J
Jonathan Sjögren
Researcher at Lund University
Publications - 23
Citations - 667
Jonathan Sjögren is an academic researcher from Lund University. The author has contributed to research in topics: Glycosylation & Glycan. The author has an hindex of 12, co-authored 22 publications receiving 488 citations. Previous affiliations of Jonathan Sjögren include University of California, San Diego.
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Journal ArticleDOI
EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and α1-acid glycoprotein.
Jonathan Sjögren,Weston B. Struwe,Eoin Cosgrave,Pauline M. Rudd,Martin Stervander,Maria Allhorn,Andrew Hollands,Andrew Hollands,Victor Nizet,Victor Nizet,Victor Nizet,Mattias Collin +11 more
TL;DR: It is concluded that EndoS2 is a unique endoglycosidase in serotype M49 of GAS and differs from EndoS of other GAS strains by targeting both IgG and AGP.
Journal ArticleDOI
Rapid and improved characterization of therapeutic antibodies and antibody related products using IdeS digestion and subunit analysis
TL;DR: A wide range of IdeS-based applications are presented for improved characterization of originator, biosimilar and next generation antibody-based therapeutics, focused on critical quality attributes of the final antibody product as studied by IdeS fragmentation.
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A novel mechanism for NETosis provides antimicrobial defense at the oral mucosa.
Tirthankar Mohanty,Jonathan Sjögren,Fredrik Kahn,Anas H. A. Abu-Humaidan,Niels Fisker,Kristian Assing,Matthias Mörgelin,Anders A. Bengtsson,Niels Borregaard,Ole E. Sørensen +9 more
TL;DR: Saliva from patients with aphthous ulcers and Behçet disease prone to oral ulcers failed to induce NETosis, but for different reasons it demonstrated that disordered homeostasis in the oral cavity may result in deficient saliva-mediated NETosis.
Journal ArticleDOI
Deciphering Protein O-Glycosylation: Solid-Phase Chemoenzymatic Cleavage and Enrichment.
Shuang Yang,Philip Onigman,Wells W. Wu,Jonathan Sjögren,Helén Nyhlén,Rong-Fong Shen,John F. Cipollo +6 more
TL;DR: A novel chemoenzymatic approach driven by a newly available O-protease and solid phase platform that enables the assignment of O-glycosylated peptides, N-glycan profile, sialyl O- glycopeptides linkage, and mapping of heterogeneous O- Glycosylation and should become an indispensable tool for investigations where O-behavioural modification is central.
Journal ArticleDOI
EndoS and EndoS2 hydrolyze Fc-glycans on therapeutic antibodies with different glycoform selectivity and can be used for rapid quantification of high-mannose glycans.
Jonathan Sjögren,Eoin Cosgrave,Maria Allhorn,Maria Nordgren,Stephan Björk,Fredrik Olsson,Sarah Fredriksson,Mattias Collin +7 more
TL;DR: It is concluded that EndoS and EndoS2 hydrolyze different glycoforms from the Fc-glycosylation site on therapeutic mAbs and that this can be used for rapid quantification of high mannose content.