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Dissecting Innate Immune Signaling in Viral Evasion of Cytokine Production
Published on: March 2, 2014
Blocking cellular N-glycosylation suppresses human cytomegalovirus entry in human fibroblasts
Luping Zheng1, Huifen Li2, Li Fu3
1Department of Biochemistry and Molecular Biology, Dalian Medical University, Liaoning Provincial Core Laboratory of Glycobiology and Glycoengineering, Dalian, Liaoning Province, China.
Abstract:
N-glycosylation plays an important role in the pathogenesis of viral infections. However, the role of host cell N-glycosylation in human cytomegalovirus (hCMV) infection remains to be elucidated. In this study, we found that blocking or removal of cellular N-glycosylation by tunicamycin, peptide-N-glycosidase F (PNGase F) treatment, or N-acetylglucosaminyltransferase I (MGAT1) knockdown resulted in suppression of hCMV infection in human fibroblasts. This suppression was reversed following N-glycosylation restoration. Immunofluorescence and flow cytometry analysis showed that blockade of cellular N-glycosylation interfered with hCMV entry rather than binding. Removal of N-glycosylation on epidermal growth factor (EGFR) and integrin β3, two proposed hCMV receptors, blocked their interaction with hCMV glycoproteins B and H. It also suppressed activation of these receptors and downstream integrin β3/Src signaling. Taken together, these results suggest that N-glycosylation of host cell glycoproteins including two proposed hCMV receptors is critical for hCMV entry rather than attachment. They provide novel insights into the biological process important for the early stage of hCMV infection with potential therapeutic implications.
Insights
Host cell N-glycosylation is crucial for human cytomegalovirus (hCMV) infection. Blocking N-glycosylation inhibits hCMV entry by affecting viral receptor interactions and signaling pathways.
Area of Science:
- Virology
- Glycobiology
- Cell Biology
Background:
- N-glycosylation is vital in viral pathogenesis.
- The specific role of host cell N-glycosylation in human cytomegalovirus (hCMV) infection requires further investigation.
Purpose of the Study:
- To elucidate the role of host cell N-glycosylation in hCMV infection.
- To determine how N-glycosylation affects hCMV entry and attachment.
Main Methods:
- Utilized tunicamycin, PNGase F, and MGAT1 knockdown to block or remove N-glycosylation.
- Employed immunofluorescence and flow cytometry to analyze hCMV infection.
- Investigated the interaction between hCMV glycoproteins and host cell receptors (EGFR, integrin β3).
Main Results:
- Blocking or removing N-glycosylation suppressed hCMV infection in human fibroblasts.
- N-glycosylation blockade inhibited hCMV entry, not attachment.
- N-glycosylation removal from EGFR and integrin β3 disrupted their interaction with hCMV glycoproteins B and H.
- Receptor activation and downstream signaling (integrin β3/Src) were suppressed.
Conclusions:
- Host cell N-glycosylation, particularly on EGFR and integrin β3, is critical for hCMV entry.
- N-glycosylation is essential for early-stage hCMV infection, offering potential therapeutic targets.
