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Quantitative proteomics reveals the crucial roles of Cathepsin D in bacterial infections

ABSTRACT: Bacterial resistance has become more and more widespread which seriously threatens human life and health. Therefore, using the natural immune system of host to kill bacteria is particularly fascinating. Here, using mass spectrometry analyses, we depicted the dynamic expression landscape of mitochondria and lysosomes proteins upon five kinds of bacteria (L. monocytogenes, Staphylococcus aureus, Bacillus subtilis, Escherichia coli, Pseudomonas aeruginosa) infection in Macrophages cells. We showed that the protein expression level of Cathepsin D (CTSD) is up-regualated after bacterial infection. The knockout of CTSD indicated that, as a broad-spectrum antibacterial protein in the host, played an indispensable role in killing bacteria. Our study shows that CTSD can serve as a potential molecular drug target for antibacterial treatment.

ORGANISM(S): Mus Musculus

SUBMITTER: Xuefeng Xia

PROVIDER: PXD016938 | iProX | Wed May 13 00:00:00 BST 2020

REPOSITORIES: iProX

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Proteomic analysis of murine macrophages mitochondria and lysosomes reveal Cathepsin D as a potential broad-spectrum antimicrobial protein.

Fu Qihuan Q Yuan Jiangbei J Wang Liting L Ran Haiying H Li Fei F Liu Fang F Zhang Junying J Liu Wenhu W Huang Wei W Huang Yi Y Xia Xuefeng X

Journal of proteomics 20200514

Bacterial resistance to antibiotics has become increasingly widespread, posing a serious threat to human life and health. Macrophages in the host's natural immune system can directly destroy most of bacteria. Therefore, exploring the function of macrophages' mitochondria and lysosomes in killing bacteria might help us overcome the problem of bacterial resistance. We used mass spectrometry to analyze the dynamic expression landscape of mitochondrial and lysosomal proteins in macrophages upon infe ...[more]

PMID: 32417293

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