Short Communication, J Virol Antivir Res Vol: 12 Issue: 1
Novel Viral Proteomics Techniques and Discoveries
Olivin Roosar*
Department of Medicine, University of Cambridge, Hills Road, Cambridge, United Kingdom
*Corresponding Author: Olivin Roosar
Department of Medicine, University of Cambridge, Hills Road, Cambridge, United Kingdom
E-mail: Olivroos@cam.ac.uk
Received date: 01 January, 2023, Manuscript No. JVA-23-95272;
Editor assigned date: 03 January, 2023, PreQC No. JVA-23-95272 (PQ);
Reviewed date: 17 January, 2023, QC No. JVA-23-95272;
Revised date: 24 January, 2023, Manuscript No. JVA-23-95272 (R);
Published date: 30 January, 2023, DOI: 10.4172/2324-8955.1000672
Citation: Roosar O (2023) Novel Viral Proteomics Techniques and Discoveries. J Virol Antivir Res 12:1.
Description
Proteomics, the study of proteins and their functions within a biological system, has emerged as a powerful tool in the field of virology. Viral proteomics involves the systematic analysis of viral proteins and their interactions with host proteins, providing valuable insights into viral pathogenesis, host-virus interactions, and potential targets for antiviral therapies. In recent years, there have been significant advancements in viral proteomics techniques and discoveries that have revolutionized our understanding of viral proteins and their roles in viral infections.
Quantitative proteomics
Quantitative proteomics techniques, such as label-free quantitation and isobaric labelling, have been extensively used in viral proteomics to quantify changes in viral protein abundance during different stages of viral infection, host response, and antiviral treatments. These techniques allow for the accurate and sensitive measurement of viral protein levels and identification of differentially expressed proteins, providing insights into the dynamics of viral protein expression and host response during viral infections [1].
Cross-linking mass spectrometry
Cross-linking mass spectrometry is a powerful technique that enables the identification of protein-protein interactions, including those involving viral proteins [2]. By introducing cross-linking agents that covalently link interacting proteins, followed by protease digestion and mass spectrometry analysis, cross-linked peptides can be identified, providing valuable information on viral protein-protein interactions and their spatial organization within viral particles or host cells [3].
Structural proteomics
Structural proteomics techniques, such as cryo-Electron Microscopy (cryo-EM) and X-ray crystallography, have enabled the determination of high-resolution structures of viral proteins and their complexes with host proteins or inhibitors. These structural insights have provided essential information on the molecular mechanisms underlying viral entry, replication, and immune evasion, which can be exploited for the development of antiviral therapies [4].
Interaction proteomics
Interaction proteomics techniques, such as yeast two-hybrid, coimmunoprecipitation, and protein microarrays, have been widely used to identify and characterize protein-protein interactions involving viral proteins. These techniques allow for the systematic mapping of the viral interactome, revealing intricate networks of protein interactions that are critical for viral replication, assembly, and evasion of host immune response [5].
Post-Translational Modifications (PTMs) profiling
PTMs, such as phosphorylation, ubiquitination, and acetylation, play critical roles in regulating the functions of viral proteins, including viral replication, protein-protein interactions, and immune evasion [6]. Novel proteomics techniques, such as mass spectrometrybased PTM profiling, have allowed for the identification and quantification of PTMs on viral proteins, providing insights into their functional relevance during viral infections and potential targets for antiviral therapies [7].
Viral protein localization studies
Advanced imaging techniques, such as immunofluorescence microscopy, super-resolution microscopy, and proximity labelling, have enabled the visualization and localization of viral proteins within infected cells or viral particles. These studies have provided insights into the subcellular localization of viral proteins, their spatial distribution, and dynamics during different stages of viral infection, shedding light on their functional roles and interactions with host proteins [8,9].
Viral proteomics in clinical research
Viral proteomics techniques have also been employed in clinical research for the diagnosis, prognosis, and monitoring of viral infections [10]. For example, proteomics-based biomarker discovery has led to the identification of viral protein signatures that can be used for early detection and monitoring of viral infections, as well as predicting disease outcomes and response to antiviral treatments.
Conclusion
The field of viral proteomics has witnessed significant advancements in recent years, with novel techniques and discoveries that have expanded our understanding of viral proteins and their roles in viral infections. These advancements have contributed to the development of new antiviral therapies, improved diagnosis and monitoring of viral infections, and deeper insights into viral pathogenesis and host-virus interactions. Viral proteomics continues to be a rapidly evolving field with immense potential for further discoveries and applications in the fight against viral diseases. As technology continues to advance, it is expected that viral proteomics will play an increasingly important role in unravelling the complex interactions between viruses and their hosts, paving the way for innovative strategies for the prevention, diagnosis, and treatment of viral infections.
References
- Aravalli RN, Steer CJ, Cressman ENK (2008) Molecular mechanisms of hepatocellular carcinoma. Hepatology 48:2047-2063.
- Low TY, Syafruddin SE, Mohtar MA, Vellaichamy A, Rahman NSA, et al. (2021) Recent progress in mass spectrometry-based strategies for elucidating protein–protein interactions. Cell Mol Life Sci 78:5325-5339.
- Chavez JD, Bruce JE (2019) Chemical cross-linking with mass spectrometry: a tool for systems structural biology. Curr Opin Chem Biol 48:8-18.
- Wang Y, Kang W, Yang W, Zhang J, Li D, et al. (2021) Structure of African swine fever virus and associated molecular mechanisms underlying infection and immunosuppression: A review. Front Immunol 12:715582.
- Bösl K, Ianevski A, Than TT, Andersen PI, Kuivanen S, et al. (2019) Common nodes of virus–host interaction revealed through an integrated network analysis. Front Immunol 10:2186.
- Wu X, Wang J, Wang S, Wu F, Chen Z et al. (2019) Inhibition of influenza A virus replication by TRIM14 via its multifaceted protein–protein interaction with NP. Front Microbiol 10:344.
- Voinnet O (2005) Induction and suppression of RNA silencing: Insights from viral infections. Nat Rev Genet 6:206-220.
- Coutinho FH, Gregoracci GB, Walter JM, Thompson CC, Thompson FL (2018) Metagenomics sheds light on the ecology of marine microbes and their viruses. Trends Microbiol 26:955-965.
- Brocca S, Grandori R, Longhi S, Uversky V (2020) Liquid–liquid phase separation by intrinsically disordered protein regions of viruses: Roles in viral life cycle and control of virus–host interactions. Int J Mol Sci 21:9045.
- Oved K, Cohen A, Boico O, Navon R, Friedman T, et al. (2015) A novel host-proteome signature for distinguishing between acute bacterial and viral infections. PloS one 10:e0120012.
