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2017 ; 28
(4
): 511-523
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The nanoscale spatial organization of B-cell receptors on immunoglobulin M- and
G-expressing human B-cells
#MMPMID27974642
Lee J
; Sengupta P
; Brzostowski J
; Lippincott-Schwartz J
; Pierce SK
Mol Biol Cell
2017[Feb]; 28
(4
): 511-523
PMID27974642
show ga
B-cell activation is initiated by the binding of antigen to the B-cell receptor
(BCR). Here we used dSTORM superresolution imaging to characterize the nanoscale
spatial organization of immunoglobulin M (IgM) and IgG BCRs on the surfaces of
resting and antigen--activated human peripheral blood B-cells. We provide
insights into both the fundamental process of antigen-driven BCR clustering and
differences in the spatial organization of IgM and IgG BCRs that may contribute
to the characteristic differences in the responses of naive and memory B-cells to
antigen. We provide evidence that although both IgM and IgG BCRs reside in highly
heterogeneous protein islands that vary in size and number of BCR single-molecule
localizations, both resting and activated B-cells intrinsically maintain a high
-frequency of single isolated BCR localizations, which likely represent BCR
monomers. IgG BCRs are more clustered than IgM BCRs on resting cells and form
larger protein islands after antigen activation. Small, dense BCR clusters likely
formed via protein-protein interactions are present on the surface of resting
cells, and antigen activation induces these to come together to form less dense,
larger islands, a process likely governed, at least in part, by protein-lipid
interactions.