HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound
Summary: 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 w...
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| Format: | Article |
| Language: | English |
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Elsevier
2020-12-01
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| Series: | Cell Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124720314911 |
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doaj-708b5101342c4ee5a05e68d73b2077b4 |
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Article |
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DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Rasmus Offersen Wen-Han Yu Eileen P. Scully Boris Julg Zelda Euler Saheli Sadanand Dario Garcia-Dominguez Lu Zheng Thomas A. Rasmussen Madeleine F. Jennewein Caitlyn Linde Jessica Sassic Giuseppe Lofano Selena Vigano Kathryn E. Stephenson Stephanie Fischinger Todd J. Suscovich Mathias Lichterfeld Douglas Lauffenburger Erik S. Rosenberg Todd Allen Marcus Altfeld Richelle C. Charles Lars Østergaard Martin Tolstrup Dan H. Barouch Ole S. Søgaard Galit Alter |
| spellingShingle |
Rasmus Offersen Wen-Han Yu Eileen P. Scully Boris Julg Zelda Euler Saheli Sadanand Dario Garcia-Dominguez Lu Zheng Thomas A. Rasmussen Madeleine F. Jennewein Caitlyn Linde Jessica Sassic Giuseppe Lofano Selena Vigano Kathryn E. Stephenson Stephanie Fischinger Todd J. Suscovich Mathias Lichterfeld Douglas Lauffenburger Erik S. Rosenberg Todd Allen Marcus Altfeld Richelle C. Charles Lars Østergaard Martin Tolstrup Dan H. Barouch Ole S. Søgaard Galit Alter HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound Cell Reports HIV antibodies glycosylation viral host response biomarkers cure |
| author_facet |
Rasmus Offersen Wen-Han Yu Eileen P. Scully Boris Julg Zelda Euler Saheli Sadanand Dario Garcia-Dominguez Lu Zheng Thomas A. Rasmussen Madeleine F. Jennewein Caitlyn Linde Jessica Sassic Giuseppe Lofano Selena Vigano Kathryn E. Stephenson Stephanie Fischinger Todd J. Suscovich Mathias Lichterfeld Douglas Lauffenburger Erik S. Rosenberg Todd Allen Marcus Altfeld Richelle C. Charles Lars Østergaard Martin Tolstrup Dan H. Barouch Ole S. Søgaard Galit Alter |
| author_sort |
Rasmus Offersen |
| title |
HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound |
| title_short |
HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound |
| title_full |
HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound |
| title_fullStr |
HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound |
| title_full_unstemmed |
HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral Rebound |
| title_sort |
hiv antibody fc n-linked glycosylation is associated with viral rebound |
| publisher |
Elsevier |
| series |
Cell Reports |
| issn |
2211-1247 |
| publishDate |
2020-12-01 |
| description |
Summary: 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. |
| topic |
HIV antibodies glycosylation viral host response biomarkers cure |
| url |
http://www.sciencedirect.com/science/article/pii/S2211124720314911 |
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1724380436042350592 |
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doaj-708b5101342c4ee5a05e68d73b2077b42020-12-17T04:48:01ZengElsevierCell Reports2211-12472020-12-013311108502HIV Antibody Fc N-Linked Glycosylation Is Associated with Viral ReboundRasmus Offersen0Wen-Han Yu1Eileen P. Scully2Boris Julg3Zelda Euler4Saheli Sadanand5Dario Garcia-Dominguez6Lu Zheng7Thomas A. Rasmussen8Madeleine F. Jennewein9Caitlyn Linde10Jessica Sassic11Giuseppe Lofano12Selena Vigano13Kathryn E. Stephenson14Stephanie Fischinger15Todd J. Suscovich16Mathias Lichterfeld17Douglas Lauffenburger18Erik S. Rosenberg19Todd Allen20Marcus Altfeld21Richelle C. Charles22Lars Østergaard23Martin Tolstrup24Dan H. Barouch25Ole S. Søgaard26Galit Alter27Ragon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USA; Department of Infectious Diseases, Aarhus University Hospital, Aarhus 8000, Denmark; Department of Clinical Medicine, Aarhus University, Aarhus 8000, DenmarkRagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USA; Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USA; Department of Medicine, Division of Infectious Diseases, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USADepartment of Biostatistics, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USADepartment of Infectious Diseases, Aarhus University Hospital, Aarhus 8000, DenmarkRagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USACenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, MA 02115, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USADivision of Infectious Disease, Brigham and Women’s Hospital, Boston, MA 02115, USADepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USADivision of Infectious Disease, Massachusetts General Hospital, Boston, MA 02114, USARagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USAHeinrich Pette Institute, Leibniz Institute for Experimental Virology, 20251 Hamburg, GermanyDivision of Infectious Disease, Massachusetts General Hospital, Boston, MA 02114, USADepartment of Infectious Diseases, Aarhus University Hospital, Aarhus 8000, Denmark; Department of Clinical Medicine, Aarhus University, Aarhus 8000, DenmarkDepartment of Infectious Diseases, Aarhus University Hospital, Aarhus 8000, Denmark; Department of Clinical Medicine, Aarhus University, Aarhus 8000, DenmarkRagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USA; Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, MA 02115, USADepartment of Infectious Diseases, Aarhus University Hospital, Aarhus 8000, Denmark; Department of Clinical Medicine, Aarhus University, Aarhus 8000, DenmarkRagon Institute of MGH, MIT, and Harvard, Cambridge, MA 02139, USA; Corresponding authorSummary: 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.http://www.sciencedirect.com/science/article/pii/S2211124720314911HIVantibodiesglycosylationviral host responsebiomarkerscure |