Characterisation of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae
The major excretory-secretory product of the rodent filarial nematode Acanthocheilonema viteae is a 62 kDa glycoprotein (ES-62), which has phosphorylcholine, attached to the N-linked carbohydrates. In this paper, we describe structural studies of N-glycans released from ES-62 by peptide N-glycosidas...
Gespeichert in:
| Veröffentlicht in: | Molecular and biochemical parasitology 1997-03, Vol.85 (1), p.53-66 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 66 |
|---|---|
| container_issue | 1 |
| container_start_page | 53 |
| container_title | Molecular and biochemical parasitology |
| container_volume | 85 |
| creator | Haslam, S M Khoo, K H Houston, K M Harnett, W Morris, H R Dell, A |
| description | The major excretory-secretory product of the rodent filarial nematode Acanthocheilonema viteae is a 62 kDa glycoprotein (ES-62), which has phosphorylcholine, attached to the N-linked carbohydrates. In this paper, we describe structural studies of N-glycans released from ES-62 by peptide N-glycosidase F. Three major classes of N-glycan structures were observed: high mannose type structures; those which had been fully trimmed to the trimannosyl core and were sub-stoichiometrically fucosylated; and those with a trimannosyl core, with and without core fucosylation, carrying between one and four additional N-acetylglucosamine resides. Of the three classes of glycans, only the last was found to be substituted with detectable levels of phosphorylcholine. The implications of these results with respect to the probable glycosylation pathways operating in A. viteae are discussed. |
| doi_str_mv | 10.1016/S0166-6851(96)02807-1 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_78940013</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>78940013</sourcerecordid><originalsourceid>FETCH-LOGICAL-c356t-cf539ab8b06912f214d6600ad31f665cbce3eafa01ea740b927e1b2db7946b7b3</originalsourceid><addsrcrecordid>eNo9UclOwzAQ9QEEZfmESj4hOATsLE5yRGWVEByAszV2Jo0htYvtIvop_C2mVBxm0cy8N6N5hEw5O-eMi4vn5EQmmoqftuKM5Q2rM75DJv_lfXIQwhtjrKqF2CN7LWdNVTYT8j0bwIOO6E2AaJylrqdxQLocXEjm16Me3GgsZtrZCMYaO6ePWaq8Y0dTZ-4CaJ1YTIeBGrtB45f2GBM6C7jNqMjp-xXQ-bjWbuldRLNZdqnBxsHpAc3oLC6AfpqIgEdkt4cx4PE2HpLXm-uX2V328HR7P7t8yHRRiZjpvipaUI1iouV5n_OyE4Ix6AreC1FppbFA6IFxhLpkqs1r5CrvVN2WQtWqOCQnf7zppo8VhigXJmgcR7DoVkHWTVsyxos0WP0Nau9C8NjLpTcL8GvJmfyVQW5kkL__lq2QGxkkT7jpdsFKLbD7R201KH4Ac1OKLg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>78940013</pqid></control><display><type>article</type><title>Characterisation of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Haslam, S M ; Khoo, K H ; Houston, K M ; Harnett, W ; Morris, H R ; Dell, A</creator><creatorcontrib>Haslam, S M ; Khoo, K H ; Houston, K M ; Harnett, W ; Morris, H R ; Dell, A</creatorcontrib><description>The major excretory-secretory product of the rodent filarial nematode Acanthocheilonema viteae is a 62 kDa glycoprotein (ES-62), which has phosphorylcholine, attached to the N-linked carbohydrates. In this paper, we describe structural studies of N-glycans released from ES-62 by peptide N-glycosidase F. Three major classes of N-glycan structures were observed: high mannose type structures; those which had been fully trimmed to the trimannosyl core and were sub-stoichiometrically fucosylated; and those with a trimannosyl core, with and without core fucosylation, carrying between one and four additional N-acetylglucosamine resides. Of the three classes of glycans, only the last was found to be substituted with detectable levels of phosphorylcholine. The implications of these results with respect to the probable glycosylation pathways operating in A. viteae are discussed.</description><identifier>ISSN: 0166-6851</identifier><identifier>DOI: 10.1016/S0166-6851(96)02807-1</identifier><identifier>PMID: 9108548</identifier><language>eng</language><publisher>Netherlands</publisher><subject>Animals ; Carbohydrate Sequence ; Dipetalonema - chemistry ; Gas Chromatography-Mass Spectrometry ; Glycoproteins - chemistry ; Helminth Proteins - chemistry ; Hydrofluoric Acid ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides - biosynthesis ; Oligosaccharides - chemistry ; Phosphorylcholine ; Sequence Analysis ; Spectrometry, Mass, Fast Atom Bombardment</subject><ispartof>Molecular and biochemical parasitology, 1997-03, Vol.85 (1), p.53-66</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-cf539ab8b06912f214d6600ad31f665cbce3eafa01ea740b927e1b2db7946b7b3</citedby><cites>FETCH-LOGICAL-c356t-cf539ab8b06912f214d6600ad31f665cbce3eafa01ea740b927e1b2db7946b7b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9108548$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haslam, S M</creatorcontrib><creatorcontrib>Khoo, K H</creatorcontrib><creatorcontrib>Houston, K M</creatorcontrib><creatorcontrib>Harnett, W</creatorcontrib><creatorcontrib>Morris, H R</creatorcontrib><creatorcontrib>Dell, A</creatorcontrib><title>Characterisation of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>The major excretory-secretory product of the rodent filarial nematode Acanthocheilonema viteae is a 62 kDa glycoprotein (ES-62), which has phosphorylcholine, attached to the N-linked carbohydrates. In this paper, we describe structural studies of N-glycans released from ES-62 by peptide N-glycosidase F. Three major classes of N-glycan structures were observed: high mannose type structures; those which had been fully trimmed to the trimannosyl core and were sub-stoichiometrically fucosylated; and those with a trimannosyl core, with and without core fucosylation, carrying between one and four additional N-acetylglucosamine resides. Of the three classes of glycans, only the last was found to be substituted with detectable levels of phosphorylcholine. The implications of these results with respect to the probable glycosylation pathways operating in A. viteae are discussed.</description><subject>Animals</subject><subject>Carbohydrate Sequence</subject><subject>Dipetalonema - chemistry</subject><subject>Gas Chromatography-Mass Spectrometry</subject><subject>Glycoproteins - chemistry</subject><subject>Helminth Proteins - chemistry</subject><subject>Hydrofluoric Acid</subject><subject>Models, Biological</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Oligosaccharides - biosynthesis</subject><subject>Oligosaccharides - chemistry</subject><subject>Phosphorylcholine</subject><subject>Sequence Analysis</subject><subject>Spectrometry, Mass, Fast Atom Bombardment</subject><issn>0166-6851</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9UclOwzAQ9QEEZfmESj4hOATsLE5yRGWVEByAszV2Jo0htYvtIvop_C2mVBxm0cy8N6N5hEw5O-eMi4vn5EQmmoqftuKM5Q2rM75DJv_lfXIQwhtjrKqF2CN7LWdNVTYT8j0bwIOO6E2AaJylrqdxQLocXEjm16Me3GgsZtrZCMYaO6ePWaq8Y0dTZ-4CaJ1YTIeBGrtB45f2GBM6C7jNqMjp-xXQ-bjWbuldRLNZdqnBxsHpAc3oLC6AfpqIgEdkt4cx4PE2HpLXm-uX2V328HR7P7t8yHRRiZjpvipaUI1iouV5n_OyE4Ix6AreC1FppbFA6IFxhLpkqs1r5CrvVN2WQtWqOCQnf7zppo8VhigXJmgcR7DoVkHWTVsyxos0WP0Nau9C8NjLpTcL8GvJmfyVQW5kkL__lq2QGxkkT7jpdsFKLbD7R201KH4Ac1OKLg</recordid><startdate>199703</startdate><enddate>199703</enddate><creator>Haslam, S M</creator><creator>Khoo, K H</creator><creator>Houston, K M</creator><creator>Harnett, W</creator><creator>Morris, H R</creator><creator>Dell, A</creator><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>7X8</scope></search><sort><creationdate>199703</creationdate><title>Characterisation of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae</title><author>Haslam, S M ; Khoo, K H ; Houston, K M ; Harnett, W ; Morris, H R ; Dell, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-cf539ab8b06912f214d6600ad31f665cbce3eafa01ea740b927e1b2db7946b7b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Carbohydrate Sequence</topic><topic>Dipetalonema - chemistry</topic><topic>Gas Chromatography-Mass Spectrometry</topic><topic>Glycoproteins - chemistry</topic><topic>Helminth Proteins - chemistry</topic><topic>Hydrofluoric Acid</topic><topic>Models, Biological</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Oligosaccharides - biosynthesis</topic><topic>Oligosaccharides - chemistry</topic><topic>Phosphorylcholine</topic><topic>Sequence Analysis</topic><topic>Spectrometry, Mass, Fast Atom Bombardment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haslam, S M</creatorcontrib><creatorcontrib>Khoo, K H</creatorcontrib><creatorcontrib>Houston, K M</creatorcontrib><creatorcontrib>Harnett, W</creatorcontrib><creatorcontrib>Morris, H R</creatorcontrib><creatorcontrib>Dell, A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haslam, S M</au><au>Khoo, K H</au><au>Houston, K M</au><au>Harnett, W</au><au>Morris, H R</au><au>Dell, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterisation of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1997-03</date><risdate>1997</risdate><volume>85</volume><issue>1</issue><spage>53</spage><epage>66</epage><pages>53-66</pages><issn>0166-6851</issn><abstract>The major excretory-secretory product of the rodent filarial nematode Acanthocheilonema viteae is a 62 kDa glycoprotein (ES-62), which has phosphorylcholine, attached to the N-linked carbohydrates. In this paper, we describe structural studies of N-glycans released from ES-62 by peptide N-glycosidase F. Three major classes of N-glycan structures were observed: high mannose type structures; those which had been fully trimmed to the trimannosyl core and were sub-stoichiometrically fucosylated; and those with a trimannosyl core, with and without core fucosylation, carrying between one and four additional N-acetylglucosamine resides. Of the three classes of glycans, only the last was found to be substituted with detectable levels of phosphorylcholine. The implications of these results with respect to the probable glycosylation pathways operating in A. viteae are discussed.</abstract><cop>Netherlands</cop><pmid>9108548</pmid><doi>10.1016/S0166-6851(96)02807-1</doi><tpages>14</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0166-6851 |
| ispartof | Molecular and biochemical parasitology, 1997-03, Vol.85 (1), p.53-66 |
| issn | 0166-6851 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78940013 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Carbohydrate Sequence Dipetalonema - chemistry Gas Chromatography-Mass Spectrometry Glycoproteins - chemistry Helminth Proteins - chemistry Hydrofluoric Acid Models, Biological Models, Molecular Molecular Sequence Data Oligosaccharides - biosynthesis Oligosaccharides - chemistry Phosphorylcholine Sequence Analysis Spectrometry, Mass, Fast Atom Bombardment |
| title | Characterisation of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T12%3A09%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterisation%20of%20the%20phosphorylcholine-containing%20N-linked%20oligosaccharides%20in%20the%20excretory-secretory%2062%20kDa%20glycoprotein%20of%20Acanthocheilonema%20viteae&rft.jtitle=Molecular%20and%20biochemical%20parasitology&rft.au=Haslam,%20S%20M&rft.date=1997-03&rft.volume=85&rft.issue=1&rft.spage=53&rft.epage=66&rft.pages=53-66&rft.issn=0166-6851&rft_id=info:doi/10.1016/S0166-6851(96)02807-1&rft_dat=%3Cproquest_cross%3E78940013%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=78940013&rft_id=info:pmid/9108548&rfr_iscdi=true |