Structural studies of Helix aspersa agglutinin complexed with GalNAc: A lectin that serves as a diagnostic tool
Open accessAbstract
Lectins belong to a differentiated group of proteins known to possess sugar-binding properties. Due to this fact, they are interesting research targets in medical diagnostics. Helix aspersa agglutinin (HAA) is a lectin that recognizes the epitopes containing α-d-N-acetylgalactosamine (GalNAc), which is present at the surface of metastatic cancer cells. Although several reports have already described the use of HAA as a diagnostic tool, this protein was not characterized on the molecular level. Here, we present for the first time the structural information about lectin isolated from mucus of Helix aspersa (garden snail). The amino acid sequence of this agglutinin was determined by Edman degradation and tertiary as well as quaternary structure by X-ray crystallography. The high resolution crystal structure (1.38Å) and MALDI-TOF mass spectrometry analysis provide the detailed information about a large part of the HAA natural glycan chain. The topology of the GalNAc binding cleft and interaction with lectin are very well defined in the structure and fully confirmed by STD HSQC NMR spectroscopy. Together, this provides structural clues regarding HAA specificity and opens possibilities to rational modifications of this important diagnostic tool.
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C. aspersum mucus agglutinin (lectin) is considered a diagnostic tool that recognizes epitopes containing α-d-N-acetylgalactosamine present on the surface of metastatic cancer cells.
“C. aspersum mucus agglutinin (lectin) is also considered a diagnostic tool that recognizes epitopes containing α-d-N-acetylgalactosamine present on the surface of metastatic cancer cells [67].”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [67]
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Hudz, N., Turkina, V., Alyokhina, T., Motyka, O., Chemerys, N., Rumynska, T., Lozynskyi, A., Jasicka-Misiak, I., & Kobylinska, L. (2025) · Molecules · doi:10.3390/molecules30214197 · Cited by 4 · see citing works
- Authors
- Pietrzyk, A. J., Bujacz, A., Mak, P., Potempa, B., & Niedziela, T.
- Affiliations
- Lodz University of Technology (PL)
- Jagiellonian University (PL)
- University of Louisville (US)
- Ludwik Hirszfeld Institute of Immunology and Experimental Therapy (PL)
- Corresponding author
- Bujacz, Anna
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 81
- Pages
- 1059-1068
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W1816613529
- Cited by
- 20
- References
- 0
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2017: 1 · 2015: 1
- FWCI
- 0.26
- Type
- journal article
- Language
- en
- Open access
- green
- ruj.uj.edu.pl
- Licence
- cc-by-nc-nd
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- Locations
- International Journal of Biological Macromolecules (publishedVersion)
- PubMed (publishedVersion)
- Jagiellonian University Repository (Jagiellonian University) (submittedVersion, cc-by-nc-nd)
- Desy Publications Database (Deutsches Elektronen-Synchrotron DESY) (submittedVersion)
- Funders
- European Community's Seventh Framework Programme (283570)
- Ministry of Science and Higher Education, Warsaw, Poland
- European Union (POIG.02.01.00-12-064/08)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- lectins, N-acetylgalactosamine, lectin-glycan binding, crystal structure, quaternary structure, metastatic cancer cells, diagnostic biomarkers, binding cleft, STD-NMR, amino acid sequence
- MeSH terms
- Agglutinins, Amino Acid Sequence, Animals, Binding Sites, Chromatography, High Pressure Liquid, Galactosamine, Glycosylation, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Snails, X-Ray Diffraction, Zinc, Epitope Mapping, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Static Electricity, Chromatography, Reverse-Phase
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