ArticleNature communications2023
Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 6 citations in OpenAlex.
- Glycoprotein G enables HSV-2 neuroinvasion and provides protection as a glycosylated vaccine antigen.PLoS pathogens · 2026Article
- Distinct O-Linked Glycosylation Systems in Signaling and Immune Regulation.International journal of molecular sciences · 2026Review
- Multiplexed Detection of Autoantibodies to Glycopeptides Using Microarray.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Carbon Quantum Dots Assisted Virus Tracking: From Skin to Brain.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- A Bioorthogonal Precision Tool for HumanJournal of the American Chemical Society · 2024Article
- Targeting host O-linked glycan biosynthesis affects Ebola virus replication efficiency and reveals differential GalNAc-T acceptor site preferences on the Ebola virus glycoprotein.Journal of virology · 2024Article
- Non-Thermal Plasma Reduces HSV-1 Infection of and Replication in HaCaT Keratinocytes In Vitro.International journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viral and host glycans represent an understudied aspect of host-pathogen interactions, despite potential implications for treatment of viral infections. This is due to lack of easily accessible tools for analyzing glycan function in a meaningful context. Here we generate a glycoengineered keratinocyte library delineating human glycosylation pathways to uncover roles of specific glycans at different stages of herpes simplex virus type 1 (HSV-1) infectious cycle. We show the importance of cellular glycosaminoglycans and glycosphingolipids for HSV-1 attachment, N-glycans for entry and spread, and O-glycans for propagation. While altered virion surface structures have minimal effects on the early interactions with wild type cells, mutation of specific O-glycosylation sites affects glycoprotein surface expression and function. In conclusion, the data demonstrates the importance of specific glycans in a clinically relevant human model of HSV-1 infection and highlights the utility of genetic engineering to elucidate the roles of specific viral and cellular carbohydrate structures.
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