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Some Human Anti-Glycan Antibodies Lack the Ability to Activate the Complement System Научная публикация

Журнал Antibodies
ISSN: 2073-4468
Вых. Данные Год: 2024, Том: 13, Номер: 4, Номер статьи : 105, Страниц : DOI: 10.3390/antib13040105
Авторы Shilova Nadezhda 1,2 , Nokel Alexey 1,2 , Lipatnikov Alexander 2 , Khasbiullina Nailya 1 , Knirel Yuri 3 , Baidakova Ludmila 4 , Tuzikov Alexander 2 , Khaidukov Sergei 1,2 , Obukhova Polina 1,2 , Henry Stephen 5 , Shoibonov Batozhab 6 , Salimov Emin 7 , Rieben Robert 8 , Bovin Nicolai 2
Организации
1 National Medical Research Center for Obstetrics, Gynecology and Perinatology of the Ministry of Health of the Russian Federation, 117991 Moscow, Russia
2 Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Science, 117991 Moscow, Russia
3 Zelinsky Institute of Organic Chemistry Russian Academy of Science, 119991 Moscow, Russia
4 Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
5 School of Engineering, AUT University, Auckland 92006, New Zealand
6 Federal Research Center for Original and Promising Biomedical and Pharmaceutical Technologies, 125315 Moscow, Russia
7 Clinical Center of Sechenov First Moscow State Medical University of the Ministry of Health Care of the Russian Federation, 119435 Moscow, Russia
8 Department for BioMedical Research, University of Bern, 3008 Bern, Switzerland

Реферат: Background. Naturally occurring human antibodies against glycans recognize and quickly eliminate infectious bacteria, viruses and aberrantly glycosylated neoplastic malignant cells, and they often initiate processes that involve the complement system. Methods. Using a printed glycan array (PGA) containing 605 glycoligands (oligo- and polysaccharides, glycopeptides), we examined which of the glycan-binding antibodies are able to activate the complement system. Using this PGA, the specificities of antibodies of the IgM and IgG classes were determined in the blood serum of healthy donors (suggested as mostly natural), and, then, using the same array, it was determined which types of the bound immunoglobulins were also showing C3 deposition. Results. It was found that about 30% of anti-glycan antibodies in human serum detected by the PGA did not activate the complement. They were mostly IgGs and directed to bacterial O-antigens; no apparent common structural motif within their target polysaccharides was found. Antibodies to blood group systems ABO and Forssman, xeno-antigens, a number of polysaccharides from various strains of S. enterica, E. coli and P. alcalifaciens, as well as small fragments of bacterial polysaccharides were recognized by complement-activating antibodies as expected. A complement-activating antibody was affinity-isolated on glycan-Sepharose from human serum, and, in the presence of the complement, it lysed red blood cells coated with the same glycan (kodecytes, where glycans expressed on biological membranes), while an isolated complement non-activating antibody did not, which confirms the validity of the solid-phase PGA results. Conclusions. Thus, ~30% of human anti-glycan antibodies lack the ability to activate the complement system. The function of the widely represented immunoglobulins that do not cause C3 deposition remains unclear.
Библиографическая ссылка: Shilova N. , Nokel A. , Lipatnikov A. , Khasbiullina N. , Knirel Y. , Baidakova L. , Tuzikov A. , Khaidukov S. , Obukhova P. , Henry S. , Shoibonov B. , Salimov E. , Rieben R. , Bovin N.
Some Human Anti-Glycan Antibodies Lack the Ability to Activate the Complement System
Antibodies. 2024. V.13. N4. 105 . DOI: 10.3390/antib13040105 WOS Scopus OpenAlex
Идентификаторы БД:
Web of science: WOS:001385513600001
Scopus: 2-s2.0-85213466276
OpenAlex: W4405725196
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