Viral hijacking mechanism in humans through protein-protein interactions.

COVID-19 Hijacking Protein–protein interactions SARS-CoV-2 Spike Viral entry

Journal

Advances in protein chemistry and structural biology
ISSN: 1876-1631
Titre abrégé: Adv Protein Chem Struct Biol
Pays: Netherlands
ID NLM: 101497281

Informations de publication

Date de publication:
2022
Historique:
entrez: 25 7 2022
pubmed: 26 7 2022
medline: 27 7 2022
Statut: ppublish

Résumé

Numerous viruses have evolved mechanisms to inhibit or alter the host cell's apoptotic response as part of their coevolution with their hosts. The analysis of virus-host protein interactions require an in-depth understanding of both the viral and host protein structures and repertoires, as well as evolutionary mechanisms and pertinent biological facts. Throughout the course of a viral infection, there is constant battle for binding between virus and cellular proteins. Exogenous interfaces facilitating viral-host interactions are well known for constantly targeting and suppressing endogenous interfaces mediating intraspecific interactions, such as viral-viral and host-host connections. In these interactions, the protein-protein interactions (PPIs), are mostly shown as networks (protein interaction networks, PINs), with proteins represented as nodes and their interactions represented as edges. Host proteins with a higher degree of connectivity are more likely to interact with viral proteins. Due to technical advancements, three-dimensional interactions may now be visualized computationally utilizing molecular modeling and cryo-EM approaches. The uniqueness of viral domain repertoires, their evolution, and their activities during viral infection make viruses fascinating models for research. This chapter aims to provide readers a complete picture of the viral hijacking mechanism in protein-protein interactions.

Identifiants

pubmed: 35871893
pii: S1876-1623(22)00033-5
doi: 10.1016/bs.apcsb.2022.05.001
pii:
doi:

Substances chimiques

Viral Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

261-276

Informations de copyright

Copyright © 2022 Elsevier Inc. All rights reserved.

Auteurs

Chandrabose Selvaraj (C)

Computer Aided Drug Design and Molecular Modeling Lab, Department of Bioinformatics, Science Block, Alagappa University, Karaikudi, Tamil Nadu, India. Electronic address: drbioselva@gmail.com.

Gurunathan Rubha Shri (GR)

Computer Aided Drug Design and Molecular Modeling Lab, Department of Bioinformatics, Science Block, Alagappa University, Karaikudi, Tamil Nadu, India.

Rajendran Vijayakumar (R)

Department of Biology, College of Science in Zulfi, Majmaah University, Majmaah, Saudi Arabia.

Abdulaziz S Alothaim (AS)

Department of Biology, College of Science in Zulfi, Majmaah University, Majmaah, Saudi Arabia.

Saravanan Ramya (S)

Computer Aided Drug Design and Molecular Modeling Lab, Department of Bioinformatics, Science Block, Alagappa University, Karaikudi, Tamil Nadu, India.

Sanjeev Kumar Singh (SK)

Computer Aided Drug Design and Molecular Modeling Lab, Department of Bioinformatics, Science Block, Alagappa University, Karaikudi, Tamil Nadu, India. Electronic address: skysanjeev@gmail.com.

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Classifications MeSH