Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein
ES-62 is an abundant phosphorylcholine-containing secreted glycoprotein of the filarial nematode Acanthocheilonema viteae. Using an antiserum directed against the parasite molecule, 3 cDNAs of size, ∼1.5–1.6 kbp were isolated from an A. viteae expression library. Sequence analysis in combination wit...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1999-10, Vol.104 (1), p.11-23 |
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| container_title | Molecular and biochemical parasitology |
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| creator | Harnett, William Houston, Katrina M Tate, Rothwell Garate, Teresa Apfel, Heiko Adam, Ralf Haslam, Stuart M Panico, Maria Paxton, Thanai Dell, Anne Morris, Howard Brzeski, Henry |
| description | ES-62 is an abundant phosphorylcholine-containing secreted glycoprotein of the filarial nematode
Acanthocheilonema viteae. Using an antiserum directed against the parasite molecule, 3 cDNAs of size, ∼1.5–1.6 kbp were isolated from an
A. viteae expression library. Sequence analysis in combination with N-terminal amino acid sequencing of purified ES-62 revealed that each clone contained a full-length cDNA for ES-62 corresponding to 474 amino acid residues but differed in their 5′ and 3′ untranslated regions. Characterisation of the 5′ end of ES-62 mRNA using 5′ rapid amplification of cDNA ends showed that it coded for a signal sequence. Several tryptic peptides were independently sequenced using quadruple-time-of-flight mass spectrometry and used to confirm the cDNA sequence. The mature protein was found to contain three potential N-linked glycosylation sites. Comparison of the derived amino acid sequence of ES-62 with the SwissProt database identified a sequence (between amino acid residues approximately 250 and 350 of mature ES-62) with significant similarity to several bacterial/fungal aminopeptidases. Incubation of ES-62 with leucine-7-amino-4-methylcoumarin as substrate confirmed that ES-62 possessed aminopeptidase activity. |
| doi_str_mv | 10.1016/S0166-6851(99)00113-9 |
| format | Article |
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Acanthocheilonema viteae. Using an antiserum directed against the parasite molecule, 3 cDNAs of size, ∼1.5–1.6 kbp were isolated from an
A. viteae expression library. Sequence analysis in combination with N-terminal amino acid sequencing of purified ES-62 revealed that each clone contained a full-length cDNA for ES-62 corresponding to 474 amino acid residues but differed in their 5′ and 3′ untranslated regions. Characterisation of the 5′ end of ES-62 mRNA using 5′ rapid amplification of cDNA ends showed that it coded for a signal sequence. Several tryptic peptides were independently sequenced using quadruple-time-of-flight mass spectrometry and used to confirm the cDNA sequence. The mature protein was found to contain three potential N-linked glycosylation sites. Comparison of the derived amino acid sequence of ES-62 with the SwissProt database identified a sequence (between amino acid residues approximately 250 and 350 of mature ES-62) with significant similarity to several bacterial/fungal aminopeptidases. Incubation of ES-62 with leucine-7-amino-4-methylcoumarin as substrate confirmed that ES-62 possessed aminopeptidase activity.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/S0166-6851(99)00113-9</identifier><identifier>PMID: 10589978</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Acanthocheilonema viteae ; Amino Acid Sequence ; amino acid sequences ; Aminopeptidase ; aminopeptidases ; Aminopeptidases - genetics ; Aminopeptidases - isolation & purification ; animal parasitic nematodes ; Animals ; Antibodies, Helminth ; Base Sequence ; cDNA ; complementary DNA ; Dipetalonema - enzymology ; Dipetalonema - genetics ; es-62 ; excretory-secretory products ; Female ; Filariasis ; genbank/af077194 ; Gene Library ; glycoprotein ES-62 ; glycoproteins ; Glycoproteins - genetics ; Glycoproteins - isolation & purification ; Helminth Proteins - genetics ; Helminth Proteins - isolation & purification ; messenger RNA ; Molecular Sequence Data ; n terminal sequence ; nucleotide sequences ; RNA, Helminth - genetics ; RNA, Messenger - genetics ; Secreted product ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; signal peptide</subject><ispartof>Molecular and biochemical parasitology, 1999-10, Vol.104 (1), p.11-23</ispartof><rights>1999 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-578ee0b990d3041083ff79ce30d1f9da81f411cc8feeb01e4bb25118b0f2124b3</citedby><cites>FETCH-LOGICAL-c482t-578ee0b990d3041083ff79ce30d1f9da81f411cc8feeb01e4bb25118b0f2124b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0166685199001139$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10589978$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Harnett, William</creatorcontrib><creatorcontrib>Houston, Katrina M</creatorcontrib><creatorcontrib>Tate, Rothwell</creatorcontrib><creatorcontrib>Garate, Teresa</creatorcontrib><creatorcontrib>Apfel, Heiko</creatorcontrib><creatorcontrib>Adam, Ralf</creatorcontrib><creatorcontrib>Haslam, Stuart M</creatorcontrib><creatorcontrib>Panico, Maria</creatorcontrib><creatorcontrib>Paxton, Thanai</creatorcontrib><creatorcontrib>Dell, Anne</creatorcontrib><creatorcontrib>Morris, Howard</creatorcontrib><creatorcontrib>Brzeski, Henry</creatorcontrib><title>Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>ES-62 is an abundant phosphorylcholine-containing secreted glycoprotein of the filarial nematode
Acanthocheilonema viteae. Using an antiserum directed against the parasite molecule, 3 cDNAs of size, ∼1.5–1.6 kbp were isolated from an
A. viteae expression library. Sequence analysis in combination with N-terminal amino acid sequencing of purified ES-62 revealed that each clone contained a full-length cDNA for ES-62 corresponding to 474 amino acid residues but differed in their 5′ and 3′ untranslated regions. Characterisation of the 5′ end of ES-62 mRNA using 5′ rapid amplification of cDNA ends showed that it coded for a signal sequence. Several tryptic peptides were independently sequenced using quadruple-time-of-flight mass spectrometry and used to confirm the cDNA sequence. The mature protein was found to contain three potential N-linked glycosylation sites. Comparison of the derived amino acid sequence of ES-62 with the SwissProt database identified a sequence (between amino acid residues approximately 250 and 350 of mature ES-62) with significant similarity to several bacterial/fungal aminopeptidases. Incubation of ES-62 with leucine-7-amino-4-methylcoumarin as substrate confirmed that ES-62 possessed aminopeptidase activity.</description><subject>Acanthocheilonema viteae</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Aminopeptidase</subject><subject>aminopeptidases</subject><subject>Aminopeptidases - genetics</subject><subject>Aminopeptidases - isolation & purification</subject><subject>animal parasitic nematodes</subject><subject>Animals</subject><subject>Antibodies, Helminth</subject><subject>Base Sequence</subject><subject>cDNA</subject><subject>complementary DNA</subject><subject>Dipetalonema - enzymology</subject><subject>Dipetalonema - genetics</subject><subject>es-62</subject><subject>excretory-secretory products</subject><subject>Female</subject><subject>Filariasis</subject><subject>genbank/af077194</subject><subject>Gene Library</subject><subject>glycoprotein ES-62</subject><subject>glycoproteins</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - isolation & purification</subject><subject>Helminth Proteins - genetics</subject><subject>Helminth Proteins - isolation & purification</subject><subject>messenger RNA</subject><subject>Molecular Sequence Data</subject><subject>n terminal sequence</subject><subject>nucleotide sequences</subject><subject>RNA, Helminth - genetics</subject><subject>RNA, Messenger - genetics</subject><subject>Secreted product</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>signal peptide</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcuKFTEQhoMoznH0EdSsRBetVX1NViKDNxhxMc46pJPKIdKdHJOcgfP2ZqYHcTebKqj66sL_M_YS4T0Cjh-uahibUQz4Vsp3AIhdIx-xHYqpbWTfisds9w85Y89y_g0AwzSOT9kZwiCknMSO0Y-4kDkuOnGzxODDnutguaU1hlySLj4GHl0tcr36EA90KN7qTFyb4m98OXFfW9z5usLrhQdadYmW-H45mXhIsZAPz9kTp5dML-7zObv-8vnXxbfm8ufX7xefLhvTi7Y0wySIYJYSbAc9guicm6ShDiw6abVA1yMaIxzRDEj9PLcDopjBtdj2c3fO3mx7690_R8pFrT4bWhYdKB6zGmXXoxT4IIhTP4pJQAWHDTQp5pzIqUPyq04nhaBujVB3RqhblZWU6s4IJevcq_sDx3kl-9_UpnwFXm-A01HpffJZXV-1gB209clejJX4uBFUFbvxlFQ2noIh6xOZomz0DzzxFzwTots</recordid><startdate>19991025</startdate><enddate>19991025</enddate><creator>Harnett, William</creator><creator>Houston, Katrina M</creator><creator>Tate, Rothwell</creator><creator>Garate, Teresa</creator><creator>Apfel, Heiko</creator><creator>Adam, Ralf</creator><creator>Haslam, Stuart M</creator><creator>Panico, Maria</creator><creator>Paxton, Thanai</creator><creator>Dell, Anne</creator><creator>Morris, Howard</creator><creator>Brzeski, Henry</creator><general>Elsevier B.V</general><scope>FBQ</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19991025</creationdate><title>Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein</title><author>Harnett, William ; Houston, Katrina M ; Tate, Rothwell ; Garate, Teresa ; Apfel, Heiko ; Adam, Ralf ; Haslam, Stuart M ; Panico, Maria ; Paxton, Thanai ; Dell, Anne ; Morris, Howard ; Brzeski, Henry</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-578ee0b990d3041083ff79ce30d1f9da81f411cc8feeb01e4bb25118b0f2124b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Acanthocheilonema viteae</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Aminopeptidase</topic><topic>aminopeptidases</topic><topic>Aminopeptidases - genetics</topic><topic>Aminopeptidases - isolation & purification</topic><topic>animal parasitic nematodes</topic><topic>Animals</topic><topic>Antibodies, Helminth</topic><topic>Base Sequence</topic><topic>cDNA</topic><topic>complementary DNA</topic><topic>Dipetalonema - enzymology</topic><topic>Dipetalonema - genetics</topic><topic>es-62</topic><topic>excretory-secretory products</topic><topic>Female</topic><topic>Filariasis</topic><topic>genbank/af077194</topic><topic>Gene Library</topic><topic>glycoprotein ES-62</topic><topic>glycoproteins</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - isolation & purification</topic><topic>Helminth Proteins - genetics</topic><topic>Helminth Proteins - isolation & purification</topic><topic>messenger RNA</topic><topic>Molecular Sequence Data</topic><topic>n terminal sequence</topic><topic>nucleotide sequences</topic><topic>RNA, Helminth - genetics</topic><topic>RNA, Messenger - genetics</topic><topic>Secreted product</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>signal peptide</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Harnett, William</creatorcontrib><creatorcontrib>Houston, Katrina M</creatorcontrib><creatorcontrib>Tate, Rothwell</creatorcontrib><creatorcontrib>Garate, Teresa</creatorcontrib><creatorcontrib>Apfel, Heiko</creatorcontrib><creatorcontrib>Adam, Ralf</creatorcontrib><creatorcontrib>Haslam, Stuart M</creatorcontrib><creatorcontrib>Panico, Maria</creatorcontrib><creatorcontrib>Paxton, Thanai</creatorcontrib><creatorcontrib>Dell, Anne</creatorcontrib><creatorcontrib>Morris, Howard</creatorcontrib><creatorcontrib>Brzeski, Henry</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Harnett, William</au><au>Houston, Katrina M</au><au>Tate, Rothwell</au><au>Garate, Teresa</au><au>Apfel, Heiko</au><au>Adam, Ralf</au><au>Haslam, Stuart M</au><au>Panico, Maria</au><au>Paxton, Thanai</au><au>Dell, Anne</au><au>Morris, Howard</au><au>Brzeski, Henry</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1999-10-25</date><risdate>1999</risdate><volume>104</volume><issue>1</issue><spage>11</spage><epage>23</epage><pages>11-23</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><abstract>ES-62 is an abundant phosphorylcholine-containing secreted glycoprotein of the filarial nematode
Acanthocheilonema viteae. Using an antiserum directed against the parasite molecule, 3 cDNAs of size, ∼1.5–1.6 kbp were isolated from an
A. viteae expression library. Sequence analysis in combination with N-terminal amino acid sequencing of purified ES-62 revealed that each clone contained a full-length cDNA for ES-62 corresponding to 474 amino acid residues but differed in their 5′ and 3′ untranslated regions. Characterisation of the 5′ end of ES-62 mRNA using 5′ rapid amplification of cDNA ends showed that it coded for a signal sequence. Several tryptic peptides were independently sequenced using quadruple-time-of-flight mass spectrometry and used to confirm the cDNA sequence. The mature protein was found to contain three potential N-linked glycosylation sites. Comparison of the derived amino acid sequence of ES-62 with the SwissProt database identified a sequence (between amino acid residues approximately 250 and 350 of mature ES-62) with significant similarity to several bacterial/fungal aminopeptidases. Incubation of ES-62 with leucine-7-amino-4-methylcoumarin as substrate confirmed that ES-62 possessed aminopeptidase activity.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>10589978</pmid><doi>10.1016/S0166-6851(99)00113-9</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0166-6851 |
| ispartof | Molecular and biochemical parasitology, 1999-10, Vol.104 (1), p.11-23 |
| issn | 0166-6851 1872-9428 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Acanthocheilonema viteae Amino Acid Sequence amino acid sequences Aminopeptidase aminopeptidases Aminopeptidases - genetics Aminopeptidases - isolation & purification animal parasitic nematodes Animals Antibodies, Helminth Base Sequence cDNA complementary DNA Dipetalonema - enzymology Dipetalonema - genetics es-62 excretory-secretory products Female Filariasis genbank/af077194 Gene Library glycoprotein ES-62 glycoproteins Glycoproteins - genetics Glycoproteins - isolation & purification Helminth Proteins - genetics Helminth Proteins - isolation & purification messenger RNA Molecular Sequence Data n terminal sequence nucleotide sequences RNA, Helminth - genetics RNA, Messenger - genetics Secreted product Sequence Analysis, DNA Sequence Homology, Amino Acid signal peptide |
| title | Molecular cloning and demonstration of an aminopeptidase activity in a filarial nematode glycoprotein |
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