Author

E. Bratanis

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Immunology· 2 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Assay:proteomics· 3 Organism:human· 2 Organism:mouse· 1

Frequent Co-Authors

O. Shannon· 3 shared D. Tang· 2 shared H. Khakzad· 2 shared J. Malmström· 2 shared L. Happonen· 2 shared P. Nordenfelt· 2 shared S. Wrighton· 2 shared W. Bahnan· 2 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersImmunology

O. Shannon

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The increased hinge flexibility of an IgG1-IgG3 hybrid monoclonal enhances Fc-mediated protection against group A streptococci

A. Izadi, Y. Karami, E. Bratanis, S. Wrighton, H. Khakzad, M. Nyblom, B. Olofsson, L. Happonen, D. Tang, M. Nilges, J. Malmström, W. Bahnan, O. Shannon, L. Malmström, P. Nordenfelt

This study shows that increasing Fc flexibility in an IgG1-IgG3 hybrid monoclonal antibody enhances opsonic function and protection against group A streptococci.

bioRxiv · Oct 14, 2023 · PreprintImmunology

A human monoclonal antibody bivalently binding two different epitopes in streptococcal M protein protects against infection

W. Bahnan, L. Happonen, H. Khakzad, V. Kumra Ahnlide, T. de Neergaard, S. Wrighton, O. Andre, E. Bratanis, D. Tang, T. Hellmark, L. Bjorck, O. Shannon, L. Malmstrom, J. Malmstrom, P. Nordenfelt

The paper describes a human monoclonal antibody that binds two distinct epitopes on streptococcal M protein via a bivalent dual-Fab cis mode, providing protection against infection.

bioRxiv · Mar 1, 2021 · PreprintImmunology

Sweet revenge - Streptococcus pyogenes showcases first example of immune evasion through specific IgG glycan hydrolysis

A. Naegeli, E. Bratanis, C. Karlsson, O. Shannon, R. Kalluru, A. Linder, J. Malmström, M. Collin

This study identifies EndoS as a mechanism by which Streptococcus pyogenes evades the immune system by hydrolyzing IgG glycans, impairing antibody effector functions during infection.

bioRxiv · Mar 7, 2019Microbiology