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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
A recombinant fungal lectin for labeling truncated glycans on human cancer cells
Aymeric Audfray1, Mona Beldjoudi2, Adrien Breiman3
1CERMAV, UPR5301, CNRS, University Grenoble Alpes, 38041 Grenoble, France.
Abstract:
Cell surface glycoconjugates present alterations of their structures in chronic diseases and distinct oligosaccharide epitopes have been associated with cancer. Among them, truncated glycans present terminal non-reducing β-N-acetylglucosamine (GlcNAc) residues that are rare on healthy tissues. Lectins from unconventional sources such as fungi or algi provide novel markers that bind specifically to such epitopes, but their availability may be challenging. A GlcNAc-binding lectin from the fruiting body of the fungus Psathyrella velutina (PVL) has been produced in good yield in bacterial culture. A strong specificity for terminal GlcNAc residues was evidenced by glycan array. Affinity values obtained by microcalorimetry and surface plasmon resonance demonstrated a micromolar affinity for GlcNAcβ1-3Gal epitopes and for biantennary N-glycans with GlcNAcβ1-2Man capped branches. Crystal structure of PVL complexed with GlcNAcβ1-3Gal established the structural basis of the specificity. Labeling of several types of cancer cells and use of inhibitors of glycan metabolism indicated that rPVL binds to terminal GlcNAc but also to sialic acid (Neu5Ac). Analysis of glycosyltransferase expression confirmed the higher amount of GlcNAc present on cancer cells. rPVL binding is specific to cancer tissue and weak or no labeling is observed for healthy ones, except for stomach glands that present unique αGlcNAc-presenting mucins. In lung, breast and colon carcinomas, a clear delineation could be observed between cancer regions and surrounding healthy tissues. PVL is therefore a useful tool for labeling agalacto-glycans in cancer or other diseases.
Insights
A novel fungal lectin, Psathyrella velutina lectin (PVL), specifically binds to terminal N-acetylglucosamine (GlcNAc) on cancer cells. This discovery offers a potential new tool for cancer diagnostics and imaging, distinguishing tumor tissue from healthy areas.
Area of Science:
- Biochemistry
- Glycobiology
- Cancer Research
Background:
- Cell surface glycoconjugates are altered in chronic diseases, with specific oligosaccharide epitopes linked to cancer.
- Truncated glycans with terminal β-N-acetylglucosamine (GlcNAc) residues are rare in healthy tissues but prevalent in cancer.
- Lectins from fungi offer potential biomarkers for these unique glycan structures, but availability can be a challenge.
Purpose of the Study:
- To characterize a GlcNAc-binding lectin from the fungus Psathyrella velutina (PVL) for potential use as a cancer biomarker.
- To investigate the specificity and binding affinity of PVL towards specific glycan structures.
- To evaluate the utility of PVL in labeling cancer cells and tissues.
Main Methods:
- Production of recombinant PVL (rPVL) in bacterial culture.
- Glycan array analysis to determine lectin specificity.
- Microcalorimetry and surface plasmon resonance to quantify binding affinity.
- Crystal structure determination of PVL complexed with a target glycan.
- Cell labeling assays on various cancer cell lines and tissues, including the use of glycan metabolism inhibitors.
Main Results:
- rPVL demonstrated strong specificity for terminal GlcNAc residues.
- Micromolar affinity was observed for GlcNAcβ1-3Gal and specific biantennary N-glycans.
- The crystal structure elucidated the molecular basis for GlcNAcβ1-3Gal binding.
- rPVL labeled several types of cancer cells, binding to terminal GlcNAc and sialic acid (Neu5Ac).
- Higher GlcNAc levels were confirmed on cancer cells, and rPVL binding clearly delineated cancer from healthy tissues in lung, breast, and colon carcinomas, with an exception in stomach glands.
Conclusions:
- PVL is a potent GlcNAc-binding lectin with high specificity for cancer-associated glycans.
- rPVL shows promise as a diagnostic tool for identifying and delineating various cancer types.
- PVL facilitates the labeling of agalacto-glycans, offering a novel approach for cancer research and diagnostics.
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