Article
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Intrinsic Disorder in the Host Proteins Entrapped in the Rabies Virus Particles
Version 1
: Received: 20 March 2024 / Approved: 21 March 2024 / Online: 21 March 2024 (14:05:24 CET)
How to cite: Ashraf, H. N.; Uversky, V. N. Intrinsic Disorder in the Host Proteins Entrapped in the Rabies Virus Particles. Preprints 2024, 2024031317. https://doi.org/10.20944/preprints202403.1317.v1 Ashraf, H. N.; Uversky, V. N. Intrinsic Disorder in the Host Proteins Entrapped in the Rabies Virus Particles. Preprints 2024, 2024031317. https://doi.org/10.20944/preprints202403.1317.v1
Abstract
Proteomic analysis of purified rabies virus (RABV) revealed 47 entrapped host proteins within viral particles. Out of these, 11 proteins were highly disordered. Our study was particularly focused on five of the RABV-entrapped mouse proteins with the highest levels of disorder, Neuromodulin, Chmp4b, DnaJB6, Vps37B, and Wasl. We extensively utilized bioinformatics tools, such as FuzDrop, D2P2, UniProt, RIDAO, STRING, AlphaFold, and ELM for comprehensive analysis of the intrinsic disorder propensity of these proteins. Our analysis suggested that these disordered host proteins might play a significant role in facilitating the rabies virus pathogenicity, immune system evasion, and the development of the antiviral drug resistance. Our study highlighted the complex interaction of the virus with its host, with the focus on how the intrinsic disorder can play a crucial role in virus pathogenic processes and suggested that these intrinsically disordered proteins (IDPs) and disorder-related host interactions can also be a potential target for the therapeutic strategies.
Keywords
rabies virus; intrinsically disordered proteins; protein-protein interactions; Neuromodulin; Chmp4b; DnaJB6; Vps37B, Wasl
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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