A Novel C1q Domain-Containing Protein Isolated from the Mollusk Modiolus kurilensis Recognizing Glycans Enriched with Acidic Galactans and Mannans

peer-reviewed · Marine Drugs · 2021

peer-reviewed · Marine Drugs · 2021. Andrei V. Grinchenko et al. C1q domain-containing (C1qDC) proteins are a group of biopolymers involved in immune response as pattern…
Date 2021-11-26
Type peer-reviewed
Venue Marine Drugs
Publisher MDPI AG
Contribution downstream-application
DOI 10.3390/md19120668
Citations (OpenAlex) 14

Abstract

C1q domain-containing (C1qDC) proteins are a group of biopolymers involved in immune response as pattern recognition receptors (PRRs) in a lectin-like manner. A new protein MkC1qDC from the hemolymph plasma of Modiolus kurilensis bivalve mollusk widespread in the Northwest Pacific was purified. The isolation procedure included ammonium sulfate precipitation followed by affinity chromatography on pectin-Sepharose. The full-length MkC1qDC sequence was assembled using de novo mass-spectrometry peptide sequencing complemented with N-terminal Edman’s degradation, and included 176 amino acid residues with molecular mass of 19 kDa displaying high homology to bivalve C1qDC proteins. MkC1qDC demonstrated antibacterial properties against Gram-negative and Gram-positive strains. MkC1qDC binds to a number of saccharides in Ca 2+ -dependent manner which characterized by structural meta-similarity in acidic group enrichment of galactose and mannose derivatives incorporated in diversified molecular species of glycans. Alginate, κ-carrageenan, fucoidan, and pectin were found to be highly effective inhibitors of MkC1qDC activity. Yeast mannan, lipopolysaccharide (LPS), peptidoglycan (PGN) and mucin showed an inhibitory effect at concentrations three orders of magnitude greater than for the most effective saccharides. MkC1qDC localized to the mussel hemal system and interstitial compartment. Intriguingly, MkC1qDC was found to suppress proliferation of human adenocarcinoma HeLa cells in a dose-dependent manner, indicating to the biomedical potential of MkC1qDC protein.

Authors

  1. Andrei V. Grinchenko · A.V. Zhirmunsky National Scientific Center of Marine Biology Far Eastern Branch of the Russian Academy of Sciences, Russian Academy of Sciences
  2. Alex von Kriegsheim · Institute of Genetics and Cancer, University of Edinburgh
  3. Nikita A. Shved · A.V. Zhirmunsky National Scientific Center of Marine Biology Far Eastern Branch of the Russian Academy of Sciences, Far Eastern Federal University, Russian Academy of Sciences
  4. Anna E. Egorova · Far Eastern Federal University
  5. Diana V. Ilyaskina · Far Eastern Federal University
  6. Tatiana D. Karp · Far Eastern Federal University
  7. Nikolay V. Goncharov · A.V. Zhirmunsky National Scientific Center of Marine Biology Far Eastern Branch of the Russian Academy of Sciences, Far Eastern Federal University, Russian Academy of Sciences
  8. Irina Y. Petrova · A.V. Zhirmunsky National Scientific Center of Marine Biology Far Eastern Branch of the Russian Academy of Sciences, Russian Academy of Sciences
  9. Vadim V. Kumeiko · A.V. Zhirmunsky National Scientific Center of Marine Biology Far Eastern Branch of the Russian Academy of Sciences, Far Eastern Federal University, Russian Academy of Sciences

Methods and tools

  • Modiolus kurilensis C1q-domain lectin: A C1q domain-containing lectin from the mussel Modiolus kurilensis whose full sequence was assembled from de novo mass spectrometry peptide sequencing complemented by Edman degradation.

Seen in the charts

Back to the full map

Back to top