Plant N-glycan profiling of minute amounts of material
Development of convenient strategies for identification of plant N-glycan profiles has been driven by the emergence of plants as an expression system for therapeutic proteins. In this article, we reinvestigated qualitative and quantitative aspects of plant N-glycan profiling. The extraction of plant...
Saved in:
| Published in | Analytical biochemistry Vol. 379; no. 1; pp. 66 - 72 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
01.08.2008
Elsevier Masson |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0003-2697 1096-0309 1096-0309 |
| DOI | 10.1016/j.ab.2008.04.034 |
Cover
| Abstract | Development of convenient strategies for identification of plant
N-glycan profiles has been driven by the emergence of plants as an expression system for therapeutic proteins. In this article, we reinvestigated qualitative and quantitative aspects of plant
N-glycan profiling. The extraction of plant proteins through a phenol/ammonium acetate procedure followed by deglycosylation with peptide
N-glycosidase A (PNGase A) and coupling to 2-aminobenzamide provides an oligosaccharide preparation containing reduced amounts of contaminants from plant cell wall polysaccharides. Such a preparation was also suitable for accurate qualitative and quantitative evaluation of the
N-glycan content by mass spectrometry. Combining these approaches allows the profiling to be carried out from as low as 500
mg of fresh leaf material. We also demonstrated that collision-induced dissociation (CID) mass spectrometry in negative mode of
N-glycans harboring α(1,3)- or α(1,6)-fucose residue on the proximal GlcNAc leads to specific fragmentation patterns, thereby allowing the discrimination of plant
N-glycans from those arising from mammalian contamination. |
|---|---|
| AbstractList | Development of convenient strategies for identification of plant N-glycan profiles has been driven by the emergence of plants as an expression system for therapeutic proteins. In this article, we reinvestigated qualitative and quantitative aspects of plant N-glycan profiling. The extraction of plant proteins through a phenol/ammonium acetate procedure followed by deglycosylation with peptide N-glycosidase A (PNGase A) and coupling to 2-aminobenzamide provides an oligosaccharide preparation containing reduced amounts of contaminants from plant cell wall polysaccharides. Such a preparation was also suitable for accurate qualitative and quantitative evaluation of the N-glycan content by mass spectrometry. Combining these approaches allows the profiling to be carried out from as low as 500 mg of fresh leaf material. We also demonstrated that collision-induced dissociation (CID) mass spectrometry in negative mode of N-glycans harboring alpha(1,3)- or alpha(1,6)-fucose residue on the proximal GlcNAc leads to specific fragmentation patterns, thereby allowing the discrimination of plant N-glycans from those arising from mammalian contamination. Development of convenient strategies for identification of plant N-glycan profiles has been driven by the emergence of plants as an expression system for therapeutic proteins. In this article, we reinvestigated qualitative and quantitative aspects of plant N-glycan profiling. The extraction of plant proteins through a phenol/ammonium acetate procedure followed by deglycosylation with peptide N-glycosidase A (PNGase A) and coupling to 2-aminobenzamide provides an oligosaccharide preparation containing reduced amounts of contaminants from plant cell wall polysaccharides. Such a preparation was also suitable for accurate qualitative and quantitative evaluation of the N-glycan content by mass spectrometry. Combining these approaches allows the profiling to be carried out from as low as 500 mg of fresh leaf material. We also demonstrated that collision-induced dissociation (CID) mass spectrometry in negative mode of N-glycans harboring alpha(1,3)- or alpha(1,6)-fucose residue on the proximal GlcNAc leads to specific fragmentation patterns, thereby allowing the discrimination of plant N-glycans from those arising from mammalian contamination.Development of convenient strategies for identification of plant N-glycan profiles has been driven by the emergence of plants as an expression system for therapeutic proteins. In this article, we reinvestigated qualitative and quantitative aspects of plant N-glycan profiling. The extraction of plant proteins through a phenol/ammonium acetate procedure followed by deglycosylation with peptide N-glycosidase A (PNGase A) and coupling to 2-aminobenzamide provides an oligosaccharide preparation containing reduced amounts of contaminants from plant cell wall polysaccharides. Such a preparation was also suitable for accurate qualitative and quantitative evaluation of the N-glycan content by mass spectrometry. Combining these approaches allows the profiling to be carried out from as low as 500 mg of fresh leaf material. We also demonstrated that collision-induced dissociation (CID) mass spectrometry in negative mode of N-glycans harboring alpha(1,3)- or alpha(1,6)-fucose residue on the proximal GlcNAc leads to specific fragmentation patterns, thereby allowing the discrimination of plant N-glycans from those arising from mammalian contamination. Development of convenient strategies for identification of plant N-glycan profiles has been driven by the emergence of plants as an expression system for therapeutic proteins. In this article, we reinvestigated qualitative and quantitative aspects of plant N-glycan profiling. The extraction of plant proteins through a phenol/ammonium acetate procedure followed by deglycosylation with peptide N-glycosidase A (PNGase A) and coupling to 2-aminobenzamide provides an oligosaccharide preparation containing reduced amounts of contaminants from plant cell wall polysaccharides. Such a preparation was also suitable for accurate qualitative and quantitative evaluation of the N-glycan content by mass spectrometry. Combining these approaches allows the profiling to be carried out from as low as 500 mg of fresh leaf material. We also demonstrated that collision-induced dissociation (CID) mass spectrometry in negative mode of N-glycans harboring α(1,3)- or α(1,6)-fucose residue on the proximal GlcNAc leads to specific fragmentation patterns, thereby allowing the discrimination of plant N-glycans from those arising from mammalian contamination. |
| Author | Vézina, Louis-Philippe Royle, L. Rudd, Pauline M. Séveno, Martial Dwek, Raymond A. Cremata, José A. Burel, Carole Cabrera, Gleysin Lerouge, Patrice Bardor, Muriel Rihouey, Christophe Leprince, Jérome Harvey, David J. D’Aoust, Marc-André Triguero, Ada |
| Author_xml | – sequence: 1 givenname: Martial surname: Séveno fullname: Séveno, Martial organization: CNRS–FRE 3090, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cédex, France – sequence: 2 givenname: Gleysin surname: Cabrera fullname: Cabrera, Gleysin organization: Department of Carbohydrate Chemistry, Center for Genetic Engineering and Biotechnology (CIGB), Havana 10600, Cuba – sequence: 3 givenname: Ada surname: Triguero fullname: Triguero, Ada organization: Department of Carbohydrate Chemistry, Center for Genetic Engineering and Biotechnology (CIGB), Havana 10600, Cuba – sequence: 4 givenname: Carole surname: Burel fullname: Burel, Carole organization: CNRS–FRE 3090, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cédex, France – sequence: 5 givenname: Jérome surname: Leprince fullname: Leprince, Jérome organization: INSERM U 413, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cédex, France – sequence: 6 givenname: Christophe surname: Rihouey fullname: Rihouey, Christophe organization: CNRS–FRE 3090, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cédex, France – sequence: 7 givenname: Louis-Philippe surname: Vézina fullname: Vézina, Louis-Philippe organization: Medicago Inc., Québec, QC G1V 3V9, Canada – sequence: 8 givenname: Marc-André surname: D’Aoust fullname: D’Aoust, Marc-André organization: Medicago Inc., Québec, QC G1V 3V9, Canada – sequence: 9 givenname: Pauline M. surname: Rudd fullname: Rudd, Pauline M. organization: Oxford Glycobiology Institute, University of Oxford, Oxford OX1 3QU, UK – sequence: 10 givenname: L. surname: Royle fullname: Royle, L. organization: Oxford Glycobiology Institute, University of Oxford, Oxford OX1 3QU, UK – sequence: 11 givenname: Raymond A. surname: Dwek fullname: Dwek, Raymond A. organization: Oxford Glycobiology Institute, University of Oxford, Oxford OX1 3QU, UK – sequence: 12 givenname: David J. surname: Harvey fullname: Harvey, David J. organization: Oxford Glycobiology Institute, University of Oxford, Oxford OX1 3QU, UK – sequence: 13 givenname: Patrice surname: Lerouge fullname: Lerouge, Patrice email: patrice.lerouge@univ-rouen.fr organization: CNRS–FRE 3090, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cédex, France – sequence: 14 givenname: José A. surname: Cremata fullname: Cremata, José A. organization: Department of Carbohydrate Chemistry, Center for Genetic Engineering and Biotechnology (CIGB), Havana 10600, Cuba – sequence: 15 givenname: Muriel surname: Bardor fullname: Bardor, Muriel email: muriel.bardor@univ-rouen.fr organization: CNRS–FRE 3090, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cédex, France |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18482571$$D View this record in MEDLINE/PubMed https://normandie-univ.hal.science/hal-01974002$$DView record in HAL |
| BookMark | eNp1kE1r3DAURUVJaSYf-66KV4Uu7D7Jsmx1F0KTFIa2i3YtZPkp1WBLqSQH8u-rySRZFLJ6cDn3wjsn5MgHj4S8p9BQoOLzrtFjwwCGBngDLX9DNhSkqKEFeUQ2ANDWTMj-mJyktAOglHfiHTmmAx9Y19MNET9n7XP1vb6dH4z21V0M1s3O31bBVovza8ZKL2H1OT0mOmN0ej4jb62eE54_3VPy--rrr8ubevvj-tvlxbY27cByPfWUdtD12PLOskl3zAo9snYYrdVWjJybCQSnbByM7KSQUmrDLKfYIRfT1J6ST4fdP3pWd9EtOj6ooJ26udiqfQZU9hyA3dPCfjyw5Ye_K6asFpcMzuVBDGtSQjIGRVsBPzyB67jg9LL7bKUA4gCYGFKKaJVxWWcXfI7azYqC2utXO6VHtdevgKuivxThv-LL9uuVL4cKFo33DqNKxqE3OLmIJqspuNfL_wDYypki |
| CitedBy_id | crossref_primary_10_1002_mas_21622 crossref_primary_10_1146_annurev_arplant_042110_103918 crossref_primary_10_1038_s41598_017_10698_z crossref_primary_10_1002_biot_201200078 crossref_primary_10_1074_mcp_M113_028191 crossref_primary_10_1016_j_ab_2008_09_041 crossref_primary_10_1002_pmic_200900514 crossref_primary_10_1021_ac900231w crossref_primary_10_1016_j_intimp_2013_06_013 crossref_primary_10_1016_j_ijms_2022_116917 crossref_primary_10_1016_j_jprot_2012_05_013 crossref_primary_10_3390_molecules28041843 crossref_primary_10_1002_elps_201200622 crossref_primary_10_1016_j_ab_2010_01_027 crossref_primary_10_1002_mas_20333 crossref_primary_10_1128_mBio_01527_14 crossref_primary_10_1007_s11240_017_1309_1 crossref_primary_10_1074_jbc_M110_175711 |
| Cites_doi | 10.1038/nbt1104-1351 10.1073/pnas.031419998 10.1093/glycob/cwg024 10.1016/S0014-5793(04)00150-4 10.1111/j.1467-7652.2004.00062.x 10.1111/j.1467-7652.2004.00078.x 10.1016/j.sbi.2006.08.009 10.1104/pp.119.2.725 10.1016/j.jasms.2005.01.006 10.1111/j.1467-7652.2004.00100.x 10.1021/bi0204701 10.1016/j.jasms.2005.01.004 10.1007/s00425-005-0206-8 10.1073/pnas.0832472100 10.1093/oxfordjournals.jbchem.a134585 10.1111/j.1467-7652.2005.00137.x 10.1111/j.1365-313X.2005.02648.x 10.1023/A:1006012005654 10.1023/B:GLYC.0000045099.29038.04 10.1093/glycob/9.4.365 10.1016/S0021-9258(20)64302-2 10.1046/j.1467-7652.2003.00041.x 10.1073/pnas.0600879103 10.1093/glycob/cwj071 10.1073/pnas.96.8.4692 10.1007/BF00020889 10.1111/j.1467-7652.2006.00211.x 10.1016/j.abb.2004.02.034 10.1002/1522-2683(20000701)21:12<2550::AID-ELPS2550>3.0.CO;2-G 10.1021/ac0614137 |
| ContentType | Journal Article |
| Copyright | 2008 Elsevier Inc. Distributed under a Creative Commons Attribution 4.0 International License |
| Copyright_xml | – notice: 2008 Elsevier Inc. – notice: Distributed under a Creative Commons Attribution 4.0 International License |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 1XC |
| DOI | 10.1016/j.ab.2008.04.034 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic Hyper Article en Ligne (HAL) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry |
| EISSN | 1096-0309 |
| EndPage | 72 |
| ExternalDocumentID | oai_HAL_hal_01974002v1 18482571 10_1016_j_ab_2008_04_034 S0003269708002613 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GrantInformation_xml | – fundername: Wellcome Trust |
| GroupedDBID | --- --K --M -~X .55 .GJ .~1 0R~ 1B1 1RT 1~. 1~5 23M 4.4 457 4G. 53G 5GY 5VS 6J9 7-5 71M 85S 8P~ 9JM 9JN AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AARLI AAXUO ABEFU ABFNM ABFRF ABGSF ABMAC ABOCM ABTAH ABUDA ABXDB ABYKQ ACDAQ ACGFO ACKIV ACNCT ACNNM ACRLP ADBBV ADECG ADEZE ADFGL ADIYS ADMUD ADRHT ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFTJW AFXIZ AFZHZ AGHFR AGRDE AGUBO AGYEJ AHHHB AHPSJ AI. AIEXJ AIKHN AITUG AJBFU AJOXV AJSZI ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CAG COF CS3 DM4 DOVZS EBS EFBJH EFLBG EJD EO8 EO9 EP2 EP3 F5P FA8 FDB FEDTE FGOYB FIRID FLBIZ FNPLU FYGXN G-2 G-Q G8K GBLVA HLW HVGLF HZ~ H~9 IHE J1W J5H K-O KOM L7B LG5 LX2 M41 MO0 MVM N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 R2- RIG RNS ROL RPZ SBG SCB SCC SDF SDG SDP SES SEW SPC SPCBC SSK SSU SSZ T5K VH1 WH7 WUQ X7M XFK XOL XPP Y6R YYP ZA5 ZGI ZKB ZMT ZY4 AAHBH AATTM AAXKI AAYWO AAYXX ABDPE ABWVN ACRPL ACVFH ADCNI ADNMO ADVLN ADXHL AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH CGR CUY CVF ECM EIF NPM 7X8 EFKBS 1XC UMC |
| ID | FETCH-LOGICAL-c382t-d7115057e345f2da52f6ab238bffaf6b44cd06412b8c9596999ac2f41e5e46dd3 |
| IEDL.DBID | .~1 |
| ISSN | 0003-2697 1096-0309 |
| IngestDate | Fri May 09 12:12:55 EDT 2025 Fri Sep 05 03:44:37 EDT 2025 Thu Apr 03 07:05:38 EDT 2025 Tue Jul 01 03:43:05 EDT 2025 Thu Apr 24 22:50:27 EDT 2025 Fri Feb 23 02:13:34 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Keywords | N-Glycan profiling Plant glycosylation Therapeutic protein Glycoprotein |
| Language | English |
| License | https://www.elsevier.com/tdm/userlicense/1.0 Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0 |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c382t-d7115057e345f2da52f6ab238bffaf6b44cd06412b8c9596999ac2f41e5e46dd3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ORCID | 0000-0002-5000-8735 0000-0002-7814-9927 0000-0002-0966-903X 0000-0001-9989-2245 |
| PMID | 18482571 |
| PQID | 69220101 |
| PQPubID | 23479 |
| PageCount | 7 |
| ParticipantIDs | hal_primary_oai_HAL_hal_01974002v1 proquest_miscellaneous_69220101 pubmed_primary_18482571 crossref_citationtrail_10_1016_j_ab_2008_04_034 crossref_primary_10_1016_j_ab_2008_04_034 elsevier_sciencedirect_doi_10_1016_j_ab_2008_04_034 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2008-08-01 |
| PublicationDateYYYYMMDD | 2008-08-01 |
| PublicationDate_xml | – month: 08 year: 2008 text: 2008-08-01 day: 01 |
| PublicationDecade | 2000 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Analytical biochemistry |
| PublicationTitleAlternate | Anal Biochem |
| PublicationYear | 2008 |
| Publisher | Elsevier Inc Elsevier Masson |
| Publisher_xml | – name: Elsevier Inc – name: Elsevier Masson |
| References | Sriraman, Bardor, Sack, Vaquero, Faye, Fischer, Finnern, Lerouge (bib9) 2004; 2 Bardor, Loutelier-Bourhis, Paccalet, Cosette, Fitchette, Vezina, Trepanier, Dargis, Lemieux, Lange, Faye, Lerouge (bib31) 2003; 1 Kurosaka, Yano, Itoh, Kuroda, Nakagawa, Kawasaki (bib29) 1991; 266 Lerouge, Cabanes-Macheteau, Rayon, Fitchette-Lainé, Gomord, Faye (bib1) 1998; 38 Bakker, Bardor, Molhoff, Gomord, Elbers, Stevens, Jordi, Lommen, Faye, Lerouge, Bosch (bib15) 2001; 98 Paccalet, Bardor, Rihouey, Aquin, D’Aoust, Faye, Vézina, Gomord, Lerouge (bib17) 2007; 5 Bardor, Cabrera, Rudd, Dwek, Cremata, Lerouge (bib26) 2006; 16 Matsumoto, Ikura, Ueda, Sasaki (bib7) 1995; 27 Palacpac, Yoshida, Sakai, Kimura, Fujiyama, Yoshida, Seki (bib14) 1999; 96 Rayon, Cabanes-Macheteau, Loutelier-Bourrhis, Saliot-Maire, Lemoine, Reiter, Lerouge, Faye (bib19) 1999; 119 Strasser, Schoberer, Jin, Glossl, Mach, Steinkellner (bib25) 2006; 45 Tekoah, Ko, Koprowski, Harvey, Wormald, Dwek, Rudd (bib10) 2004; 426 Zeleny, Kolarich, Strasser, Altmann (bib6) 2006; 224 Navazio, Miuzzo, Royle, Baldan, Varotto, Merry, Harvey, Dwek, Rudd, Mariani (bib23) 2002; 41 Bakker, Rouwendal, Karnoup, Florack, Stoopen, Helsper, van Ree, van Die, Bosch (bib16) 2006; 103 Strasser, Altmann, Gloss, Steinkellner (bib24) 2004; 21 Triguero, Cabrera, Cremata, Yuen, Wheeler, Ramirez (bib11) 2005; 3 Lemoine, Cabanes-Macheteau, Bardor, Michalski, Faye, Lerouge (bib22) 2000; 14 Séveno, Bardor, Paccalet, Gomord, Lerouge, Faye (bib5) 2004; 22 Ko, Tekoah, Rudd, Harvey, Dwek, Spitsin, Hanlon, Rupprecht, Dietzschold, Golovkin, Koprowski (bib8) 2003; 101 Harvey (bib30) 2005; 16 Strasser, Altmann, Mach, Glossl, Steinkellner (bib12) 2004; 561 Fitchette, Tran Dinh, Faye, Bardor (bib27) 2006 Bardor, Cabanes-Macheteau, Faye, Lerouge (bib21) 2000; 21 Royle, Radcliffe, Dwek, Rudd (bib28) 2006 Jin, Bencúrová, Borth, Ferko, Jensen-Jarolin, Altmann, Hantusch (bib4) 2006; 16 Koprivova, Stemmer, Altmann, Hoffmann, Kopriva, Gorr, Reski, Decker (bib13) 2004; 2 Maslen, Sadowski, Adam, Lilley, Stephens (bib33) 2006; 78 Hase, Ibuki, Ikenaka (bib18) 1984; 95 Bardor, Faveeuw, Fitchette, Gilbert, Galas, Trottein, Faye, Lerouge (bib3) 2003; 13 Cabanes-Macheteau, Fitchette-Laine, Loutelier-Bourhis, Lange, Vine, Ma, Lerouge, Faye (bib20) 1999; 9 Gomord, Sourouille, Fitchette, Bardor, Pagny, Lerouge, Faye (bib2) 2004; 2 Harvey (bib32) 2005; 16 Lemoine (10.1016/j.ab.2008.04.034_bib22) 2000; 14 Fitchette (10.1016/j.ab.2008.04.034_bib27) 2006 Bardor (10.1016/j.ab.2008.04.034_bib31) 2003; 1 Lerouge (10.1016/j.ab.2008.04.034_bib1) 1998; 38 Koprivova (10.1016/j.ab.2008.04.034_bib13) 2004; 2 Royle (10.1016/j.ab.2008.04.034_bib28) 2006 Jin (10.1016/j.ab.2008.04.034_bib4) 2006; 16 Zeleny (10.1016/j.ab.2008.04.034_bib6) 2006; 224 Hase (10.1016/j.ab.2008.04.034_bib18) 1984; 95 Gomord (10.1016/j.ab.2008.04.034_bib2) 2004; 2 Navazio (10.1016/j.ab.2008.04.034_bib23) 2002; 41 Rayon (10.1016/j.ab.2008.04.034_bib19) 1999; 119 Matsumoto (10.1016/j.ab.2008.04.034_bib7) 1995; 27 Tekoah (10.1016/j.ab.2008.04.034_bib10) 2004; 426 Harvey (10.1016/j.ab.2008.04.034_bib32) 2005; 16 Sriraman (10.1016/j.ab.2008.04.034_bib9) 2004; 2 Triguero (10.1016/j.ab.2008.04.034_bib11) 2005; 3 Bardor (10.1016/j.ab.2008.04.034_bib3) 2003; 13 Palacpac (10.1016/j.ab.2008.04.034_bib14) 1999; 96 Bakker (10.1016/j.ab.2008.04.034_bib15) 2001; 98 Harvey (10.1016/j.ab.2008.04.034_bib30) 2005; 16 Strasser (10.1016/j.ab.2008.04.034_bib24) 2004; 21 Bakker (10.1016/j.ab.2008.04.034_bib16) 2006; 103 Bardor (10.1016/j.ab.2008.04.034_bib26) 2006; 16 Paccalet (10.1016/j.ab.2008.04.034_bib17) 2007; 5 Strasser (10.1016/j.ab.2008.04.034_bib25) 2006; 45 Bardor (10.1016/j.ab.2008.04.034_bib21) 2000; 21 Séveno (10.1016/j.ab.2008.04.034_bib5) 2004; 22 Strasser (10.1016/j.ab.2008.04.034_bib12) 2004; 561 Kurosaka (10.1016/j.ab.2008.04.034_bib29) 1991; 266 Cabanes-Macheteau (10.1016/j.ab.2008.04.034_bib20) 1999; 9 Ko (10.1016/j.ab.2008.04.034_bib8) 2003; 101 Maslen (10.1016/j.ab.2008.04.034_bib33) 2006; 78 |
| References_xml | – volume: 2 start-page: 517 year: 2004 end-page: 523 ident: bib13 article-title: Targeted knockouts of publication-title: Plant Biotechnol. J. – volume: 45 start-page: 789 year: 2006 end-page: 803 ident: bib25 article-title: Molecular cloning and characterization of publication-title: Plant J. – volume: 3 start-page: 449 year: 2005 end-page: 457 ident: bib11 article-title: Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogeneously throughout the plant with mostly high-mannose-type publication-title: Plant Biotechnol. J. – volume: 13 start-page: 427 year: 2003 end-page: 434 ident: bib3 article-title: Immunoreactivity in mammals of two typical plant glyco-epitopes, core-α(1,3)-fucose and core-xylose publication-title: Glycobiology – volume: 119 start-page: 725 year: 1999 end-page: 733 ident: bib19 article-title: Characterization of publication-title: Plant Physiol. – volume: 16 start-page: 576 year: 2006 end-page: 583 ident: bib26 article-title: Analytical strategies to investigate plant publication-title: Curr. Opin. Struct. Biol. – volume: 101 start-page: 8013 year: 2003 end-page: 8018 ident: bib8 article-title: Function and glycosylation of plant-derived antiviral monoclonal antibody publication-title: Proc. Natl. Acad. Sci. USA – volume: 561 start-page: 132 year: 2004 end-page: 136 ident: bib12 article-title: Generation of publication-title: FEBS Lett. – volume: 27 start-page: 1163 year: 1995 end-page: 1172 ident: bib7 article-title: Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells publication-title: Plant Mol. Biol. – volume: 96 start-page: 4692 year: 1999 end-page: 4697 ident: bib14 article-title: Stable expression of human (-1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns publication-title: Proc. Natl. Acad. Sci. USA – volume: 41 start-page: 14141 year: 2002 end-page: 14149 ident: bib23 article-title: Monitoring endoplasmic reticulum-to-Golgi traffic of a plant calreticulin by protein glycosylation analysis publication-title: Biochemistry – start-page: 125 year: 2006 end-page: 144, ident: bib28 article-title: Detailed structural analysis of publication-title: Glycobiology Protocols – volume: 2 start-page: 279 year: 2004 end-page: 287 ident: bib9 article-title: Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-α(1,3)-fucose residues publication-title: Plant Biotechnol. J. – start-page: 317 year: 2006 end-page: 342 ident: bib27 article-title: Plant proteomics and glycosylation publication-title: Plant Proteomics: Methods and Protocols – volume: 22 start-page: 5 year: 2004 end-page: 6 ident: bib5 article-title: Glycoprotein sialylation in plants? publication-title: Nat. Biotechnol. – volume: 38 start-page: 31 year: 1998 end-page: 48 ident: bib1 publication-title: Plant Mol. Biol. – volume: 95 start-page: 197 year: 1984 end-page: 203 ident: bib18 article-title: Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins publication-title: J. Biochem. – volume: 103 start-page: 7577 year: 2006 end-page: 7582 ident: bib16 article-title: An antibody produced in tobacco expressing a hybrid (-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes publication-title: Proc. Natl. Acad. Sci. USA – volume: 16 start-page: 349 year: 2006 end-page: 357 ident: bib4 article-title: Immunoglobulin G specifically binding plant publication-title: Glycobiology – volume: 14 start-page: 100 year: 2000 end-page: 104 ident: bib22 article-title: Analysis of 8-aminonaphthalene-1,3,6-trisulfonic acid labelled publication-title: Mass Spectrom. – volume: 98 start-page: 2899 year: 2001 end-page: 2904 ident: bib15 article-title: Humanized glycans on antibodies produced by transgenic plants publication-title: Proc. Natl. Acad. Sci. USA – volume: 224 start-page: 222 year: 2006 end-page: 227 ident: bib6 article-title: Sialic acid concentrations in plants are in the range of inadvertent contamination publication-title: Planta – volume: 5 start-page: 12 year: 2007 end-page: 25 ident: bib17 article-title: Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes publication-title: Plant Biotechnol. J. – volume: 21 start-page: 2550 year: 2000 end-page: 2556 ident: bib21 article-title: Monitoring the N-glycosylation by fluorophore-assisted carbohydrate electrophoresis publication-title: Electrophoresis – volume: 2 start-page: 83 year: 2004 end-page: 100 ident: bib2 article-title: Production and glycosylation of plant-made pharmaceuticals: The antibody as a challenge publication-title: Plant Biotechnol. J. – volume: 21 start-page: 275 year: 2004 end-page: 282 ident: bib24 article-title: Unaltered complex publication-title: Glycoconj. J. – volume: 1 start-page: 451 year: 2003 end-page: 462 ident: bib31 article-title: Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures publication-title: Plant Biotechnol. J. – volume: 16 start-page: 622 year: 2005 end-page: 630 ident: bib30 article-title: Fragmentation of negative ions from carbohydrates: I. Use of nitrate or other anionic adducts for the production of negative ion electrospray spectra from N-linked carbohydrates publication-title: J. Am. Soc. Mass Spectrom. – volume: 266 start-page: 4168 year: 1991 end-page: 4172 ident: bib29 article-title: The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum publication-title: J. Biol. Chem. – volume: 16 start-page: 647 year: 2005 end-page: 659 ident: bib32 article-title: Fragmentation of negative ions from carbohydrates: III. Fragmentation of hybrid and complex N-linked glycan publication-title: J. Am. Soc. Mass Spectrom. – volume: 78 start-page: 8491 year: 2006 end-page: 8498 ident: bib33 article-title: Differentiation of isomeric publication-title: Anal. Chem. – volume: 426 start-page: 266 year: 2004 end-page: 278 ident: bib10 article-title: Controlled glycosylation of therapeutic antibodies in plants publication-title: Arch. Biochem. Biophys. – volume: 9 start-page: 365 year: 1999 end-page: 372 ident: bib20 article-title: N-Glycosylation of a mouse IgG expressed in transgenic tobacco plants publication-title: Glycobiology – volume: 22 start-page: 5 year: 2004 ident: 10.1016/j.ab.2008.04.034_bib5 article-title: Glycoprotein sialylation in plants? publication-title: Nat. Biotechnol. doi: 10.1038/nbt1104-1351 – volume: 98 start-page: 2899 year: 2001 ident: 10.1016/j.ab.2008.04.034_bib15 article-title: Humanized glycans on antibodies produced by transgenic plants publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.031419998 – volume: 13 start-page: 427 year: 2003 ident: 10.1016/j.ab.2008.04.034_bib3 article-title: Immunoreactivity in mammals of two typical plant glyco-epitopes, core-α(1,3)-fucose and core-xylose publication-title: Glycobiology doi: 10.1093/glycob/cwg024 – volume: 561 start-page: 132 year: 2004 ident: 10.1016/j.ab.2008.04.034_bib12 article-title: Generation of Arabidopsis thaliana plants with complex N -glycans lacking (-1,2-linked xylose and core α-1,3-linked fucose publication-title: FEBS Lett. doi: 10.1016/S0014-5793(04)00150-4 – volume: 2 start-page: 83 year: 2004 ident: 10.1016/j.ab.2008.04.034_bib2 article-title: Production and glycosylation of plant-made pharmaceuticals: The antibody as a challenge publication-title: Plant Biotechnol. J. doi: 10.1111/j.1467-7652.2004.00062.x – volume: 2 start-page: 279 year: 2004 ident: 10.1016/j.ab.2008.04.034_bib9 article-title: Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-α(1,3)-fucose residues publication-title: Plant Biotechnol. J. doi: 10.1111/j.1467-7652.2004.00078.x – volume: 16 start-page: 576 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib26 article-title: Analytical strategies to investigate plant N -glycan profiles in the context of plant-made pharmaceuticals publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2006.08.009 – volume: 119 start-page: 725 year: 1999 ident: 10.1016/j.ab.2008.04.034_bib19 article-title: Characterization of N -glycans from Arabidopsis thaliana: Application to a fucose-deficient mutant publication-title: Plant Physiol. doi: 10.1104/pp.119.2.725 – volume: 16 start-page: 647 year: 2005 ident: 10.1016/j.ab.2008.04.034_bib32 article-title: Fragmentation of negative ions from carbohydrates: III. Fragmentation of hybrid and complex N-linked glycan publication-title: J. Am. Soc. Mass Spectrom. doi: 10.1016/j.jasms.2005.01.006 – volume: 2 start-page: 517 year: 2004 ident: 10.1016/j.ab.2008.04.034_bib13 article-title: Targeted knockouts of Physcomitrella lacking plant-specific immunogenic N -glycans publication-title: Plant Biotechnol. J. doi: 10.1111/j.1467-7652.2004.00100.x – volume: 41 start-page: 14141 year: 2002 ident: 10.1016/j.ab.2008.04.034_bib23 article-title: Monitoring endoplasmic reticulum-to-Golgi traffic of a plant calreticulin by protein glycosylation analysis publication-title: Biochemistry doi: 10.1021/bi0204701 – volume: 16 start-page: 622 year: 2005 ident: 10.1016/j.ab.2008.04.034_bib30 article-title: Fragmentation of negative ions from carbohydrates: I. Use of nitrate or other anionic adducts for the production of negative ion electrospray spectra from N-linked carbohydrates publication-title: J. Am. Soc. Mass Spectrom. doi: 10.1016/j.jasms.2005.01.004 – volume: 224 start-page: 222 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib6 article-title: Sialic acid concentrations in plants are in the range of inadvertent contamination publication-title: Planta doi: 10.1007/s00425-005-0206-8 – volume: 101 start-page: 8013 year: 2003 ident: 10.1016/j.ab.2008.04.034_bib8 article-title: Function and glycosylation of plant-derived antiviral monoclonal antibody publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0832472100 – volume: 95 start-page: 197 year: 1984 ident: 10.1016/j.ab.2008.04.034_bib18 article-title: Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins publication-title: J. Biochem. doi: 10.1093/oxfordjournals.jbchem.a134585 – volume: 3 start-page: 449 year: 2005 ident: 10.1016/j.ab.2008.04.034_bib11 article-title: Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogeneously throughout the plant with mostly high-mannose-type N -glycans publication-title: Plant Biotechnol. J. doi: 10.1111/j.1467-7652.2005.00137.x – volume: 45 start-page: 789 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib25 article-title: Molecular cloning and characterization of Arabidopsis thaliana Golgi α-mannosidase II, a key enzyme in the formation of complex N -glycans in plants publication-title: Plant J. doi: 10.1111/j.1365-313X.2005.02648.x – volume: 38 start-page: 31 year: 1998 ident: 10.1016/j.ab.2008.04.034_bib1 article-title: N -Glycoprotein biosynthesis: Recent development and future trends publication-title: Plant Mol. Biol. doi: 10.1023/A:1006012005654 – start-page: 317 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib27 article-title: Plant proteomics and glycosylation – volume: 21 start-page: 275 year: 2004 ident: 10.1016/j.ab.2008.04.034_bib24 article-title: Unaltered complex N -glycan profiles in Nicotiana benthamiana despite drastic reduction of β-1,2-N-acetylglucosaminyltransferase I activity publication-title: Glycoconj. J. doi: 10.1023/B:GLYC.0000045099.29038.04 – volume: 9 start-page: 365 year: 1999 ident: 10.1016/j.ab.2008.04.034_bib20 article-title: N-Glycosylation of a mouse IgG expressed in transgenic tobacco plants publication-title: Glycobiology doi: 10.1093/glycob/9.4.365 – volume: 266 start-page: 4168 year: 1991 ident: 10.1016/j.ab.2008.04.034_bib29 article-title: The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(20)64302-2 – volume: 14 start-page: 100 year: 2000 ident: 10.1016/j.ab.2008.04.034_bib22 article-title: Analysis of 8-aminonaphthalene-1,3,6-trisulfonic acid labelled N -glycans by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry publication-title: Mass Spectrom. – volume: 1 start-page: 451 year: 2003 ident: 10.1016/j.ab.2008.04.034_bib31 article-title: Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures publication-title: Plant Biotechnol. J. doi: 10.1046/j.1467-7652.2003.00041.x – volume: 103 start-page: 7577 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib16 article-title: An antibody produced in tobacco expressing a hybrid (-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0600879103 – volume: 16 start-page: 349 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib4 article-title: Immunoglobulin G specifically binding plant N -glycans with high affinity could be generated in rabbits but not in mice publication-title: Glycobiology doi: 10.1093/glycob/cwj071 – volume: 96 start-page: 4692 year: 1999 ident: 10.1016/j.ab.2008.04.034_bib14 article-title: Stable expression of human (-1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.96.8.4692 – volume: 27 start-page: 1163 year: 1995 ident: 10.1016/j.ab.2008.04.034_bib7 article-title: Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells publication-title: Plant Mol. Biol. doi: 10.1007/BF00020889 – volume: 5 start-page: 12 year: 2007 ident: 10.1016/j.ab.2008.04.034_bib17 article-title: Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes publication-title: Plant Biotechnol. J. doi: 10.1111/j.1467-7652.2006.00211.x – start-page: 125 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib28 article-title: Detailed structural analysis of N-glycans released from glycoproteins in SDS–PAGE gel bands using HPLC combined with exoglycosidase array digestions – volume: 426 start-page: 266 year: 2004 ident: 10.1016/j.ab.2008.04.034_bib10 article-title: Controlled glycosylation of therapeutic antibodies in plants publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2004.02.034 – volume: 21 start-page: 2550 year: 2000 ident: 10.1016/j.ab.2008.04.034_bib21 article-title: Monitoring the N-glycosylation by fluorophore-assisted carbohydrate electrophoresis publication-title: Electrophoresis doi: 10.1002/1522-2683(20000701)21:12<2550::AID-ELPS2550>3.0.CO;2-G – volume: 78 start-page: 8491 year: 2006 ident: 10.1016/j.ab.2008.04.034_bib33 article-title: Differentiation of isomeric N -glycan structures by normal-phase liquid chromatography–MALDI–TOF/TOF tandem mass spectrometry publication-title: Anal. Chem. doi: 10.1021/ac0614137 |
| SSID | ssj0011456 |
| Score | 2.0198393 |
| Snippet | Development of convenient strategies for identification of plant
N-glycan profiles has been driven by the emergence of plants as an expression system for... Development of convenient strategies for identification of plant N-glycan profiles has been driven by the emergence of plants as an expression system for... |
| SourceID | hal proquest pubmed crossref elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 66 |
| SubjectTerms | Cell Behavior Cellular Biology Chemical Sciences Chromatography, High Pressure Liquid Glycopeptides Glycopeptides - chemistry Glycopeptides - metabolism Glycoprotein Life Sciences Medicago sativa Medicago sativa - chemistry Medicinal Chemistry N-Glycan profiling Neurobiology Neurons and Cognition Nicotiana - chemistry ortho-Aminobenzoates ortho-Aminobenzoates - chemistry Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism Pharmaceutical sciences Pharmacology Plant glycosylation Plant Leaves Plant Leaves - chemistry Plants Plants - chemistry Polysaccharides Polysaccharides - analysis Polysaccharides - chemistry Polysaccharides - isolation & purification Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Therapeutic protein Tobacco |
| Title | Plant N-glycan profiling of minute amounts of material |
| URI | https://dx.doi.org/10.1016/j.ab.2008.04.034 https://www.ncbi.nlm.nih.gov/pubmed/18482571 https://www.proquest.com/docview/69220101 https://normandie-univ.hal.science/hal-01974002 |
| Volume | 379 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1NT9wwELUoHNoLotCWjxasqqrUQ9jEmTjxcbUqWth2D1VRuVlOYreL2CyCLBIXfjszjrNVD3DoKZI1TkYea-Y5fvZj7JNUTopaxbjIcTICAMyDoJLIxZAktQMbCzrv_H0qx-dwdpFdrLFRfxaGaJUh93c53Wfr0DIIozm4ns3ojG-M2EPlHvNIr1yLn6K5fvywonkg3PcKrmQckXXYquw4XqYMbEo4jlN4qjS9-EMcyacAqC9EJ1tsMyBIPuycfM3WbLPNdoYNrp7n9_wz95xO_7N8m70c9XpuO0ySPlHLp9Hvq3scT96pdWPl4gvH57Nm2Vpu5iQdcetbTOsn5xt2fvL152gcBdWEqEoL0UZ1TiAvy20KmRO1oSCYEitz6ZxxsgSoasQhiSiLSmVKIkI0lXCQ2MyCrOv0LVtvFo3dZRxrl3I2M0WcGVCVKOKqEGVeFcaoIrfJHhv0A6arcKU4KVtc6Z47dqlNGZQuQeMQ77Evqx7X3XUaz9imfQz0P1NCY7Z_ptdHDNfq5XR79nj4TVMbotkcU5a4Q8eP-mhqjALtkZjGLpa3WipB_AC0eNcF-a-bBeBqOk_2_8utA_aqY5oQdfA9W29vlvYDwpm2PPTz9ZBtDE8n4yk9Jz9-TR4B0AzwhQ |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1NT9wwELUoPdBLVT5aaEuxKoTUQ9jEmTjxcbUCbdtlTyBxs5zELovYLCrZSlz47cw4zlYc4MDVGkejGWvmOX72Y-xQKidFrWLc5DgZAQDWQVBJ5GJIktqBjQXddz6byvEF_LrMLtfYqL8LQ7TKUPu7mu6rdRgZhGgObmczuuMbI_ZQucc8kpRr30KW5sTrO35Y8TwQ73sJV7KOyDycVXYkL1MGOiUcxyk815veXBFJ8jkE6jvR6Qf2PkBIPuy83GRrttli28MGt8_ze37EPanT_y3fYhujXtBtm0kSKGr5NPpzc48B5Z1cN7YuvnB8PmuWreVmTtoRd37EtH517rCL05Pz0TgKsglRlRaijeqcUF6W2xQyJ2pDWTAltubSOeNkCVDVCEQSURaVypREiGgq4SCxmQVZ1-lHtt4sGrvLODYv5WxmijgzoCpRxFUhyrwqjFFFbpM9NugDpqvwpjhJW9zonjx2rU0ZpC5BY4j32I_VjNvuPY0XbNM-B_rJmtBY7l-Y9R3Ttfo4PZ89Hk40jSGczbFmiX_o-EGfTY1ZoEMS09jF8k5LJYgggBafuiT_d7MA3E7nyedXuXXANsbnZxM9-Tn9_YW962gnxCP8ytbbv0u7j9imLb_5tfsI30LwdQ |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Plant+N-glycan+profiling+of+minute+amounts+of+material&rft.jtitle=Analytical+biochemistry&rft.au=S%C3%A9veno%2C+Martial&rft.au=Cabrera%2C+Gleysin&rft.au=Triguero%2C+Ada&rft.au=Burel%2C+Carole&rft.date=2008-08-01&rft.pub=Elsevier+Inc&rft.issn=0003-2697&rft.eissn=1096-0309&rft.volume=379&rft.issue=1&rft.spage=66&rft.epage=72&rft_id=info:doi/10.1016%2Fj.ab.2008.04.034&rft.externalDocID=S0003269708002613 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0003-2697&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0003-2697&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0003-2697&client=summon |