Volume 59, Issue 6 pp. 2235-2240
Communication

Tracking Pathogen Infections by Time-Resolved Chemical Proteomics

Prof. Dr. Ying Zhang

Corresponding Author

Prof. Dr. Ying Zhang

Department of Biochemistry, Department of Chemistry, Center for Cancer Research, Purdue University, West Lafayette, IN, 47907 USA

Minghang Hospital and Institutes of Biomedical Sciences, Fudan University, 131 Dong'an Road, Shanghai, 200032 China

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Der-Shyang Kao

Der-Shyang Kao

Department of Biochemistry, Department of Chemistry, Center for Cancer Research, Purdue University, West Lafayette, IN, 47907 USA

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Dr. Bing Gu

Dr. Bing Gu

Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907 USA

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Dr. Rajdeep Bomjan

Dr. Rajdeep Bomjan

Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907 USA

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Dr. Mayank Srivastava

Dr. Mayank Srivastava

Department of Biochemistry, Department of Chemistry, Center for Cancer Research, Purdue University, West Lafayette, IN, 47907 USA

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Prof. Dr. Haojie Lu

Prof. Dr. Haojie Lu

Minghang Hospital and Institutes of Biomedical Sciences, Fudan University, 131 Dong'an Road, Shanghai, 200032 China

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Prof. Dr. Daoguo Zhou

Prof. Dr. Daoguo Zhou

Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907 USA

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Prof. Dr. W. Andy Tao

Corresponding Author

Prof. Dr. W. Andy Tao

Department of Biochemistry, Department of Chemistry, Center for Cancer Research, Purdue University, West Lafayette, IN, 47907 USA

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First published: 26 November 2019
Citations: 5

Graphical Abstract

A tip of the hap: A time-resolved chemical proteomics strategy enables host and pathogen temporal interaction profiling (HAPTIP) for tracking the entry of bacteria into host cell.

Abstract

Studying the dynamic interaction between host cells and pathogen is vital but remains technically challenging. We describe herein a time-resolved chemical proteomics strategy enabling host and pathogen temporal interaction profiling (HAPTIP) for tracking the entry of a pathogen into the host cell. A novel multifunctional chemical proteomics probe was introduced to label living bacteria followed by in vivo crosslinking of bacteria proteins to their interacting host-cell proteins at different time points initiated by UV for label-free quantitative proteomics analysis. We observed over 400 specific interacting proteins crosslinked with the probe during the formation of Salmonella-containing vacuole (SCV). This novel chemical proteomics approach provides a temporal interaction profile of host and pathogen in high throughput and would facilitate better understanding of the infection process at the molecular level.

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