Related Experiment Video
Updated: May 26, 2026

A Microphysiological System to Study Leukocyte-Endothelial Cell Interaction during Inflammation
Published on: December 9, 2021
M-ficolin and leukosialin (CD43): new partners in neutrophil adhesion
Andrea N Moreno-Amaral1, Evelyne Gout, Claudia Danella-Polli
1Batiment Lavoisier, Hôpital Necker, 149 rue de Sevres, Paris, France.
Abstract:
M-ficolin specificity for sialylated ligands prompted us to investigate its interactions with the main membrane sialoprotein of human neutrophils, CD43. rM-ficolin bound CD43 and prevented the access of anti-CD43 mAb. Moreover, rM-ficolin reacted exclusively with CD43 on Western blots of neutrophil lysate. We confirmed that M-ficolin is secreted by fMLP-activated neutrophils, and this endogenous M-ficolin also binds to CD43 and competes with anti-CD43 mAb. Anti-CD43 antibody cross-linking or fMLP resulted in M-ficolin and CD43 colocalization on polarized neutrophils. The binding of rM-ficolin to resting neutrophils induced cell polarization, adhesion, and homotypic aggregation as anti-CD43 mAb. The M-ficolin Y271F mutant, unable to bind sialic acid, neither reacted with neutrophils nor modulated their functions. Finally, rM-ficolin activated the lectin complement pathway on neutrophils. These results emphasize a new function of M-ficolin, different from ficolin pathogen recognition, i.e., a participation to neutrophil adhesion potentially important in early inflammation, as nanomolar agonist concentrations are sufficient to mobilize M-ficolin to the neutrophil surface. This multivalent lectin could then endow the antiadhesive CD43, essentially designed to prevent leukocyte aggregation in the blood flow, with new adhesive properties and explain, at least in part, dual-adhesive/antiadhesive roles of CD43 in neutrophil recruitment.
Insights
M-ficolin binds to CD43 on neutrophils, modulating their adhesion and aggregation. This interaction, distinct from pathogen recognition, highlights M-ficolin's role in early inflammation and neutrophil recruitment.
Area of Science:
- Immunology
- Cell Biology
Background:
- M-ficolin is a lectin known for pathogen recognition.
- CD43 is a major sialoprotein on human neutrophils with anti-adhesive properties.
Purpose of the Study:
- To investigate the interaction between M-ficolin and CD43 on human neutrophils.
- To determine the functional consequences of this interaction on neutrophil behavior and complement activation.
Main Methods:
- Recombinant M-ficolin (rM-ficolin) binding assays to neutrophils and Western blots.
- Analysis of M-ficolin secretion by fMLP-activated neutrophils.
- Immunofluorescence microscopy to assess colocalization of M-ficolin and CD43.
- Functional assays measuring neutrophil polarization, adhesion, and aggregation.
- Assessment of M-ficolin's effect on the lectin complement pathway.
Main Results:
- rM-ficolin binds specifically to CD43 on neutrophils, inhibiting anti-CD43 mAb binding.
- Endogenous M-ficolin secreted by activated neutrophils also binds CD43.
- M-ficolin and CD43 colocalize on activated neutrophils.
- rM-ficolin binding induces neutrophil polarization, adhesion, and aggregation.
- A M-ficolin mutant unable to bind sialic acid did not interact with neutrophils.
- rM-ficolin activated the lectin complement pathway on neutrophils.
Conclusions:
- M-ficolin interacts with CD43 on neutrophils, mediating novel adhesive functions.
- This interaction is independent of M-ficolin's known pathogen recognition role.
- M-ficolin binding to CD43 contributes to neutrophil adhesion and aggregation in early inflammation.
- M-ficolin may explain the dual adhesive/anti-adhesive roles of CD43 in neutrophil recruitment.
- M-ficolin activates the complement system on neutrophils.
Related Concept Videos
Selectins
Intracellular Signaling Affects Focal Adhesions
Some...
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Fibronectins Connect Cells with ECM
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Mechanism of Filopodia Formation
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Laminins are the Adhesive Proteins of Basal Lamina
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...

