Interferon-α alters host glycosylation machinery during treated HIV infection
Leila B. Giron, Florent Colomb, Emmanouil Papasavvas, Livio Azzoni, Xiangfan Yin, Matthew Fair, Alitzel Anzurez, Mohammad Damra, Karam Mounzer, Jay R. Kostman, Pablo Tebas, Una O’Doherty, Hiroaki Tateno, Qin Liu, Michael R. Betts, Luis J. Montaner, Mohamed Abdel‐Mohsen
Abstract
BACKGROUND: A comprehensive understanding of host factors modulated by the antiviral cytokine interferon-α (IFNα) is imperative for harnessing its beneficial effects while avoiding its detrimental side-effects during HIV infection. Cytokines modulate host glycosylation which plays a critical role in mediating immunological functions. However, the impact of IFNα on host glycosylation has never been characterized. METHODS: T and NK cell phenotypes, and HIV DNA. FINDINGS: T cell functions. Last, IFNα increases levels of fucose on NK cells. This induction is associated with higher NK functions upon K562 stimulation. INTERPRETATION: IFNα causes host glycomic alterations that are known to modulate immunological responses. These alterations are associated with both detrimental and beneficial consequences of IFNα. Manipulating host glycomic interactions may represent a strategy for enhancing the positive effects of IFNα while avoiding its detrimental side-effects. FUNDING: NIH grants R21AI143385, U01AI110434.