HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound
Name
1-s2.0-S2211124720314911-main.pdf
Description
Published version
Size
1.67 MB
Format
Adobe PDF
Checksum (MD5)
82b309f45e164cf6f65467801b9353cd
Author(s)
Offersen, Rasmus
Yu, Wen-Han
Scully, Eileen P
Julg, Boris
Euler, Zelda
Sadanand, Saheli
Garcia-Dominguez, Dario
Zheng, Lu
Rasmussen, Thomas A
Jennewein, Madeleine F
Date Issued
2020
Journal
Cell Reports
Publisher
Elsevier BV
Version
Final published version
Abstract
© 2020 The Authors Changes in antibody glycosylation are linked to inflammation across several diseases. Alterations in bulk antibody galactosylation can predict rheumatic flares, act as a sensor for immune activation, predict gastric cancer relapse, track with biological age, shift with vaccination, change with HIV reservoir size on therapy, and decrease in HIV and HCV infections. However, whether changes in antibody Fc biology also track with reservoir rebound time remains unclear. The identification of a biomarker that could forecast viral rebound time could significantly accelerate the downselection and iterative improvement of promising HIV viral eradication strategies. Using a comprehensive antibody Fc-profiling approach, the level of HIV-specific antibody Fc N-galactosylation is significantly associated with time to rebound after treatment discontinuation across three independent cohorts. Thus virus-specific antibody glycosylation may represent a promising, simply measured marker to track reservoir reactivation.
MIT Department
Ragon Institute of MGH, MIT and Harvard
Massachusetts Institute of Technology. Department of Biological Engineering
Terms of Use
Creative Commons Attribution 4.0 International license
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/J.CELREP.2020.108502
