دورية أكاديمية

Human Natural Antibodies Recognizing Glycan Galβ1-3GlcNAc (LeC)

التفاصيل البيبلوغرافية
العنوان: Human Natural Antibodies Recognizing Glycan Galβ1-3GlcNAc (LeC)
المؤلفون: Kira Dobrochaeva, Nailya Khasbiullina, Nadezhda Shilova, Nadezhda Antipova, Polina Obukhova, Oxana Galanina, Mikhail Gorbach, Inna Popova, Sergey Khaidukov, Natalia Grishchenko, Nikolai Tupitsyn, Jacques Le Pendu, Nicolai Bovin
المصدر: International Journal of Molecular Sciences, Vol 21, Iss 18, p 6511 (2020)
بيانات النشر: MDPI AG, 2020.
سنة النشر: 2020
المجموعة: LCC:Biology (General)
LCC:Chemistry
مصطلحات موضوعية: breast cancer, cancer-associated antibodies, LeC antigen, natural anti-glycan antibodies, printed glycan array, Biology (General), QH301-705.5, Chemistry, QD1-999
الوصف: The level of human natural antibodies of immunoglobulin M isotype against LeC in patients with breast cancer is lower than in healthy women. The epitope specificity of these antibodies has been characterized using a printed glycan array and enzyme-linked immunosorbent assay (ELISA), the antibodies being isolated from donors’ blood using LeC-Sepharose (LeC is Galβ1-3GlcNAcβ). The isolated antibodies recognize the disaccharide but do not bind to glycans terminated with LeC, which implies the impossibility of binding to regular glycoproteins of non-malignant cells. The avidity (as dissociation constant value) of antibodies probed with a multivalent disaccharide is 10−9 M; the nanomolar level indicates that the concentration is sufficient for physiological binding to the cognate antigen. Testing of several breast cancer cell lines showed the strongest binding to ZR 75-1. Interestingly, only 7% of the cells were positive in a monolayer with a low density, increasing up to 96% at highest density. The enhanced interaction (instead of the expected inhibition) of antibodies with ZR 75-1 cells in the presence of Galβ1-3GlcNAcβ disaccharide, indicates that the target epitope of anti-LeC antibodies is a molecular pattern with a carbohydrate constituent rather than a glycan.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1422-0067
1661-6596
Relation: https://www.mdpi.com/1422-0067/21/18/6511; https://doaj.org/toc/1661-6596; https://doaj.org/toc/1422-0067
DOI: 10.3390/ijms21186511
URL الوصول: https://doaj.org/article/9d2bf7e2805a4415b9706a63caab4528
رقم الأكسشن: edsdoj.9d2bf7e2805a4415b9706a63caab4528
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:14220067
16616596
DOI:10.3390/ijms21186511