Author

J. Petrlova

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· 2 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:host-pathogen & immune response· 4 Organism:human· 4 Assay:proteomics· 4 Approach:experimental assay· 3 Approach:biophysical modeling· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Schmidtchen· 4 shared G. Petruk· 3 shared M. Puthia· 3 shared P. J. Bond· 2 shared A.-C. Strömdahl· 1 shared D. A. Holdbrook· 1 shared E. Hartman· 1 shared F. Samsudin· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersImmunology

A. Schmidtchen

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Author profile →

4 papers

Recent·Most cited

Protein aggregation in wound fluid confines bacterial lipopolysaccharide and reduces inflammation

J. Petrlova, E. Hartman, G. Petruk, J. C. H. Lim, S. S. Adav, S. Kjellstrom, M. Puthia, A. Schmidtchen

The paper shows that LPS-induced protein aggregates in wound fluid reduce inflammation by confining LPS, using mass spectrometry, imaging, and animal models.

bioRxiv · Jan 27, 2023 · PreprintImmunology

SARS-CoV-2 spike protein as a bacterial lipopolysaccharide delivery system in an overzealous inflammatory cascade

F. Samsudin, P. Raghuvamsi, G. Petruk, M. Puthia, J. Petrlova, P. MacAry, G. S. Anand, A. Schmidtchen, P. J. Bond

This study shows SARS-CoV-2 spike protein binds LPS, which may enhance immune activation via TLR4, with conserved binding sites across variants.

bioRxiv · Oct 29, 2021Microbiology

SARS-CoV-2 Spike protein binds to bacterial lipopolysaccharide and boosts proinflammatory activity

G. Petruk, M. Puthia, J. Petrlova, A.-C. Strömdahl, S. Kjellström, A. Schmidtchen

This study shows that SARS-CoV-2 Spike protein binds to bacterial lipopolysaccharide, enhancing proinflammatory responses in vitro and in vivo.

bioRxiv · Jun 29, 2020Immunology

Structural basis for endotoxin neutralization and anti-inflammatory activity of thrombin-derived C-terminal peptides

R. Saravanan, D. A. Holdbrook, J. Petrlova, S. Singh, N. A. Berglund, Y. K. Choong, P. J. Bond, M. Malmsten, A. Schmidtchen

This paper identifies the structural basis of thrombin-derived C-terminal peptides' ability to neutralize endotoxin and reduce inflammation by interacting with LPS and CD14.

bioRxiv · Dec 12, 2017Biophysics