Author

C. F. Lesser

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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Microbiology· 3 Immunology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 5 Research Focus:cell signaling & trafficking· 2 Organism:mouse· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:development & morphogenesis· 1 Organism:human· 1

Frequent Co-Authors

L. Goers· 3 shared R. E. Vance· 3 shared A. Y. Lee· 2 shared E. A. Turcotte· 2 shared J. L. Roncaioli· 2 shared P. S. Mitchell· 2 shared R. A. Chavez· 2 shared A. Sandstrom· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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3 shared papersMicrobiology

L. Goers

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

A hierarchy of cell death pathways confers layered resistance to shigellosis in mice

J. L. Roncaioli, J. P. Babirye, R. A. Chavez, F. L. Liu, E. A. Turcotte, A. Y. Lee, C. F. Lesser, R. E. Vance

The paper shows that multiple cell death pathways work together to protect mice from Shigella infection, with some pathways compensating for others when one is removed.

eLife · Jan 16, 2023Peer-reviewedImmunology

Shigella IpaH9.8 limits GBP1-dependent LPS release from intracytosolic bacteria to suppress caspase-4 activation

L. Goers, K. Kim, P. J. Canning, T. C. Stedman, X. Mou, N. Heinz Ernst, J. Coers, c. F. lesser

This study shows that Shigella IpaH9.8 inhibits GBP1-dependent LPS release from intracellular bacteria, preventing caspase-4 activation and pyroptosis.

bioRxiv · Nov 14, 2022 · PreprintMicrobiology

The Shigella type III effector protein OspB is a cysteine protease

T. E. Wood, K. A. Westervelt, J. M. Yoon, H. D. Eshleman, H. Burnes, R. Levy, D. J. Slade, C. F. Lesser, M. B. Goldberg

This paper identifies OspB as a cysteine protease in Shigella spp. and shows it interacts with the TORC1 pathway in yeast through proteolytic cleavage of Tco89p.

bioRxiv · Sep 1, 2021 · PreprintMicrobiology

NAIP-NLRC4-deficient mice are susceptible to shigellosis

P. S. Mitchell, J. L. Roncaioli, E. A. Turcotte, L. Goers, R. A. Chavez, A. Y. Lee, C. F. Lesser, I. Rauch, R. E. Vance

This study shows that NAIP-NLRC4-deficient mice are susceptible to Shigella infection, mimicking human shigellosis, and reveals that inflammasome-mediated cell death protects against the disease.

bioRxiv · May 16, 2020Microbiology

Functional degradation: a mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes

A. Sandstrom, P. S. Mitchell, L. Goers, E. W. Mu, C. F. Lesser, R. E. Vance

The paper identifies proteasome-mediated degradation of NLRP1B as a mechanism by which two distinct pathogen enzymes activate the inflammasome.

bioRxiv · Nov 6, 2018Immunology