Plasma membrane topography governs the 3D dynamic localization of IgM B cell antigen receptor clusters

Deniz Saltukoglu1,2, Bugra Özdemir2,3, Michael Holtmannspötter4

  • 1Department of Molecular Immunology, Biology III, Faculty of Biology, University of Freiburg, Freiburg, Germany.

The EMBO Journal
|January 3, 2023
PubMed

Insights

B cells use dynamic surface structures called microvilli and ridges to screen antigens. This cell surface topography guides the movement of the B cell antigen receptor (BCR), enhancing antigen detection.

Area of Science:

  • Immunology
  • Cell Biology
  • Biophysics

Background:

  • B lymphocytes are crucial for adaptive immunity, recognizing antigens via B cell receptors (BCR).
  • Lymphocyte microvilli are cell surface protrusions involved in sensory functions, including antigen screening.
  • The B cell antigen receptor (BCR), particularly IgM-BCR, plays a vital role in initiating immune responses.

Purpose of the Study:

  • To investigate the dynamic cell-surface topography of B cells.
  • To understand the spatiotemporal organization of the IgM-BCR on B cell surfaces.
  • To elucidate the relationship between cell surface structures and BCR mobility for antigen screening.

Main Methods:

  • Utilized lattice light-sheet microscopy for high-resolution imaging of B cells.
  • Employed custom-built 4D image analysis to study dynamic cellular processes.
  • Investigated Ramos Burkitt's Lymphoma B cells to analyze surface topography and IgM-BCR organization.

Main Results:

  • Ramos B cell surfaces exhibit dynamic networks of ridges connecting microvilli.
  • IgM-BCR clusters were predominantly found on these ridges and microvilli.
  • The organization of the ridge network and IgM-BCR cluster mobility are interdependent and regulated by Arp2/3 complex activity.

Conclusions:

  • Dynamic cell surface topography significantly influences IgM-BCR cluster localization and transport.
  • These topographical features are essential for efficient antigen screening by B cells.
  • Arp2/3 complex activity is a key regulator of both surface dynamics and BCR organization.

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