Journal article
Specific Sialoforms Required for the Immune Suppressive Activity of Human Soluble CD52
Abdulrahman M Shathili, Esther Bandala-Sanchez, Alan John, Ethan D Goddard-Borger, Morten Thaysen-Andersen, Arun V Everest-Dass, Timothy E Adams, Leonard C Harrison, Nicolle H Packer
FRONTIERS IN IMMUNOLOGY | FRONTIERS MEDIA SA | Published : 2019
Abstract
Human CD52 is a small glycopeptide (12 amino acid residues) with one N-linked glycosylation site at asparagine 3 (Asn3) and several potential O-glycosylation serine/threonine sites. Soluble CD52 is released from the surface of activated T cells and mediates immune suppression via its glycan moiety. In suppressing activated T cells, it first sequesters the pro-inflammatory high mobility group Box 1 (HMGB1) protein, which facilitates its binding to the inhibitory sialic acid-binding immunoglobulin-like lectin-10 (Siglec-10) receptor. We aimed to identify the features of CD52 glycan that underlie its bioactivity. Analysis of native CD52 purified from human spleen revealed extensive heterogeneit..
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Awarded by Australian National Health and Medical Research Council (NHMRC)
Awarded by NHMRC
Awarded by Australian Research Council Centre of Excellence for Nanoscale Biophotonics
Funding Acknowledgements
This work was supported by an Australian National Health and Medical Research Council (NHMRC) Program Grant (1037321) and the Walter and Eliza Hall Institute Catalyst Fund. LH is the recipient of a NHMRC Senior Principal Research Fellowship (1080887). This work was made possible through Victorian State Government Operational Infrastructure Support and NHMRC Research Institute Infrastructure Support Scheme. This work was also funded by the Australian Research Council Centre of Excellence for Nanoscale Biophotonics (CE140100003) and was made possible via access to the Australian Proteome Analysis Facility (APAF). We thank Zeynep Sumer-Bayraktar for her assistance.