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Basic Characteristics of Mutations
|
|
Mutation Site
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T268A |
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Mutation Site Sentence
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T268A exhibited reduced fusion activity, as did T267A. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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gB |
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Standardized Encoding Gene
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UL27
|
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Genotype/Subtype
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- |
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Viral Reference
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-
|
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Functional Impact and Mechanisms
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|
Disease
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Cell line
|
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Immune
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- |
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Target Gene
|
-
|
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
|
- |
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Location
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- |
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Literature Information
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PMID
|
37919266
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Title
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Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection
|
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Author
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Bagdonaite I,Marinova IN,Rudjord-Levann AM,Pallesen EMH,King-Smith SL,Karlsson R,Romer TB,Chen YH,Miller RL,Olofsson S,Norden R,Bergstrom T,Dabelsteen S,Wandall HH
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Journal
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Nature communications
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Journal Info
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2023 Nov 2;14(1):7000
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Abstract
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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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Sequence Data
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-
|
|
|