Dataset Information

Quantitative proteomic screen identifies Annexin A2 as a host target for Salmonella pathogenicity island-2 effectors SopD2 and PipB2

ABSTRACT: In this work we use stable isotope labeling of amino acids in cell culture (SILAC) and a S. Typhimurium mutant that secretes increased amounts of effectors to identify cognate effector binding partners during infection. Using this method, we identified the host protein annexin A2 as a binding partner for both SopD2 and PipB2 and were able to confirm its binding to SopD2 by reciprocal pull down. This indicates that SopD2 and PipB2 likely both interact with annexin A2 through protein-protein interactions to establish the S. Typhimurium intracellular replicativeniche. This demonstrates the value of studying effector interactions using proteomic techniques and natural effector delivery during infection rather than transfection.

INSTRUMENT(S): Bruker Daltonics instrument model

ORGANISM(S): Homo Sapiens (human) Salmonella Enterica Subsp. Enterica Serovar Typhimurium Str. 5579 Salmonella Enterica Subsp. Enterica Serovar Typhimurium Str. A130

SUBMITTER: Jenny Moon

LAB HEAD: Leonard J. Foster

PROVIDER: PXD025582 | Pride | 2022-02-17

REPOSITORIES: Pride

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Publications

Quantitative proteomic screen identifies annexin A2 as a host target for Salmonella pathogenicity island-2 effectors SopD2 and PipB2.

Knuff-Janzen Katelyn K Serapio-Palacios Antonio A McCoy James J Krekhno Zakhar Z Moon Kyung-Mee KM Deng Wanyin W Foster Leonard J LJ Finlay B Brett BB

Scientific reports 20211208 1

Intracellular pathogens need to establish an intracellular replicative niche to promote survival and replication within the hostile environment inside the host cell. Salmonella enterica serovar Typhimurium (S. Typhimurium) initiates formation of the unique Salmonella-containing vacuole and an extensive network of Salmonella-induced tubules in order to survive and thrive within host cells. At least six effectors secreted by the type III secretion system encoded within Salmonella pathogenicity isl ...[more]

PMID: 34880286

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Project description:To combat virus infections, which are major human killers, a deeper understanding of how viruses reprogram their hosts to create optimal production of progeny is needed. Most knowledge on the regulation of cellular gene expression during adenovirus infection is derived from studies of mRNA expression. Here, we investigated the changes in cellular protein expression during the late phase of adenovirus type 2 (Ad2) infection of primary human cells by stable isotope labeling in cell culture (SILAC) with subsequent liquid chromatography-high resolution tandem mass spectrometric (LC-MS/MS) analysis using a Q-Exactive Orbitrap instrument. Cells were in-depth evaluated 24 and 36 hours post infection (hpi) and two biological replicates were investigated using swapped labeling. In total, 2648 and 2394 proteins were quantified at 24 and 36 hpi, respectively. Among them, 659 and 645 were deregulated more than 1.6-fold at the two time points, and approximately 80% of them had sustained regulation from 24 to 36 hpi. For the deregulated genes the change in protein expression was compared with that of RNA expression using cDNA sequencing data from the same time points of infection. The comparison revealed a surprisingly low correlation (r = 0.3). Consistency between changes in RNA and protein expression was observed for approximately 30% of the genes, whereas a majority showed either divergent or opposite expression profiles. The deregulated proteins were subjected to pathway and biological function analysis using bioinformatics tools. A surprising observation was that proteins related to carbohydrate metabolism were up-regulated at the protein level but unchanged at the RNA level whereas histone proteins were down-regulated at the protein level but up-regulated at the RNA level. Our results show that regulation of cellular gene expression in the response to viral infection is more complex than hitherto believed and several examples of posttranscriptional regulation of gene expression were observed. The results contribute to our understanding of host cell gene regulation during infection at a deeper level.

Dataset Information

Quantitative proteomic screen identifies Annexin A2 as a host target for Salmonella pathogenicity island-2 effectors SopD2 and PipB2

Publications

Quantitative proteomic screen identifies annexin A2 as a host target for Salmonella pathogenicity island-2 effectors SopD2 and PipB2.

Similar Datasets

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