Polysaccharide epitopes recognized by human α-l-Rha antibodies

Polysaccharide epitopes recognized by human α-l-Rha antibodies Full article

Journal

Carbohydrate Research
ISSN: 1873-426X , E-ISSN: 0008-6215

Output data

Year: 2026, Volume: 559, Article number : 109717, Pages count : DOI: 10.1016/j.carres.2025.109717

Authors

Shilova Nadezhda V. ¹ , Obukhova Polina S. ¹ , Knirel Yuriy A. ² , Golovchenko Victoria V. ³ , Patova Olga A. ³ , Tsygankova Svetlana V. ⁴ , Mikshina Polina V. ⁵ , Henry Stephen ⁶ , Bovin Nicolai V. ⁷

Affiliations

1	M. M. Shemyakin-Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya Str., 117997, Moscow, Russian Federation; National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after V.I. Kulakov of the Ministry of Health Care of Russian Federation, 4 Oparina Str., 117997, Moscow, Russian Federation.
2	N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 47 Leninsky Prosp., 119991, Moscow, Russian Federation.
3	Institute of Physiology of Federal Research Centre "Komi Science Centre of the Urals Branch of the Russian Academy of Sciences", 50 Pervomaiskaya Str., 167982, Syktyvkar, Russian Federation.
4	M. M. Shemyakin-Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya Str., 117997, Moscow, Russian Federation.
5	Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center, Russian Academy of Sciences, 2/31 Lobachevsky Str., 420111, Kazan, Russian Federation.
6	School of Engineering, AUT University, 55 Wellesley Street East, Auckland City, New Zealand. Electronic address: stephen.henry@aut.ac.nz.
7	M. M. Shemyakin-Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya Str., 117997, Moscow, Russian Federation. Electronic address: nvbovin@gmail.com.

The levels of antibodies in human blood binding to the monosaccharide α-L-Rha are the highest among all anti-glycan antibodies. Moreover, anti-Rha antibodies are found in all individuals, suggesting that they are naturally occurring rather than adaptive immunoglobulins. Rhamnose is common in both bacterial (especially infectious) and plant polysaccharides, however, it remains poorly understood which rhamnose-containing epitope(s) – whether monosaccharide, oligosaccharide, or complex molecular patterns – are recognized by human antibodies. Using an affinity adsorbent, α-L-Rha-Sepharose, antibodies were isolated from human immunoglobulin preparations (IgG + IgM + IgA) and analyzed using highly representative arrays of bacterial and plant polysaccharides (about 1000 glycans, of which >240 contained Rha). Isolated anti-α-L-Rha antibodies bound to almost all polysaccharides where the rhamnose residue was located either terminally or as α1–2, 1–3 or 1–4 linked pendant substituent, but not to internal positions, regardless of whether they were bacterial O-antigens or plant polysaccharides. It was concluded that human polyclonal anti-α-L-Rha antibodies have a reasonably narrow range of epitope specificity. The recognition of a small-sized monosaccharide epitope, on one hand, and a high proportion of IgM and IgA, on the other, suggest a high degree of polyvalence in recognizing the natural targets of the antibodies studied. In vivo, anti-α-L-Rha antibodies are more likely to recognize a pattern composed of tightly packed lipopolysaccharides (or capsular polysaccharides, or plant cell walls) rather than repetitive epitopes on a single polysaccharide molecule.

Shilova N.V. , Obukhova P.S. , Knirel Y.A. , Golovchenko V.V. , Patova O.A. , Tsygankova S.V. , Mikshina P.V. , Henry S. , Bovin N.V.
Polysaccharide epitopes recognized by human α-l-Rha antibodies
Carbohydrate Research. 2026. V.559. 109717 . DOI: 10.1016/j.carres.2025.109717 WOS OpenAlex

Web of science:	WOS:001612681800001
OpenAlex:	W4415641230

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