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Polysaccharide epitopes recognized by human α-L-Rha antibodies.

Nadezhda V Shilova1, Polina S Obukhova1, Yuriy A Knirel2

  • 1M. 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.

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Human antibodies targeting alpha-L-rhamnose (α-L-Rha) are naturally occurring and recognize specific rhamnose positions on bacterial and plant polysaccharides. These anti-Rha antibodies exhibit polyvalence, recognizing patterns of tightly packed molecules in vivo.

Keywords:
Bacterial polysaccharidesEpitopeHuman antibodiesPlant polysaccharidesRhamnose

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Area of Science:

  • Immunology
  • Glycobiology
  • Microbiology

Background:

  • Anti-glycan antibodies are abundant in human blood, with anti-rhamnose (anti-Rha) antibodies being the most prevalent.
  • These anti-Rha antibodies are found in all individuals, indicating a natural, non-adaptive origin.
  • Rhamnose is a component of bacterial and plant polysaccharides, but the specific epitopes recognized by human antibodies remain unclear.

Purpose of the Study:

  • To identify the specific rhamnose-containing epitopes recognized by human anti-Rha antibodies.
  • To investigate the binding characteristics of naturally occurring anti-Rha antibodies from human immunoglobulin preparations.
  • To understand the in vivo recognition patterns of these antibodies.

Main Methods:

  • Antibodies (IgG, IgM, IgA) were isolated from human immunoglobulin preparations using an alpha-L-rhamnose (α-L-Rha)-Sepharose affinity adsorbent.
  • Isolated antibodies were analyzed against a large array of approximately 1000 bacterial and plant polysaccharides, with over 240 containing rhamnose.
  • Binding specificity was assessed based on the location and linkage of rhamnose residues within the polysaccharide structures.

Main Results:

  • Anti-α-L-Rha antibodies bound to polysaccharides with terminal or pendant rhamnose (α1-2, 1-3, 1-4 linkages) but not internal positions.
  • Recognition occurred for both bacterial O-antigens and plant polysaccharides.
  • A high proportion of IgM and IgA antibodies suggested polyvalence, with a narrow epitope specificity for the monosaccharide.

Conclusions:

  • Human polyclonal anti-α-L-Rha antibodies possess a defined epitope specificity, primarily recognizing terminal or pendant rhamnose.
  • The polyvalent nature of these antibodies, particularly IgM and IgA, suggests efficient recognition of natural targets.
  • In vivo, anti-Rha antibodies likely target patterns of densely packed polysaccharides like lipopolysaccharides or plant cell walls rather than single repetitive epitopes.