International Journal of Molecular Sciences

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Bacterial and Viral Pathogenesis: Insights from Proteomics

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Dear Colleagues,

Mass spectrometry (MS)-based proteomics, a cutting-edge molecular technique, has emerged as a promising biotechnological tool in the post-genomic era, particularly in systems biology. Comparative quantitative proteomic platforms not only offer the global expression pattern of thousands of proteins but also unveil the post-translational modifications and potential pathways regulated in the cell under certain conditions. Therefore, the utility of proteomic platforms, including but not limited to discovery proteomics, analysis of post-translationally modified protein/peptides, immuno-proteomics, and mass-spectrometry-based targeted methods have been employed to provide insight into the molecular drivers of bacterial and viral infections in host cells and pathogenesis in plant, animals, etc. Results from these studies have been instrumental in advancing knowledge about pathogen–host interaction, resistance mechanisms, and evolutionary trends and in many instances have revealed promising novel drug targets and novel therapeutical venues.

This Special Issue on “Bacterial and Viral Pathogenesis: Insights from Proteomics" will focus on all aspects of proteomics and infectious disease. We welcome you to submit your original research paper, recent reviews, and commentaries on this topic.

Dr. Nagib Ahsan
Dr. Adam Duerfeldt
Dr. Luciana Jesus Costa
Guest Editors

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Keywords

proteomics
bacterial diseases
viral diseases
plants
animals

Published Papers (2 papers)

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Research

13 pages, 2064 KiB

Open AccessArticle

Proteomic Profiling Skin Mucus of European Eel Anguilla anguilla Infected with Anguillid Herpesvirus

by Ying-Ying Li, Jin-Xian Yang, Xi Chen, Qiang Chen, Tie-Ying Song and Jun-Qing Ge

Int. J. Mol. Sci. 2022, 23(19), 11283; https://doi.org/10.3390/ijms231911283 - 24 Sep 2022

Cited by 3 | Viewed by 1599

Abstract

Anguillid herpesvirus 1 (AngHV) is an important viral pathogen affecting eel. This study was designed to investigate the potential molecular mechanisms and immune response elicited at the protein levels in the skin mucus of AngHV-infected Anguilla anguilla. Tandem mass tag (TMT)-labelling proteomics with the liquid chromatography tandem mass spectrometry (LC-MS/MS) was used for performing quantitative identification of the proteins. In addition, the quantitative protein amount was detected by parallel reaction monitoring (PRM) analysis. A total of 3486 proteins were identified, of which 2935 were quantified. When a protein fold change was greater than 1.3 or less than 0.76, it indicated a differentially expressed protein (DEP). Overall, 187 up-regulated proteins and 126 down-regulated proteins were detected, and most of the DEPs were enriched in the CAMs pathway, intestinal immune pathway, herpes simplex virus 1 infection pathway, phagosome pathway and p53 signaling pathway. The results of the DEPs detected by PRM were highly consistent with the results of the TMT-labelled quantitative proteomic analysis. The findings of this study provide an important research basis for further understanding the pathogenesis of AngHV. Full article

(This article belongs to the Special Issue Bacterial and Viral Pathogenesis: Insights from Proteomics)

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18 pages, 4896 KiB

Open AccessArticle

YdfD, a Lysis Protein of the Qin Prophage, Is a Specific Inhibitor of the IspG-Catalyzed Step in the MEP Pathway of Escherichia coli

by Zhifang Lu, Biying Wang, Zhiyu Qiu, Ruiling Zhang, Jimin Zheng and Zongchao Jia

Int. J. Mol. Sci. 2022, 23(3), 1560; https://doi.org/10.3390/ijms23031560 - 29 Jan 2022

Viewed by 2125

Abstract

Bacterial cryptic prophage (defective prophage) genes are known to drastically influence host physiology, such as causing cell growth arrest or lysis, upon expression. Many phages encode lytic proteins to destroy the cell envelope. As natural antibiotics, only a few lysis target proteins were identified. ydfD is a lytic gene from the Qin cryptic prophage that encodes a 63-amino-acid protein, the ectopic expression of which in Escherichia coli can cause nearly complete cell lysis rapidly. The bacterial 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway is responsible for synthesizing the isoprenoids uniquely required for sustaining bacterial growth. In this study, we provide evidence that YdfD can interact with IspG, a key enzyme involved in the MEP pathway, both in vivo and in vitro. We show that intact YdfD is required for the interaction with IspG to perform its lysis function and that the mRNA levels of ydfD increase significantly under certain stress conditions. Crucially, the cell lysis induced by YdfD can be abolished by the overexpression of ispG or the complementation of the IspG enzyme catalysis product methylerythritol 2,4-cyclodiphosphate. We propose that YdfD from the Qin cryptic prophage inhibits IspG to block the MEP pathway, leading to a compromised cell membrane and cell wall biosynthesis and eventual cell lysis. Full article

(This article belongs to the Special Issue Bacterial and Viral Pathogenesis: Insights from Proteomics)

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