Complement receptor 3 / CD11b-CD18

Where it participates (unsigned role)

1. Recent data indicated that barley beta-1,3;1,4-glucan given orally potentiated the activity of antitumour monoclonal antibody leading to enhanced tumour regression and survival, and this investigation showed that orally administered yeast beta-1,3;1,6-glucan functioned similarly to barley beta-1,3;1,4-glucan with antitumour monoclonal antibody, with both oral beta-1,3-glucans a requirement for iC3b on tumours and CR3 on granulocytes being confirmed by demonstrating therapeutic failures in mice deficient in C3 or CR3.

   Barley mixed-linkage beta-(1->3)/(1->4)-glucan → Yeast beta-(1->3)/(1->6)-glucan source_derived_draftungraded
   Experimental context and source evidence

   availability_state

   machinery_impairment Imported condition classification; unverified.

   evidence_span

   {"source_cache": "artifacts/glucan-research/15240666.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781", "start_char": 0, "end_char": 1454, "text_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781"}

   experimental_model

   Fluorescein-labelled oral glucans tracked through macrophages to marrow, with therapy in C3-deficient and CR3-deficient mice

   exposure

   Orally administered barley beta-1,3;1,4-glucan and orally administered yeast beta-1,3;1,6-glucan, each with antitumour monoclonal antibody

   limitations

   The single experiment in this collection that tested a cereal mixed-linkage glucan and a yeast branched glucan side by side in the same protocol. It is a mouse tumour model, and oral uptake in mice does not establish the same uptake in people.

   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

   A cereal glucan and a yeast glucan did the same job by the same route, which is the result that refuses to let the two be filed apart.

   primary_references

   [bg-p15240666] Mechanism by which orally administered beta-1,3-glucans enhance the tumoricidal activity of antitumor monoclonal antibodies in murine tumor models. (2004). https://pubmed.ncbi.nlm.nih.gov/15240666/ DOI: 10.4049/jimmunol.173.2.797

   tissue_or_cell_type

   Gut, spleen, lymph node, bone marrow and tumour

   trigger_kind

   machinery_impairment Imported condition classification; unverified.

   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 242–253

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fluorescein-labelled oral glucans tracked through macrophages to marrow, with therapy in C3-deficient and CR3-deficient mice · source_derived_draft · unverified_draft

   ### bg-barley-and-yeast-converge Recent data indicated that barley beta-1,3;1,4-glucan given orally potentiated the activity of antitumour monoclonal antibody leading to enhanced tumour regression and survival, and this investigation showed that orally administered yeast beta-1,3;1,6-glucan functioned similarly to barley beta-1,3;1,4-glucan with antitumour monoclonal antibody, with both oral beta-1,3-glucans a requirement for iC3b on tumours and CR3 on granulocytes being confirmed by demonstrating therapeutic failures in mice deficient in C3 or CR3. Condition category: machinery_impairment 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: A cereal glucan and a yeast glucan did the same job by the same route, which is the result that refuses to let the two be filed apart. organism: Mouse tissue_or_cell_type: Gut, spleen, lymph node, bone marrow and tumour experimental_model: Fluorescein-labelled oral glucans tracked through macrophages to marrow, with therapy in C3-deficient and CR3-deficient mice limitations: The single experiment in this collection that tested a cereal mixed-linkage glucan and a yeast branched glucan side by side in the same protocol. It is a mouse tumour model, and oral uptake in mice does not establish the same uptake in people. exposure: Orally administered barley beta-1,3;1,4-glucan and orally administered yeast beta-1,3;1,6-glucan, each with antitumour monoclonal antibody evidence_span: {"source_cache": "artifacts/glucan-research/15240666.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781", "start_char": 0, "end_char": 1454, "text_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781"} [bg-p15240666] Mechanism by which orally administered beta-1,3-glucans enhance the tumoricidal activity of antitumor monoclonal antibodies in murine tumor models. (2004). https://pubmed.ncbi.nlm.nih.gov/15240666/ DOI: 10.4049/jimmunol.173.2.797

   Complete structured claim and evidence

2. The carbohydrate polymers known as beta-1,3-D-glucans exert potent effects on the immune system, stimulating antitumour and antimicrobial activity for example, by binding to receptors on macrophages and other white blood cells and activating them, and although beta-glucans are known to bind to receptors such as complement receptor 3 there is evidence that another beta-glucan receptor is present on macrophages, which is identified here as dectin-1.

   Dectin-1 / CLEC7A → Beta-glucan source_derived_draftungraded
   Experimental context and source evidence

   evidence_span

   {"source_cache": "artifacts/glucan-research/11544516.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14e7f5285cdda3bdcf3596e5e9517683d195dd4a4ae42ff1f9d07f1d3288bf1c", "start_char": 0, "end_char": 573, "text_sha256": "14e7f5285cdda3bdcf3596e5e9517683d195dd4a4ae42ff1f9d07f1d3288bf1c"}

   experimental_model

   Identification of the unknown macrophage beta-glucan receptor

   exposure

   Beta-1,3-D-glucans binding to macrophage surface receptors

   limitations

   A brief communication announcing the identification. It states that beta-glucans were already known to bind complement receptor 3, so it adds a receptor rather than replacing one.

   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 and human cells

   plain_language

   A second receptor for these sugars was identified, alongside the complement receptor already known to bind them.

   primary_references

   [bg-p11544516] Immune recognition. A new receptor for beta-glucans. (2001). https://pubmed.ncbi.nlm.nih.gov/11544516/ DOI: 10.1038/35092620

   tissue_or_cell_type

   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 99–110

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Identification of the unknown macrophage beta-glucan receptor · source_derived_draft · unverified_draft

   ### bg-dectin1-is-the-unknown-receptor The carbohydrate polymers known as beta-1,3-D-glucans exert potent effects on the immune system, stimulating antitumour and antimicrobial activity for example, by binding to receptors on macrophages and other white blood cells and activating them, and although beta-glucans are known to bind to receptors such as complement receptor 3 there is evidence that another beta-glucan receptor is present on macrophages, which is identified here as dectin-1. 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: A second receptor for these sugars was identified, alongside the complement receptor already known to bind them. organism: Mouse and human cells tissue_or_cell_type: Macrophage experimental_model: Identification of the unknown macrophage beta-glucan receptor limitations: A brief communication announcing the identification. It states that beta-glucans were already known to bind complement receptor 3, so it adds a receptor rather than replacing one. exposure: Beta-1,3-D-glucans binding to macrophage surface receptors evidence_span: {"source_cache": "artifacts/glucan-research/11544516.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14e7f5285cdda3bdcf3596e5e9517683d195dd4a4ae42ff1f9d07f1d3288bf1c", "start_char": 0, "end_char": 573, "text_sha256": "14e7f5285cdda3bdcf3596e5e9517683d195dd4a4ae42ff1f9d07f1d3288bf1c"} [bg-p11544516] Immune recognition. A new receptor for beta-glucans. (2001). https://pubmed.ncbi.nlm.nih.gov/11544516/ DOI: 10.1038/35092620

   Complete structured claim and evidence

3. 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

4. Imprime-induced anti-cancer functionality is dependent on immune complex formation with naturally-occurring anti-beta glucan antibodies, the formation of Imprime-antibody complexes activates complement primarily via the classical complement pathway and is opsonised by iC3b, immune complex binding depends upon Complement Receptor 3 and Fc gamma Receptor IIa eliciting phenotypic activation of and enhanced chemokine production by neutrophils and monocytes enabling these effector cells to kill antibody-opsonized tumour cells, and importantly these innate immune cell changes were not evident in subjects with low antibody levels but could be rescued with exogenous antibody supplementation.

   Naturally occurring anti-beta-glucan IgG antibodies → Imprime PGG / BTH1677, a soluble yeast beta-(1->3)/(1->6)-glucan source_derived_draftungraded
   Experimental context and source evidence

   evidence_span

   {"source_cache": "artifacts/glucan-research/27812183.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "949fc5939bec2e3fab259b6b6161fba8cdd7779c7efa0261a1e7dbf1cab111cf", "start_char": 0, "end_char": 1493, "text_sha256": "949fc5939bec2e3fab259b6b6161fba8cdd7779c7efa0261a1e7dbf1cab111cf"}

   experimental_model

   Whole blood from healthy human subjects with antibody-depleted and antibody-supplemented conditions

   exposure

   Imprime PGG in whole blood across a range of naturally occurring anti-beta-glucan antibody levels

   limitations

   Ex vivo whole blood rather than treated patients. The antibody dependence is demonstrated both by absence in low-antibody donors and by rescue with added antibody.

   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

   Human

   plain_language

   This soluble glucan does nothing on its own; it has to be caught by an antibody the person already had.

   primary_references

   [bg-p27812183] Imprime PGG-Mediated Anti-Cancer Immune Activation Requires Immune Complex Formation. (2016). https://pubmed.ncbi.nlm.nih.gov/27812183/ DOI: 10.1371/journal.pone.0165909

   tissue_or_cell_type

   Whole blood, neutrophil and monocyte

   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 268–279

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Whole blood from healthy human subjects with antibody-depleted and antibody-supplemented conditions · source_derived_draft · unverified_draft

   ### bg-imprime-needs-an-antibody-first Imprime-induced anti-cancer functionality is dependent on immune complex formation with naturally-occurring anti-beta glucan antibodies, the formation of Imprime-antibody complexes activates complement primarily via the classical complement pathway and is opsonised by iC3b, immune complex binding depends upon Complement Receptor 3 and Fc gamma Receptor IIa eliciting phenotypic activation of and enhanced chemokine production by neutrophils and monocytes enabling these effector cells to kill antibody-opsonized tumour cells, and importantly these innate immune cell changes were not evident in subjects with low antibody levels but could be rescued with exogenous antibody supplementation. 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: This soluble glucan does nothing on its own; it has to be caught by an antibody the person already had. organism: Human tissue_or_cell_type: Whole blood, neutrophil and monocyte experimental_model: Whole blood from healthy human subjects with antibody-depleted and antibody-supplemented conditions limitations: Ex vivo whole blood rather than treated patients. The antibody dependence is demonstrated both by absence in low-antibody donors and by rescue with added antibody. exposure: Imprime PGG in whole blood across a range of naturally occurring anti-beta-glucan antibody levels evidence_span: {"source_cache": "artifacts/glucan-research/27812183.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "949fc5939bec2e3fab259b6b6161fba8cdd7779c7efa0261a1e7dbf1cab111cf", "start_char": 0, "end_char": 1493, "text_sha256": "949fc5939bec2e3fab259b6b6161fba8cdd7779c7efa0261a1e7dbf1cab111cf"} [bg-p27812183] Imprime PGG-Mediated Anti-Cancer Immune Activation Requires Immune Complex Formation. (2016). https://pubmed.ncbi.nlm.nih.gov/27812183/ DOI: 10.1371/journal.pone.0165909

   Complete structured claim and evidence

5. Barley and yeast beta-1,3-glucan were labelled with fluorescein to track their oral uptake and processing in vivo, orally administered beta-1,3-glucans were taken up by macrophages that transported them to spleen, lymph nodes and bone marrow, within the bone marrow the macrophages degraded the large beta-1,3-glucans into smaller soluble beta-1,3-glucan fragments that were taken up by the CR3 of marginated granulocytes, and these granulocytes with CR3-bound beta-1,3-glucan-fluorescein were shown to kill iC3b-opsonized tumour cells following their recruitment to a site of complement activation resembling a tumour coated with monoclonal antibody.

   Transport of ingested glucan by macrophages to spleen, lymph node and marrow → Beta-(1->3)-linked gluco-oligosaccharides source_derived_draftungraded
   Experimental context and source evidence

   evidence_span

   {"source_cache": "artifacts/glucan-research/15240666.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781", "start_char": 0, "end_char": 1454, "text_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781"}

   experimental_model

   Fluorescein-labelled oral glucans tracked through macrophages to marrow, with therapy in C3-deficient and CR3-deficient mice

   exposure

   Orally administered barley beta-1,3;1,4-glucan and orally administered yeast beta-1,3;1,6-glucan, each with antitumour monoclonal antibody

   limitations

   The single experiment in this collection that tested a cereal mixed-linkage glucan and a yeast branched glucan side by side in the same protocol. It is a mouse tumour model, and oral uptake in mice does not establish the same uptake in people.

   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

   Swallowed glucan is carried to the marrow inside macrophages, cut up there, and handed to granulocytes on the way out.

   primary_references

   [bg-p15240666] Mechanism by which orally administered beta-1,3-glucans enhance the tumoricidal activity of antitumor monoclonal antibodies in murine tumor models. (2004). https://pubmed.ncbi.nlm.nih.gov/15240666/ DOI: 10.4049/jimmunol.173.2.797

   tissue_or_cell_type

   Gut, spleen, lymph node, bone marrow and tumour

   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 255–266

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fluorescein-labelled oral glucans tracked through macrophages to marrow, with therapy in C3-deficient and CR3-deficient mice · source_derived_draft · unverified_draft

   ### bg-macrophages-carry-and-cut-it Barley and yeast beta-1,3-glucan were labelled with fluorescein to track their oral uptake and processing in vivo, orally administered beta-1,3-glucans were taken up by macrophages that transported them to spleen, lymph nodes and bone marrow, within the bone marrow the macrophages degraded the large beta-1,3-glucans into smaller soluble beta-1,3-glucan fragments that were taken up by the CR3 of marginated granulocytes, and these granulocytes with CR3-bound beta-1,3-glucan-fluorescein were shown to kill iC3b-opsonized tumour cells following their recruitment to a site of complement activation resembling a tumour coated with monoclonal antibody. 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: Swallowed glucan is carried to the marrow inside macrophages, cut up there, and handed to granulocytes on the way out. organism: Mouse tissue_or_cell_type: Gut, spleen, lymph node, bone marrow and tumour experimental_model: Fluorescein-labelled oral glucans tracked through macrophages to marrow, with therapy in C3-deficient and CR3-deficient mice limitations: The single experiment in this collection that tested a cereal mixed-linkage glucan and a yeast branched glucan side by side in the same protocol. It is a mouse tumour model, and oral uptake in mice does not establish the same uptake in people. exposure: Orally administered barley beta-1,3;1,4-glucan and orally administered yeast beta-1,3;1,6-glucan, each with antitumour monoclonal antibody evidence_span: {"source_cache": "artifacts/glucan-research/15240666.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781", "start_char": 0, "end_char": 1454, "text_sha256": "eaff7297fa40df19ef82e5e1de433ec0cf34590a7e3fda6aa6061e0922666781"} [bg-p15240666] Mechanism by which orally administered beta-1,3-glucans enhance the tumoricidal activity of antitumor monoclonal antibodies in murine tumor models. (2004). https://pubmed.ncbi.nlm.nih.gov/15240666/ DOI: 10.4049/jimmunol.173.2.797

   Complete structured claim and evidence

6. In comparison with antitumour monoclonal antibody or beta-glucan alone, combined treatment produced significantly greater tumour regression in all five models, tumour-free survival only occurred in models that incorporated stable expression of the target antigen, beta-glucan enhancement of the monoclonal antibody tumoricidal response did not occur in mice deficient in either leukocyte CR3 or serum C3 confirming the requirement for CR3 on leukocytes and iC3b on tumours, and granulocytes appeared to be primarily responsible for tumoricidal activity because beta-glucan therapeutic responses did not occur in granulocyte-depleted mice.

   Beta-glucan → Complement-activating antitumour monoclonal antibodies source_derived_draftungraded
   Experimental context and source evidence

   availability_state

   machinery_impairment Imported condition classification; unverified.

   evidence_span

   {"source_cache": "artifacts/glucan-research/14695221.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "810d6af738d83f5bd304be109db27808437a1f7fb7398253366d88d0b258ccc5", "start_char": 0, "end_char": 1827, "text_sha256": "810d6af738d83f5bd304be109db27808437a1f7fb7398253366d88d0b258ccc5"}

   experimental_model

   Five mouse tumour models with antitumour monoclonal antibody, in CR3-deficient, C3-deficient and granulocyte-depleted animals

   exposure

   Intravenous beta-glucan combined with antitumour monoclonal antibodies in BALB/c and C57Bl/6 mice

   limitations

   Five models with genetic and depletion controls, which is what makes the requirement claim strong. Tumour-free survival occurred only where the target antigen was stably expressed.

   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

   Take away the complement protein, the receptor, or the granulocytes, and the effect disappears entirely.

   primary_references

   [bg-p14695221] Beta-glucan functions as an adjuvant for monoclonal antibody immunotherapy by recruiting tumoricidal granulocytes as killer cells. (2003). https://pubmed.ncbi.nlm.nih.gov/14695221/

   tissue_or_cell_type

   Mammary, subcutaneous and hepatic tumours

   trigger_kind

   machinery_impairment Imported condition classification; unverified.

   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 229–240

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Five mouse tumour models with antitumour monoclonal antibody, in CR3-deficient, C3-deficient and granulocyte-depleted animals · source_derived_draft · unverified_draft

   ### bg-needs-cr3-c3-and-granulocytes In comparison with antitumour monoclonal antibody or beta-glucan alone, combined treatment produced significantly greater tumour regression in all five models, tumour-free survival only occurred in models that incorporated stable expression of the target antigen, beta-glucan enhancement of the monoclonal antibody tumoricidal response did not occur in mice deficient in either leukocyte CR3 or serum C3 confirming the requirement for CR3 on leukocytes and iC3b on tumours, and granulocytes appeared to be primarily responsible for tumoricidal activity because beta-glucan therapeutic responses did not occur in granulocyte-depleted mice. Condition category: machinery_impairment 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: Take away the complement protein, the receptor, or the granulocytes, and the effect disappears entirely. organism: Mouse tissue_or_cell_type: Mammary, subcutaneous and hepatic tumours experimental_model: Five mouse tumour models with antitumour monoclonal antibody, in CR3-deficient, C3-deficient and granulocyte-depleted animals limitations: Five models with genetic and depletion controls, which is what makes the requirement claim strong. Tumour-free survival occurred only where the target antigen was stably expressed. exposure: Intravenous beta-glucan combined with antitumour monoclonal antibodies in BALB/c and C57Bl/6 mice evidence_span: {"source_cache": "artifacts/glucan-research/14695221.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "810d6af738d83f5bd304be109db27808437a1f7fb7398253366d88d0b258ccc5", "start_char": 0, "end_char": 1827, "text_sha256": "810d6af738d83f5bd304be109db27808437a1f7fb7398253366d88d0b258ccc5"} [bg-p14695221] Beta-glucan functions as an adjuvant for monoclonal antibody immunotherapy by recruiting tumoricidal granulocytes as killer cells. (2003). https://pubmed.ncbi.nlm.nih.gov/14695221/

   Complete structured claim and evidence

7. When phagocyte or natural killer cell CR3 adheres to iC3b on erythrocytes or tumour cells that lack CR3-binding membrane polysaccharides neither lysis nor cytotoxicity are stimulated, but soluble CR3-specific polysaccharides such as beta-glucan induced a primed state of CR3 that could trigger killing of iC3b-target cells that were otherwise resistant to cytotoxicity, priming required tyrosine kinases and a magnesium-dependent conformational change of the I-domain that exposed the CBRM1/5 activation epitope, and unlike LPS or cytokines polysaccharides did not up-regulate neutrophil CR3 expression nor expose the high affinity ICAM-1-binding state.

   Beta-glucan → The primed state of complement receptor 3 source_derived_draftungraded
   Experimental context and source evidence

   evidence_span

   {"source_cache": "artifacts/glucan-research/8690804.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e6e6ce1cbb7d4a4d3170e4b86ac33d4b3220d59645c53d757fe3a2681397287e", "start_char": 0, "end_char": 1478, "text_sha256": "e6e6ce1cbb7d4a4d3170e4b86ac33d4b3220d59645c53d757fe3a2681397287e"}

   experimental_model

   Priming of neutrophil and natural killer cell CR3 with soluble polysaccharide, then challenge with iC3b-coated targets

   exposure

   Soluble CR3-specific polysaccharides including beta-glucan, with antibody blockade before or after the sugar

   limitations

   An in vitro cytotoxicity mechanism. It establishes how priming works and what it requires, not that the same sequence occurs in a treated patient.

   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

   Human

   plain_language

   The sugar does not make the killer cell find the tumour; it changes the receptor so that a target it was already touching becomes one it will kill.

   primary_references

   [bg-p8690804] Soluble beta-glucan polysaccharide binding to the lectin site of neutrophil or natural killer cell complement receptor type 3 (CD11b/CD18) generates a primed state of the receptor capable of mediating cytotoxicity of iC3b-opsonized target cells. (1996). https://pubmed.ncbi.nlm.nih.gov/8690804/ DOI: 10.1172/jci118777

   tissue_or_cell_type

   Neutrophil and natural killer 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 216–227

   AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Priming of neutrophil and natural killer cell CR3 with soluble polysaccharide, then challenge with iC3b-coated targets · source_derived_draft · unverified_draft

   ### bg-soluble-glucan-primes-cr3 When phagocyte or natural killer cell CR3 adheres to iC3b on erythrocytes or tumour cells that lack CR3-binding membrane polysaccharides neither lysis nor cytotoxicity are stimulated, but soluble CR3-specific polysaccharides such as beta-glucan induced a primed state of CR3 that could trigger killing of iC3b-target cells that were otherwise resistant to cytotoxicity, priming required tyrosine kinases and a magnesium-dependent conformational change of the I-domain that exposed the CBRM1/5 activation epitope, and unlike LPS or cytokines polysaccharides did not up-regulate neutrophil CR3 expression nor expose the high affinity ICAM-1-binding state. 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 sugar does not make the killer cell find the tumour; it changes the receptor so that a target it was already touching becomes one it will kill. organism: Human tissue_or_cell_type: Neutrophil and natural killer cell experimental_model: Priming of neutrophil and natural killer cell CR3 with soluble polysaccharide, then challenge with iC3b-coated targets limitations: An in vitro cytotoxicity mechanism. It establishes how priming works and what it requires, not that the same sequence occurs in a treated patient. exposure: Soluble CR3-specific polysaccharides including beta-glucan, with antibody blockade before or after the sugar evidence_span: {"source_cache": "artifacts/glucan-research/8690804.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e6e6ce1cbb7d4a4d3170e4b86ac33d4b3220d59645c53d757fe3a2681397287e", "start_char": 0, "end_char": 1478, "text_sha256": "e6e6ce1cbb7d4a4d3170e4b86ac33d4b3220d59645c53d757fe3a2681397287e"} [bg-p8690804] Soluble beta-glucan polysaccharide binding to the lectin site of neutrophil or natural killer cell complement receptor type 3 (CD11b/CD18) generates a primed state of the receptor capable of mediating cytotoxicity of iC3b-opsonized target cells. (1996). https://pubmed.ncbi.nlm.nih.gov/8690804/ DOI: 10.1172/jci118777

   Complete structured claim and evidence