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Open AccessArticle

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

1
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya, 117997 Moscow, Russia
2
Semiotik LLC, 16/10 Miklukho-Maklaya, 117997 Moscow, Russia
3
National Medical Research Center for Obstetrics, Gynecology and Perinatology named after Academician V.I. Kulakov of the Ministry of Healthcare of Russian Federation, 4 Oparin str., 117997 Moscow, Russia
4
N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 47 Leninsky pr., 119991 Moscow, Russia
5
Peoples’Friendship University of Russia (RUDN), 6 Miklukho-Maklaya, 117198 Moscow, Russia
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National Research University Higher School of Economics, 101000 Moscow, Russia
7
N.N. Blokhin Russian Cancer Research Centre of the Ministry of Healthcare of Russian Federation, 24 Kashyrskoe Sh., 115478 Moscow, Russia
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CRCINA, INSERM, Université d’Angers, Université de Nantes, 8 quai Moncousu, BP 70721-44007 Nantes, France
9
Centre for Kode Technology Innovation, Auckland University of Technology, 55 Wellesley Street East, Auckland 1010, New Zealand
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(18), 6511; https://doi.org/10.3390/ijms21186511
Received: 3 August 2020 / Revised: 30 August 2020 / Accepted: 3 September 2020 / Published: 5 September 2020
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. View Full-Text
Keywords: breast cancer; cancer-associated antibodies; LeC antigen; natural anti-glycan antibodies; printed glycan array breast cancer; cancer-associated antibodies; LeC antigen; natural anti-glycan antibodies; printed glycan array
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Dobrochaeva, K.; Khasbiullina, N.; Shilova, N.; Antipova, N.; Obukhova, P.; Galanina, O.; Gorbach, M.; Popova, I.; Khaidukov, S.; Grishchenko, N.; Tupitsyn, N.; Pendu, J.L.; Bovin, N. Human Natural Antibodies Recognizing Glycan Galβ1-3GlcNAc (LeC). Int. J. Mol. Sci. 2020, 21, 6511.

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