Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection
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Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection. / Bagdonaite, Ieva; Marinova, Irina N.; Rudjord-Levann, Asha M.; Pallesen, Emil M. H.; King-Smith, Sarah L.; Karlsson, Richard; Rømer, Troels B.; Chen, Yen-Hsi; Miller, Rebecca L.; Olofsson, Sigvard; Nordén, Rickard; Bergström, Tomas; Dabelsteen, Sally; Wandall, Hans H.
In: Nature Communications, Vol. 14, 7000, 2023.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection
AU - Bagdonaite, Ieva
AU - Marinova, Irina N.
AU - Rudjord-Levann, Asha M.
AU - Pallesen, Emil M. H.
AU - King-Smith, Sarah L.
AU - Karlsson, Richard
AU - Rømer, Troels B.
AU - Chen, Yen-Hsi
AU - Miller, Rebecca L.
AU - Olofsson, Sigvard
AU - Nordén, Rickard
AU - Bergström, Tomas
AU - Dabelsteen, Sally
AU - Wandall, Hans H.
N1 - Publisher Copyright: © 2023, The Author(s).
PY - 2023
Y1 - 2023
N2 - 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.
AB - 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.
U2 - 10.1038/s41467-023-42669-6
DO - 10.1038/s41467-023-42669-6
M3 - Journal article
C2 - 37919266
AN - SCOPUS:85175847515
VL - 14
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 7000
ER -
ID: 372964535