan Proteins - genetics Protozoan Proteins - immunology Protozoan Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction Sequence Analysis, DNA serine protease Serine Proteases - chemistry Serine Proteases - genetics Serine Proteases - immunology Serine Proteases - metabolism Sexually transmitted diseases STD subtilisin Subtilisin - chemistry Subtilisin - genetics Subtilisin - immunology Subtilisin - metabolism surface protein Trichomonas vaginalis Trichomonas vaginalis - enzymology Trichomonas vaginalis - genetics Trichomonas vaginalis - metabolism |
title | Identification and characterization of a surface-associated, subtilisin-like serine protease in Trichomonas vaginalis |
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