Author

Jan‐Åke Liljeqvist

Sahlgrenska University HospitalORCID 0000-0002-1226-9870Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Microbiology· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:proteomics· 2 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Organism:mouse· 1 Research Focus:protein structure prediction· 1 Research Focus:variant calling· 1 Approach:wet-lab / biochemical assay· 1

Frequent Co-Authors

Ebba SamuelssoniD· 2 shared Rickard NordéniD· 2 shared Beata Adamiak· 1 shared Carolina Gustafsson· 1 shared Edward TrybalaiD· 1 shared Ekaterina E. MirgorodskayaiD· 1 shared Ekaterina MirgorodskayaiD· 1 shared Eva JennischeiD· 1 shared

Activity by Year

2022-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersMicrobiology

Ebba SamuelssonORCID

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2 papers

Recent·Most cited

MicrobiologyPLoS PathogensPeer-reviewedJul 9, 2026

Glycoprotein G enables HSV-2 neuroinvasion and provides protection as a glycosylated vaccine antigen

Ebba Samuelsson, Carolina Gustafsson, Lindvi Gudmundsdotter…·Rickard Nordén

This study shows that HSV-2 glycoprotein G (mgG-2) is critical for neuroinvasion and that its glycosylation is essential for vaccine efficacy against HSV-2.

DOI 10.1371/journal.ppat.1014339

mouseproteomics

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Molecular BiologybioRxivPreprintJan 20, 2022

Sialic acid and fucose residues on the SARS-CoV-2 receptor binding domain modulate IgG reactivity

Ebba Samuelsson, Ekaterina E. Mirgorodskaya, Kristina Nyström…·Rickard Nordén

The paper examines how carbohydrate modifications on the SARS-CoV-2 RBD affect IgG reactivity, finding that reduced sialylation and fucosylation enhance antibody binding.

DOI 10.1101/2022.01.20.477056

humanproteomics

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