» Articles » PMID: 35539973

Understanding the Interactability of Chikungunya Virus Proteins Molecular Recognition Feature Analysis

Overview
Journal RSC Adv
Specialty Chemistry
Date 2022 May 11
PMID 35539973
Authors
Affiliations
Soon will be listed here.
Abstract

The chikungunya virus (CHIKV) is an alphavirus that has an enveloped icosahedral capsid and is transmitted by sp. mosquitos. It contains four non-structural proteins, namely nsP1, nsP2, nsP3, and nsP4, encoded at the 5' end of the genome, and five structural proteins encoded at the 3' end of the genome, including three glycosylated proteins, namely E1, E2, E3, a small 64 amino-acids glycoprotein 6K, and one non-glycosylated nucleocapsid protein C. The surface of this positive-stranded RNA alphavirus is covered with 80 trimeric glycoprotein spikes, which facilitate viral access into the host cell, with each consisting of three copies of E1-E2 heterodimers. The proper folding of p62, which is the precursor of E2, and formation of the E1-p62 heterodimers are controlled by E3, which is therefore essential for producing mature spikes on the alphavirus surface. Finally, 6K, a small 64 amino-acids glycoprotein, assists in the translocation of structural polyproteins to the endoplasmic reticulum and in the cleavage of p62 into mature structural proteins E2. The CHIKV proteins have been shown to contain variable levels of intrinsic disorder, often containing intrinsically disordered protein regions (IDPRs). IDPRs can interact with many unrelated partners, and these interactions are frequently accompanied by a transition from a disordered to ordered state. The corresponding sub-regions of IDPRs are acknowledged as molecular recognition features (MoRFs). Although the existence of IDPRs in CHIKV proteome has been analyzed, the prevalence of disorder-based protein-protein interactions ( MoRF) in this virus have not been evaluated as of yet. To fill this gap, in our study, we utilized several computational methods to identify the MoRFs regions in CHIKV proteins. These computational tools included ANCHOR, DISOPRED3, MoRFpred and MoRFchibi_web server. These analyses revealed the presence of numerous MoRF regions in all the CHIKV proteins. In future, the results of this study could be used to identify the nature of chikungunya virus pathogenesis and might be helpful in designing drugs against this virus.

Citing Articles

Structure Characterization of a Disordered Peptide Using In-Droplet Hydrogen/Deuterium Exchange Mass Spectrometry and Molecular Dynamics.

Rahman M, Sultana M, Sharif D, Mahmud S, Legleiter J, Li P ACS Phys Chem Au. 2025; 5(1):17-29.

PMID: 39867440 PMC: 11758492. DOI: 10.1021/acsphyschemau.4c00048.


Identification of RACK1 as a novel regulator of non-structural protein 4 of chikungunya virus.

Yan Y, Zhang F, Zou M, Chen H, Xu J, Lu S Acta Biochim Biophys Sin (Shanghai). 2024; 56(10):1425-1436.

PMID: 38813597 PMC: 11532265. DOI: 10.3724/abbs.2024073.


Chikungunya in Zhejiang Province, Southeast China.

Ren J, Ling F, Liu Y, Sun J Infect Med (Beijing). 2024; 2(4):315-323.

PMID: 38205180 PMC: 10774776. DOI: 10.1016/j.imj.2023.11.005.


DeepBindPPI: Protein-Protein Binding Site Prediction Using Attention Based Graph Convolutional Network.

Sunny S, Prakash P, Gopakumar G, Jayaraj P Protein J. 2023; 42(4):276-287.

PMID: 37198346 PMC: 10191823. DOI: 10.1007/s10930-023-10121-9.


Hepatitis C Virus Infection and Intrinsic Disorder in the Signaling Pathways Induced by Toll-Like Receptors.

Redwan E, Aljadawi A, Uversky V Biology (Basel). 2022; 11(7).

PMID: 36101469 PMC: 9312352. DOI: 10.3390/biology11071091.


References
1.
Midic U, Oldfield C, Dunker A, Obradovic Z, Uversky V . Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome. Protein Pept Lett. 2009; 16(12):1533-47. DOI: 10.2174/092986609789839377. View

2.
Ranea J, Morilla I, Lees J, Reid A, Yeats C, Clegg A . Finding the "dark matter" in human and yeast protein network prediction and modelling. PLoS Comput Biol. 2010; 6(9). PMC: 2944794. DOI: 10.1371/journal.pcbi.1000945. View

3.
Oldfield C, Meng J, Yang J, Yang M, Uversky V, Dunker A . Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics. 2008; 9 Suppl 1:S1. PMC: 2386051. DOI: 10.1186/1471-2164-9-S1-S1. View

4.
Uchime O, Fields W, Kielian M . The role of E3 in pH protection during alphavirus assembly and exit. J Virol. 2013; 87(18):10255-62. PMC: 3754015. DOI: 10.1128/JVI.01507-13. View

5.
Nguyen P, Yu H, Keller P . Identification of chikungunya virus nsP2 protease inhibitors using structure-base approaches. J Mol Graph Model. 2015; 57:1-8. DOI: 10.1016/j.jmgm.2015.01.001. View