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Updated: May 16, 2026

Super-Resolution Imaging of Bacterial Secreted Proteins Using Genetic Code Expansion
Published on: February 10, 2023
Structure of the catalytic domain of the Salmonella virulence factor SseI
Shyam S Bhaskaran1, C Erec Stebbins
1Laboratory of Structural Microbiology, The Rockefeller University, New York, NY 10065, USA.
Abstract:
SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 Å resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting of Cys178, His216 and Asp231 that is critical to its virulence activities. Structure-based analysis revealed that SseI is likely to possess either acyl hydrolase or acyltransferase activity, placing this virulence factor in the rapidly growing class of enzymes of this family utilized by bacterial pathogens inside eukaryotic cells.
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