Zymosan, a beta-glucan and mannan-rich yeast particle

Where it participates (unsigned role)

1. Non-opsonic zymosan binding was unaffected by genetic CD11b deficiency or a blocking monoclonal antibody against CR3, demonstrating that CR3 was not the beta-glucan receptor mediating this activity, and using the novel anti-Dectin-1 antibody 2A11 Dectin-1 was shown to be almost exclusively responsible for the beta-glucan-dependent non-opsonic recognition of zymosan by primary macrophages, defining Dectin-1 as the leukocyte beta-glucan receptor first described over 50 years ago and resolving the long-standing controversy regarding the identity of this important molecule.

   Dectin-1 / CLEC7A → Non-opsonic recognition of a yeast particle source_derived_draftungraded
   Experimental context and source evidence

   evidence_span

   {"source_cache": "artifacts/glucan-research/12163569.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "533d8630c3d727db58869724825f47c5241cf9c3159acce359d3bc8b0fdb2a6a", "start_char": 0, "end_char": 1365, "text_sha256": "533d8630c3d727db58869724825f47c5241cf9c3159acce359d3bc8b0fdb2a6a"}

   experimental_model

   Carbohydrate inhibition, CD11b-deficient cells and a new anti-Dectin-1 monoclonal antibody applied to non-opsonic zymosan binding

   exposure

   Zymosan binding to primary macrophages with specific carbohydrate inhibitors, CD11b deficiency, a blocking anti-CR3 antibody and the novel anti-Dectin-1 antibody 2A11

   limitations

   The ligand is zymosan, which is a mannan-rich particle as well as a glucan one, and the readout is non-opsonic binding rather than every glucan response.

   nutrient_topic

   Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. · Beta-glucan

   organism

   Mouse

   plain_language

   Removing the complement receptor entirely did not change how macrophages grabbed yeast particles; blocking the other receptor did.

   primary_references

   [bg-p12163569] Dectin-1 is a major beta-glucan receptor on macrophages. (2002). https://pubmed.ncbi.nlm.nih.gov/12163569/ DOI: 10.1084/jem.20020470

   tissue_or_cell_type

   Primary macrophage

   Beta-glucan: a structural family rather than an agent, what decides whether a bound glucan actually signals, the complement route that a cereal and a yeast preparation share, and the unequal human evidence behind each (2026-09-22) · lines 112–123

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Carbohydrate inhibition, CD11b-deficient cells and a new anti-Dectin-1 monoclonal antibody applied to non-opsonic zymosan binding · source_derived_draft · unverified_draft

   ### bg-dectin1-not-cr3-binds-zymosan Non-opsonic zymosan binding was unaffected by genetic CD11b deficiency or a blocking monoclonal antibody against CR3, demonstrating that CR3 was not the beta-glucan receptor mediating this activity, and using the novel anti-Dectin-1 antibody 2A11 Dectin-1 was shown to be almost exclusively responsible for the beta-glucan-dependent non-opsonic recognition of zymosan by primary macrophages, defining Dectin-1 as the leukocyte beta-glucan receptor first described over 50 years ago and resolving the long-standing controversy regarding the identity of this important molecule. Condition category: normal nutrient_topic: Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. plain_language: Removing the complement receptor entirely did not change how macrophages grabbed yeast particles; blocking the other receptor did. organism: Mouse tissue_or_cell_type: Primary macrophage experimental_model: Carbohydrate inhibition, CD11b-deficient cells and a new anti-Dectin-1 monoclonal antibody applied to non-opsonic zymosan binding limitations: The ligand is zymosan, which is a mannan-rich particle as well as a glucan one, and the readout is non-opsonic binding rather than every glucan response. exposure: Zymosan binding to primary macrophages with specific carbohydrate inhibitors, CD11b deficiency, a blocking anti-CR3 antibody and the novel anti-Dectin-1 antibody 2A11 evidence_span: {"source_cache": "artifacts/glucan-research/12163569.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "533d8630c3d727db58869724825f47c5241cf9c3159acce359d3bc8b0fdb2a6a", "start_char": 0, "end_char": 1365, "text_sha256": "533d8630c3d727db58869724825f47c5241cf9c3159acce359d3bc8b0fdb2a6a"} [bg-p12163569] Dectin-1 is a major beta-glucan receptor on macrophages. (2002). https://pubmed.ncbi.nlm.nih.gov/12163569/ DOI: 10.1084/jem.20020470

   Complete structured claim and evidence

2. Dectin-1 is recruited to phagosomes containing zymosan particles but not to phagosomes containing immunoglobulin G-opsonised particles, dectin-1 expression enhances Toll-like receptor-mediated activation of nuclear factor kappa B by beta-glucan-containing particles, and in macrophages and dendritic cells dectin-1 and Toll-like receptors are synergistic in mediating production of cytokines such as interleukin 12 and tumour necrosis factor alpha, while dectin-1 triggers production of reactive oxygen species, an inflammatory response that is primed by Toll-like receptor activation.

   Dectin-1 / CLEC7A → Activation of nuclear factor kappa B source_derived_draftungraded
   Experimental context and source evidence

   evidence_span

   {"source_cache": "artifacts/glucan-research/12719479.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425", "start_char": 0, "end_char": 1588, "text_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425"}

   experimental_model

   Dectin-1 and Toll-like receptor co-expression with phagosome recruitment and cytokine measurement

   exposure

   Beta-glucan-containing zymosan particles on cells expressing dectin-1 with and without Toll-like receptor signalling

   limitations

   The particle is zymosan, which carries mannan and other yeast wall components as well as glucan, so a response to zymosan is not by itself a response to purified beta-glucan.

   nutrient_topic

   Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. · Beta-glucan

   organism

   Mouse

   plain_language

   The glucan receptor does not work alone; paired with a bacterial sensor the same particle produces far more than either would.

   primary_references

   [bg-p12719479] Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. (2003). https://pubmed.ncbi.nlm.nih.gov/12719479/ DOI: 10.1084/jem.20021787

   tissue_or_cell_type

   Macrophage and dendritic cell

   Beta-glucan: a structural family rather than an agent, what decides whether a bound glucan actually signals, the complement route that a cereal and a yeast preparation share, and the unequal human evidence behind each (2026-09-22) · lines 190–201

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Dectin-1 and Toll-like receptor co-expression with phagosome recruitment and cytokine measurement · source_derived_draft · unverified_draft

   ### bg-dectin1-works-with-tlr2 Dectin-1 is recruited to phagosomes containing zymosan particles but not to phagosomes containing immunoglobulin G-opsonised particles, dectin-1 expression enhances Toll-like receptor-mediated activation of nuclear factor kappa B by beta-glucan-containing particles, and in macrophages and dendritic cells dectin-1 and Toll-like receptors are synergistic in mediating production of cytokines such as interleukin 12 and tumour necrosis factor alpha, while dectin-1 triggers production of reactive oxygen species, an inflammatory response that is primed by Toll-like receptor activation. Condition category: normal nutrient_topic: Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. plain_language: The glucan receptor does not work alone; paired with a bacterial sensor the same particle produces far more than either would. organism: Mouse tissue_or_cell_type: Macrophage and dendritic cell experimental_model: Dectin-1 and Toll-like receptor co-expression with phagosome recruitment and cytokine measurement limitations: The particle is zymosan, which carries mannan and other yeast wall components as well as glucan, so a response to zymosan is not by itself a response to purified beta-glucan. exposure: Beta-glucan-containing zymosan particles on cells expressing dectin-1 with and without Toll-like receptor signalling evidence_span: {"source_cache": "artifacts/glucan-research/12719479.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425", "start_char": 0, "end_char": 1588, "text_sha256": "297eb222223ff6861d6890a273716f4cfb3f3c14f887c57c057c2af524f8b425"} [bg-p12719479] Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. (2003). https://pubmed.ncbi.nlm.nih.gov/12719479/ DOI: 10.1084/jem.20021787

   Complete structured claim and evidence

3. Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins, and among 187 diverse sequence-defined oligosaccharide probes together with designer microarrays from a neutral soluble glucan from S. cerevisiae, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer, and 11-13 gluco-oligomers in clustered form displayed on liposomes mimic the macromolecular beta-glucans and compete with zymosan binding and triggering of tumour necrosis factor alpha secretion.

   Dectin-1 / CLEC7A → Beta-(1->3)-linked gluco-oligosaccharides source_derived_draftungraded
   Experimental context and source evidence

   evidence_span

   {"source_cache": "artifacts/glucan-research/16371356.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dd98941694dedd8e3e85766c0c299b54fbc29ca8cce7c61a333efceee796867f", "start_char": 0, "end_char": 1911, "text_sha256": "dd98941694dedd8e3e85766c0c299b54fbc29ca8cce7c61a333efceee796867f"}

   experimental_model

   Neoglycolipid oligosaccharide microarrays built from three glucan polysaccharides and screened against 187 sequence-defined probes

   exposure

   Dectin-1 binding to oligosaccharide probes generated from a soluble yeast glucan, curdlan and pustulan

   limitations

   A binding assignment on arrayed probes rather than on a cell surface. The clustered-ligand test uses liposomes and a Dectin-1-expressing cell line.

   nutrient_topic

   Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. · Beta-glucan

   organism

   Recombinant protein and a macrophage cell line

   plain_language

   The receptor reads only one linkage, needs a run of about ten sugars to grip at all, and needs them clustered to fire.

   primary_references

   [bg-p16371356] Ligands for the beta-glucan receptor, Dectin-1, assigned using "designer" microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides. (2006). https://pubmed.ncbi.nlm.nih.gov/16371356/ DOI: 10.1074/jbc.m511461200

   tissue_or_cell_type

   Cell-free microarray and cultured cells

   Beta-glucan: a structural family rather than an agent, what decides whether a bound glucan actually signals, the complement route that a cereal and a yeast preparation share, and the unequal human evidence behind each (2026-09-22) · lines 125–136

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Neoglycolipid oligosaccharide microarrays built from three glucan polysaccharides and screened against 187 sequence-defined probes · source_derived_draft · unverified_draft

   ### bg-only-beta-1-3-oligomers-bind Dectin-1 lacks residues involved in calcium ligation that mediates carbohydrate-binding by classical C-type lectins, and among 187 diverse sequence-defined oligosaccharide probes together with designer microarrays from a neutral soluble glucan from S. cerevisiae, curdlan from Alcaligenes faecalis and pustulan from Umbilicaria papullosa, Dectin-1 binding is detected exclusively to 1,3-linked glucose oligomers, the minimum length required for detectable binding being a 10- or 11-mer, and 11-13 gluco-oligomers in clustered form displayed on liposomes mimic the macromolecular beta-glucans and compete with zymosan binding and triggering of tumour necrosis factor alpha secretion. Condition category: normal nutrient_topic: Beta-glucan research collection; topical membership is not evidence of a direct clinical effect, and each preparation is recorded as its own entity with no family link joining any pair. plain_language: The receptor reads only one linkage, needs a run of about ten sugars to grip at all, and needs them clustered to fire. organism: Recombinant protein and a macrophage cell line tissue_or_cell_type: Cell-free microarray and cultured cells experimental_model: Neoglycolipid oligosaccharide microarrays built from three glucan polysaccharides and screened against 187 sequence-defined probes limitations: A binding assignment on arrayed probes rather than on a cell surface. The clustered-ligand test uses liposomes and a Dectin-1-expressing cell line. exposure: Dectin-1 binding to oligosaccharide probes generated from a soluble yeast glucan, curdlan and pustulan evidence_span: {"source_cache": "artifacts/glucan-research/16371356.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dd98941694dedd8e3e85766c0c299b54fbc29ca8cce7c61a333efceee796867f", "start_char": 0, "end_char": 1911, "text_sha256": "dd98941694dedd8e3e85766c0c299b54fbc29ca8cce7c61a333efceee796867f"} [bg-p16371356] Ligands for the beta-glucan receptor, Dectin-1, assigned using "designer" microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides. (2006). https://pubmed.ncbi.nlm.nih.gov/16371356/ DOI: 10.1074/jbc.m511461200

   Complete structured claim and evidence