Abstract
Chikungunya virus (CHIKV) is a mosquito-borne alphavirus. The outbreak of CHIKV infection has been seen in many tropical and subtropical regions of the biosphere. Current reports evidenced that after outbreaks in 2005–06, the fitness of this virus propagating in Aedes albopictus enhanced due to the epistatic mutational changes in its envelope protein. In our study, we evaluated the prevalence of intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) in CHIKV proteome. IDPs/IDPRs are known as members of a ‘Dark Proteome’ that defined as a set of polypeptide segments or whole protein without unique three-dimensional structure within the cellular milieu but with significant biological functions, such as cell cycle regulation, control of signaling pathways, and maintenance of viral proteomes. However, the intrinsically disordered aspects of CHIKV proteome and roles of IDPs/IDPRs in the pathogenic mechanism of this important virus have not been evaluated as of yet. There are no existing reports on the analysis of intrinsic disorder status of CHIKV. To fulfil this goal, we have analyzed the abundance and functionality of IDPs/IDPRs in CHIKV proteins, involved in the replication and maturation. It is likely that these IDPs/IDPRs can serve as novel targets for disorder based drug design.
Highlights
Chikungunya fever is triggered by an arthropod-borne virus known as Chikungunya virus (CHIKV) that is transmitted by mosquitoes (Aedes aegypti and Aedes albopictus)[1] and is disseminated at a higher rate in tropical regions
A recent study evidenced the mutational changes happen in the E1 and E2 proteins that are identified as K211E and A226V (E1) and V264A (E2) polymorphism[7]
It has been found that mutational changes occur in the disordered loop regions of E1 and E2 protein. These mutational changes trigger the conformational change in E1 protein to enhance the fitness of CHIKV propagating in Indian Aedes agepty & Aedes albopictus[7]
Summary
Chikungunya fever is triggered by an arthropod-borne virus (arbovirus) known as Chikungunya virus (CHIKV) that is transmitted by mosquitoes (Aedes aegypti and Aedes albopictus)[1] and is disseminated at a higher rate in tropical regions. Most of the dark proteome are IDPs of hybrid proteins containing ordered domains and IDPRs16, which show specific functions without being folded into unique 3D structure under physiological conditions[17] It is known, hydrophobic interaction plays a driving force in protein folding[18]. Structural and non-structural proteins of Zika virus has MoRF regions that regulate the functionality of this virus[34] Being disordered, these proteins increase the probability of binding to their partners by providing greater capture radii; i.e., utilizing a binding mode known as a fly-casting mechanism[35]. Despite this fly-casting mechanism, it was proposed that some disordered systems such as transactivation domain of c-Myb region, cannot speed up the recognition events between an IDP and its partner[36] In recent studies, it is evidenced IDPs/IDPRs play a vital role in the establishment of several macromolecular complexes[37] and serve as assembly hubs[38]. We have analyzed the dark proteome of CHIKV and evaluated disordered regions of viral proteins in terms of their functional significance
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
