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...

Descripción completa

Detalles Bibliográficos
Autores principales: Lee, Jinmin, Sengupta, Prabuddha, Brzostowski, Joseph, Lippincott-Schwartz, Jennifer, Pierce, Susan K.
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