دورية أكاديمية

Minimal epitope for Mannitou IgM on paucimannose-carrying glycoproteins

التفاصيل البيبلوغرافية
العنوان: Minimal epitope for Mannitou IgM on paucimannose-carrying glycoproteins
المؤلفون: Robakiewicz, Stefania, Bridot, Clarisse, Serna, Sonia, Gimeno, Ana, Echeverria, Begoña, Delgado, Sandra, de Ruyck, Jerome, Semwal, Shubham, Charro, Diego, Dansercoer, Ann, Verstraete, Kenneth, Azkargorta, Mikel, van Noort, Kim, Wilbers, Ruud H P, Savvides, Savvas N, Abrescia, Nicola G A, Arda, Ana, Reichardt, Niels C, Jiménez-Barbero, Jesús, Bouckaert, Julie
المساهمون: Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centro de Investigación Cooperativa en Biomateriales (CIC biomaGUNE), Center for Cooperative Research in Biosciences = Centro de Investigación cooperativa en biociencia (Derio, Biscay, Espagne) (CIC bioGUNE), VIB-UGent Center for Inflammation Research Gand, Belgique (IRC), VIB Belgium, Wageningen University and Research Wageningen (WUR), Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), Instituto de Salud Carlos III Madrid (ISC)-ministerio de ciencia e innovacion
المصدر: ISSN: 0959-6658.
بيانات النشر: HAL CCSD
Oxford University Press (OUP)
سنة النشر: 2021
المجموعة: LillOA (HAL Lille Open Archive, Université de Lille)
مصطلحات موضوعية: core fucose, IgM, Mannitou, N-glycan, paucimannosidic epitopes, [SDV]Life Sciences [q-bio]
الوصف: International audience ; Abstract Paucimannosidic glycans are restricted to the core structure [Man1–3GlcNAc2Fuc0–1] of N-glycans and are rarely found in mammalian tissues. Yet, especially [Man2-3GlcNAc2Fuc1] have been found significantly upregulated in tumors, including in colorectal and liver cancer. Mannitou IgM is a murine monoclonal antibody that was previously shown to recognize Man3GlcNAc2 with an almost exclusive selectivity. Here, we have sought the definition of the minimal glycan epitope of Mannitou IgM, initiated by screening on a newly designed paucimannosidic glycan microarray; among the best binders were Man3GlcNAc2 and its α1,6 core-fucosylated variant, Man3GlcNAc2Fuc1. Unexpectedly and in contrast to earlier findings, Man5GlcNAc2-type structures bind equally well and a large tolerance was observed for substitutions on the α1,6 arm. It was confirmed that any substitution on the single α1,3-linked mannose completely abolishes binding. Surface plasmon resonance for kinetic measurements of Mannitou IgM binding, either directly on the glycans or as presented on omega-1 and kappa-5 soluble egg antigens from the helminth parasite Schistosoma mansoni, showed submicromolar affinities. To characterize the epitope in greater and atomic detail, saturation transfer difference nuclear magnetic resonance spectroscopy was performed with the Mannitou antigen-binding fragment. The STD-NMR data demonstrated the strongest interactions with the aliphatic protons H1 and H2 of the α1–3-linked mannose and weaker imprints on its H3, H4 and H5 protons. In conclusion, Mannitou IgM binding requires a nonsubstituted α1,3-linked mannose branch of paucimannose also on proteins, making it a highly specific tool for the distinction of concurrent human tumor-associated carbohydrate antigens.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: hal-03283666; https://hal.univ-lille.fr/hal-03283666Test; https://hal.univ-lille.fr/hal-03283666v2/documentTest; https://hal.univ-lille.fr/hal-03283666v2/file/P21.02%20GLYCO-2021-00007.R1_Proof_hi.pdfTest
الإتاحة: https://hal.univ-lille.fr/hal-03283666Test
https://hal.univ-lille.fr/hal-03283666v2/documentTest
https://hal.univ-lille.fr/hal-03283666v2/file/P21.02%20GLYCO-2021-00007.R1_Proof_hi.pdfTest
حقوق: info:eu-repo/semantics/OpenAccess
رقم الانضمام: edsbas.864263BD
قاعدة البيانات: BASE