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Specificity of viscumin revised. As probed with a printed glycan array.

Nadezhda Shilova1, Nicolai Bovin2, Diana Maltseva3

  • 1Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya str., Moscow, 117997, Russia; National Medical Research Center for Obstetrics, Gynecology and Perinatology Named After Academician V.I. Kulakov of the Ministry of Healthcare of Russian Federation, 4 Oparina str., Moscow, 117997, Russia.

Biochimie
|August 21, 2022
PubMed
Summary

Viscumin, an anti-cancer lectin, binds strongly to sulfated glycans, challenging its classification as a simple β-galactoside binder. Its two binding sites show distinct preferences, with one favoring charged moieties.

Keywords:
Printed glycan arraySialoglycanSulfated glycanViscuminαGal epitope

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Area of Science:

  • Glycobiology
  • Biochemistry
  • Carbohydrate Chemistry

Background:

  • Viscumin is an anti-cancer lectin initially identified as a β-galactoside-binding protein.
  • Previous studies indicated its ability to bind 6'-sialyl N-acetyllactosamine (6'SLN) terminated gangliosides.

Purpose of the Study:

  • To investigate the glycan-binding specificity of viscumin using a comprehensive printed glycan array (PGA).
  • To re-evaluate the classification of viscumin as a β-galactoside-binding lectin based on its interactions with diverse mammalian glycans.

Main Methods:

  • Probing viscumin binding to a printed glycan array (PGA) containing numerous mammalian sulfated glycans.
  • Utilizing PGA in the presence of neutral or sulfated/sialylated glycans.
  • Sequential elution from lactose-sepharose and consideration of protein structure.

Main Results:

  • Viscumin exhibited strong binding to glycans containing the 6-O-SuGal moiety, including lactose, N-acetyllactosamine (LN), and di-N-acetyllactosamine (LacdiNAc).
  • Binding was also observed for some α-galactoside terminated glycans, such as Galα1-3Galβ1-4GlcNAc.
  • Weak interactions were detected with neutral β-galactosides, suggesting a more complex binding profile than previously assumed.

Conclusions:

  • Viscumin's binding profile extends beyond simple β-galactosides, with a notable preference for sulfated and sialylated glycans.
  • The study suggests that viscumin possesses two distinct glycan-binding sites with differing specificities.
  • These findings necessitate a revised understanding of viscumin's molecular interactions and potential therapeutic applications.