Cargando…
The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells
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-cell...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5305258/ https://www.ncbi.nlm.nih.gov/pubmed/27974642 http://dx.doi.org/10.1091/mbc.E16-06-0452 |
_version_ | 1782507020787646464 |
---|---|
author | Lee, Jinmin Sengupta, Prabuddha Brzostowski, Joseph Lippincott-Schwartz, Jennifer Pierce, Susan K. |
author_facet | Lee, Jinmin Sengupta, Prabuddha Brzostowski, Joseph Lippincott-Schwartz, Jennifer Pierce, Susan K. |
author_sort | Lee, Jinmin |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5305258 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-53052582017-04-30 The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells Lee, Jinmin Sengupta, Prabuddha Brzostowski, Joseph Lippincott-Schwartz, Jennifer Pierce, Susan K. Mol Biol Cell Articles 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. The American Society for Cell Biology 2017-02-15 /pmc/articles/PMC5305258/ /pubmed/27974642 http://dx.doi.org/10.1091/mbc.E16-06-0452 Text en © 2017 Lee, Sengupta, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Lee, Jinmin Sengupta, Prabuddha Brzostowski, Joseph Lippincott-Schwartz, Jennifer Pierce, Susan K. The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells |
title | The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells |
title_full | The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells |
title_fullStr | The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells |
title_full_unstemmed | The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells |
title_short | The nanoscale spatial organization of B-cell receptors on immunoglobulin M– and G–expressing human B-cells |
title_sort | nanoscale spatial organization of b-cell receptors on immunoglobulin m– and g–expressing human b-cells |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5305258/ https://www.ncbi.nlm.nih.gov/pubmed/27974642 http://dx.doi.org/10.1091/mbc.E16-06-0452 |
work_keys_str_mv | AT leejinmin thenanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT senguptaprabuddha thenanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT brzostowskijoseph thenanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT lippincottschwartzjennifer thenanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT piercesusank thenanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT leejinmin nanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT senguptaprabuddha nanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT brzostowskijoseph nanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT lippincottschwartzjennifer nanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells AT piercesusank nanoscalespatialorganizationofbcellreceptorsonimmunoglobulinmandgexpressinghumanbcells |