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. 2021 Feb 24:11:625430.
doi: 10.3389/fcimb.2021.625430. eCollection 2021.

Proteomic Analyses of Acinetobacter baumannii Clinical Isolates to Identify Drug Resistant Mechanism

Ping Wang  1 , Ren-Qing Li  2 , Lei Wang  3 , Wen-Tao Yang  3 , Qing-Hua Zou  1 , Di Xiao  3
Affiliations

Proteomic Analyses of Acinetobacter baumannii Clinical Isolates to Identify Drug Resistant Mechanism

Ping Wang et al. Front Cell Infect Microbiol. .

Abstract

Acinetobacter baumannii is one of the main causes of nosocomial infections. Increasing numbers of multidrug-resistant Acinetobacter baumannii cases have been reported in recent years, but its antibiotic resistance mechanism remains unclear. We studied 9 multidrug-resistant (MDR) and 10 drug-susceptible Acinetobacter baumannii clinical isolates using Label free, TMT labeling approach and glycoproteomics analysis to identify proteins related to drug resistance. Our results showed that 164 proteins exhibited different expressions between MDR and drug-susceptible isolates. These differential proteins can be classified into six groups: a. proteins related to antibiotic resistance, b. membrane proteins, membrane transporters and proteins related to membrane formation, c. Stress response-related proteins, d. proteins related to gene expression and protein translation, e. metabolism-related proteins, f. proteins with unknown function or other functions containing biofilm formation and virulence. In addition, we verified seven proteins at the transcription level in eight clinical isolates by using quantitative RT-PCR. Results showed that four of the selected proteins have positive correlations with the protein level. This study provided an insight into the mechanism of antibiotic resistance of multidrug-resistant Acinetobacter baumannii.

Keywords: Acinetobacter baumannii; TMT; antibiotic resistance; glycopeptides; label free; proteomic.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
The experiment process of this study.
Figure 2
Figure 2
GO enrichment analysis of DEPs in TMT-labeling proteomics. The MDR isolates and drug-susceptible isolates were labelled by 127 and 126 reagent. Up-regulated and down-regulated means 127/126 ≥ 2 and ≤0.5, respectively. Each column represented the number of proteins involved in GO annotation analysis of DEPs in TMT-labeling proteomics. Statistically significant differences of GO terms were defined by P < 0.05.
Figure 3
Figure 3
GO enrichment analysis of DEPs in label free proteomics. The proteins in label free proteomics are all present in more than 8 resistant isolates and only in 1 or less susceptible isolate. Each column represented the number of proteins involved in GO annotation analysis of DEPs in label free proteomics. Statistically significant differences of GO terms were defined by P < 0.05.
Figure 4
Figure 4
Heat map of the representative proteins of each isolate. “R” means drug-resistant isolates and “S” means drug-susceptible isolates. The representative proteins identified from label free proteomics are clustered if they exhibit a similar expression trend across the samples. The hierarchical clustering is generated using neighbor joining algorithm with a Euclidean distance similarity measurement of the log2 ratios of the abundance of each sample relative to the average abundance.
Figure 5
Figure 5
The subcellular localization of DEPs in TMT-labeling proteomics and label free proteomics.
Figure 6
Figure 6
qRT-PCR analysis of 7 representative proteins: The normalized expression level (2-ΔΔct) of 7 DEPs genes of the resistant isolates and susceptible isolates were tested by qRT-PCR. rpoB was used as the internal parameter. Error bars represent the SDs.
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References

    1. Ahmad Izaham A. R., Scott N. E. (2020). Open Database Searching Enables the Identification and Comparison of Bacterial Glycoproteomes without Defining Glycan Compositions Prior to Searching. Mol. Cell Proteomics 19 (9), 1561–1574. 10.1074/mcp.TIR120.002100 - DOI - PMC - PubMed
    1. Al-Kadmy I. M. S., Ibrahim S. A., Al-Saryi N., Aziz S. N., Besinis A., Hetta H. F. (2020). Prevalence of Genes Involved in Colistin Resistance in Acinetobacter baumannii: First Report from Iraq. Microb. Drug Resist. 26 (6), 616–622. 10.1089/mdr.2019.0243 - DOI - PubMed
    1. Bell E. W., Zheng E. J., Ryno L. M. (2018). Identification of inhibitors of the E. coli chaperone SurA using in silico and in vitro techniques. Bioorg. Med. Chem. Lett. 28 (22), 3540–3548. 10.1016/j.bmcl.2018.09.034 - DOI - PubMed
    1. Bezsudnova E. Y., Boyko K. M., Popov V. O. (2017). Properties of Bacterial and Archaeal Branched-Chain Amino Acid Aminotransferases. Biochemistry (Mosc) 82 (13), 1572–1591. 10.1134/s0006297917130028 - DOI - PubMed
    1. Bhakdi S., Mackman N., Menestrina G., Gray L., Hugo F., Seeger W., et al. . (1988). The hemolysin of Escherichia coli. Eur. J. Epidemiol. 4 (2), 135–143. 10.1007/bf00144740 - DOI - PubMed

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