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clusters on the cell surface
Image courtesy of V.
Altounian/Science Signaling
New research has provided a clearer picture of the B-cell surface, unearthing new insights regarding antigen receptors.
Mature B cells have 2 classes of antigen receptors on their surface, immunoglobulin M (IgM) and immunoglobulin D (IgD).
Using multiple imaging techniques, researchers studied the spatial relationship of these receptor types in B cells from cell lines, mice, and human blood.
The team described this work in Science Signaling.
Receptors on the surface of resting T cells are thought to reside in preformed clusters known as protein islands, but whether these islands exist on B cells has been unclear.
Palash Maity, PhD, of the University of Freiburg in Germany, and colleagues found these islands do exist on B cells, but their structure changes upon B-cell activation.
Using 2-color direct stochastical optical reconstruction microscopy (dSTORM), the researchers found that IgM and IgD reside on the plasma membrane of resting B cells in separate protein islands of approximately 150 and 240 nanometers, respectively.
The team also observed this class-specific compartmentalization of the antigen receptors using transmission electron microscopy (TEM) and Fab-based proximity-ligation assay (Fab-PLA).
However, the researchers noted a change during B-cell activation. Upon activation, the IgM and IgD protein islands broke up into smaller islands, allowing the 2 types to intermingle, although they did not make direct contact.
The researchers said it is not clear whether this increased affinity between the receptor types is a result of a direct interaction or is mediated by an adaptor protein. The function of the association between the receptors is not clear, either.
But the team believes that one possibility is that, upon B-cell activation, the IgM and IgD protein islands form nanosynapses that allow the islands to exchange proteins and lipids with one another.
The researchers hope these new insights into the nanoscale organization of antigen receptors will support the design of more efficient vaccines or better treatments for B-cell tumors, in which membrane organization is often altered. 
clusters on the cell surface
Image courtesy of V.
Altounian/Science Signaling
New research has provided a clearer picture of the B-cell surface, unearthing new insights regarding antigen receptors.
Mature B cells have 2 classes of antigen receptors on their surface, immunoglobulin M (IgM) and immunoglobulin D (IgD).
Using multiple imaging techniques, researchers studied the spatial relationship of these receptor types in B cells from cell lines, mice, and human blood.
The team described this work in Science Signaling.
Receptors on the surface of resting T cells are thought to reside in preformed clusters known as protein islands, but whether these islands exist on B cells has been unclear.
Palash Maity, PhD, of the University of Freiburg in Germany, and colleagues found these islands do exist on B cells, but their structure changes upon B-cell activation.
Using 2-color direct stochastical optical reconstruction microscopy (dSTORM), the researchers found that IgM and IgD reside on the plasma membrane of resting B cells in separate protein islands of approximately 150 and 240 nanometers, respectively.
The team also observed this class-specific compartmentalization of the antigen receptors using transmission electron microscopy (TEM) and Fab-based proximity-ligation assay (Fab-PLA).
However, the researchers noted a change during B-cell activation. Upon activation, the IgM and IgD protein islands broke up into smaller islands, allowing the 2 types to intermingle, although they did not make direct contact.
The researchers said it is not clear whether this increased affinity between the receptor types is a result of a direct interaction or is mediated by an adaptor protein. The function of the association between the receptors is not clear, either.
But the team believes that one possibility is that, upon B-cell activation, the IgM and IgD protein islands form nanosynapses that allow the islands to exchange proteins and lipids with one another.
The researchers hope these new insights into the nanoscale organization of antigen receptors will support the design of more efficient vaccines or better treatments for B-cell tumors, in which membrane organization is often altered.
clusters on the cell surface
Image courtesy of V.
Altounian/Science Signaling
New research has provided a clearer picture of the B-cell surface, unearthing new insights regarding antigen receptors.
Mature B cells have 2 classes of antigen receptors on their surface, immunoglobulin M (IgM) and immunoglobulin D (IgD).
Using multiple imaging techniques, researchers studied the spatial relationship of these receptor types in B cells from cell lines, mice, and human blood.
The team described this work in Science Signaling.
Receptors on the surface of resting T cells are thought to reside in preformed clusters known as protein islands, but whether these islands exist on B cells has been unclear.
Palash Maity, PhD, of the University of Freiburg in Germany, and colleagues found these islands do exist on B cells, but their structure changes upon B-cell activation.
Using 2-color direct stochastical optical reconstruction microscopy (dSTORM), the researchers found that IgM and IgD reside on the plasma membrane of resting B cells in separate protein islands of approximately 150 and 240 nanometers, respectively.
The team also observed this class-specific compartmentalization of the antigen receptors using transmission electron microscopy (TEM) and Fab-based proximity-ligation assay (Fab-PLA).
However, the researchers noted a change during B-cell activation. Upon activation, the IgM and IgD protein islands broke up into smaller islands, allowing the 2 types to intermingle, although they did not make direct contact.
The researchers said it is not clear whether this increased affinity between the receptor types is a result of a direct interaction or is mediated by an adaptor protein. The function of the association between the receptors is not clear, either.
But the team believes that one possibility is that, upon B-cell activation, the IgM and IgD protein islands form nanosynapses that allow the islands to exchange proteins and lipids with one another.
The researchers hope these new insights into the nanoscale organization of antigen receptors will support the design of more efficient vaccines or better treatments for B-cell tumors, in which membrane organization is often altered.