Author

L. Happonen

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

Biology Disciplines

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Immunology· 3 Biochemistry· 2 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:host-pathogen & immune response· 6 Assay:proteomics· 6 Organism:human· 4 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Organism:mouse· 1

Frequent Co-Authors

H. Khakzad· 4 shared J. Malmström· 4 shared L. Malmström· 4 shared D. Tang· 3 shared P. Nordenfelt· 3 shared S. Wrighton· 3 shared W. Bahnan· 3 shared E. Bratanis· 2 shared

Activity by Year

2021-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersImmunology

H. Khakzad

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Multi-Modal Mass Spectrometry Identifies a Conserved Protective Epitope in S. pyogenes Streptolysin O

D. Tang, C. A. Gueto-Tettay, E. Hjortswang, J. Ströbaek, S. Ekström, L. Happonen, L. Malmström, J. Malmström

This study uses multi-modal mass spectrometry to identify a conserved protective epitope in Streptolysin O from S. pyogenes, which could inform vaccine and therapeutic development.

bioRxiv · Dec 2, 2023 · PreprintBiochemistry

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

Molecular view of ER membrane remodeling by the Sec61/TRAP translocon

S. Karki, M. Javanainen, D. Tranter, S. Rehan, J. T. Huiskonen, L. Happonen, V. Paavilainen

The paper determines the structure of the Sec61/TRAP complex bound to a ribosome using Cryo-EM, revealing how TRAP facilitates ER membrane remodeling and polypeptide translocation.

bioRxiv · Sep 30, 2022Biochemistry

Proteome-wide cross-linking mass spectrometry to identify specific virus capsid-host interactions between tick-borne encephalitis virus and neuroblastoma cells

S. V. Barrass, L. I. A. Pulkkinen, O. Vapalahti, S. Kuivanen, M. Anastasina, L. Happonen, S. J. Butcher

This paper identifies 59 high confidence virus-host protein interactions between tick-borne encephalitis virus and neuroblastoma cells using chemical cross-linking and mass spectrometry.

bioRxiv · Oct 29, 2021 · PreprintMicrobiology

Opsonization by non-neutralizing antibodies can confer protection to SARS-CoV-2 despite Spike-dependent modulation of phagocytosis

W. Bahnan, S. Wrighton, M. Sundwall, A. Bläckberg, O. Larsson, U. Höglund, H. Khakzad, M. Godzwon, M. Walle, E. Elder, L. Happonen, O. Andre, J. Kumra Ahnlide, T. Hellmark, V. Wendel-Hansen, , P. Nordenfelt

This study shows that non-neutralizing Spike-specific antibodies can enhance phagocytosis of SARS-CoV-2 by monocytes, potentially offering protection despite not neutralizing the virus.

bioRxiv · Oct 14, 2021Immunology

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

Streptococcus pyogenes forms serotype and local environment-dependent inter-species protein complexes

S. Chowdhury, H. Khakzad, G. E. Bergdahl, R. Lood, S. Ekstrom, D. Linke, L. Malmström, L. Happonen, j. Malmström

This study identifies serotype- and microenvironment-dependent protein interactions between Streptococcus pyogenes and host proteins using mass spectrometry and modeling.

bioRxiv · Feb 9, 2021Microbiology