Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection
Identification of host antiviral restriction factors could provide targets for antiviral therapy. Here, using a genome-wide CRISPR screen, the authors identify the glycosyltransferase B3GAT1 as a host protein which, when ectopically overexpressed, restricts influenza virus infection in vitro and in...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-34111-0 |
| _version_ | 1797991615971721216 |
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| author | Joseph D. Trimarco Sarah L. Nelson Ryan R. Chaparian Alexandra I. Wells Nathan B. Murray Parastoo Azadi Carolyn B. Coyne Nicholas S. Heaton |
| author_facet | Joseph D. Trimarco Sarah L. Nelson Ryan R. Chaparian Alexandra I. Wells Nathan B. Murray Parastoo Azadi Carolyn B. Coyne Nicholas S. Heaton |
| author_sort | Joseph D. Trimarco |
| collection | DOAJ |
| description | Identification of host antiviral restriction factors could provide targets for antiviral therapy. Here, using a genome-wide CRISPR screen, the authors identify the glycosyltransferase B3GAT1 as a host protein which, when ectopically overexpressed, restricts influenza virus infection in vitro and in mice, as well as other viruses relying on sialic acid for entry. |
| first_indexed | 2024-04-11T08:55:02Z |
| format | Article |
| id | doaj.art-421acf3c2de24f58bda9a6d24454f5bd |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-11T08:55:02Z |
| publishDate | 2022-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-421acf3c2de24f58bda9a6d24454f5bd2022-12-22T04:33:20ZengNature PortfolioNature Communications2041-17232022-10-0113111510.1038/s41467-022-34111-0Cellular glycan modification by B3GAT1 broadly restricts influenza virus infectionJoseph D. Trimarco0Sarah L. Nelson1Ryan R. Chaparian2Alexandra I. Wells3Nathan B. Murray4Parastoo Azadi5Carolyn B. Coyne6Nicholas S. Heaton7Department of Molecular Genetics and Microbiology, Duke University School of MedicineDepartment of Molecular Genetics and Microbiology, Duke University School of MedicineDepartment of Molecular Genetics and Microbiology, Duke University School of MedicineDepartment of Pediatrics, Division of Infectious Diseases, UPMC Children’s Hospital of PittsburghComplex Carbohydrate Research Center, The University of GeorgiaComplex Carbohydrate Research Center, The University of GeorgiaDepartment of Molecular Genetics and Microbiology, Duke University School of MedicineDepartment of Molecular Genetics and Microbiology, Duke University School of MedicineIdentification of host antiviral restriction factors could provide targets for antiviral therapy. Here, using a genome-wide CRISPR screen, the authors identify the glycosyltransferase B3GAT1 as a host protein which, when ectopically overexpressed, restricts influenza virus infection in vitro and in mice, as well as other viruses relying on sialic acid for entry.https://doi.org/10.1038/s41467-022-34111-0 |
| spellingShingle | Joseph D. Trimarco Sarah L. Nelson Ryan R. Chaparian Alexandra I. Wells Nathan B. Murray Parastoo Azadi Carolyn B. Coyne Nicholas S. Heaton Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection Nature Communications |
| title | Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection |
| title_full | Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection |
| title_fullStr | Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection |
| title_full_unstemmed | Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection |
| title_short | Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection |
| title_sort | cellular glycan modification by b3gat1 broadly restricts influenza virus infection |
| url | https://doi.org/10.1038/s41467-022-34111-0 |
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