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Martijn’s paper on germinal center B-cell glycans is online

A new study links germinal center-associated N-glycan remodeling with reduced recombinant CD22 binding in human B cells.

A new study links germinal center-associated N-glycan remodeling with reduced recombinant CD22 binding in human B cells.
Martijn Breeuwsma

We’re happy to share that Martijn Breeuwsma’s new paper is now published in Biochemical and Biophysical Research Communications. The study examines how human B cells remodel their surface N-glycans as they develop, and how these changes relate to binding by CD22.

N-glycans are sugar chains attached to proteins. Some of these structures can be recognized by CD22, an inhibitory receptor that helps regulate B-cell signaling. Martijn and colleagues profiled N-glycans across human B-cell subsets and measured cell-surface binding of recombinant CD22.

They found that recombinant CD22 binding was reduced in germinal center B-cell subsets, despite largely stable CD22 expression. This identifies an association between germinal center-associated N-glycan remodeling and reduced CD22 binding.

The results do not establish that particular glycan changes cause the reduction or alter CD22 signaling. Further direct-binding and perturbation experiments will be needed to test the role of individual glycan structures. The study provides a new perspective on how glycan remodeling during the germinal center response may shape interactions at the B-cell surface.

Read the paper: Germinal center-associated N-glycan remodeling correlates with reduced recombinant CD22 binding in human B cells.

Martijn, congratulations on the publication!

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