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Review
. 2024 Dec;15(1):2401985.
doi: 10.1080/21505594.2024.2401985. Epub 2024 Sep 12.

Host-adaptive mutations in Chikungunya virus genome

Xinhang Ning  1 , Binghui Xia  1 , Jiaqi Wang  1 , Rong Gao  2 , Hao Ren  1
Affiliations
Review

Host-adaptive mutations in Chikungunya virus genome

Xinhang Ning et al. Virulence. 2024 Dec.

Abstract

Chikungunya virus (CHIKV) is the causative agent of chikungunya fever (CHIKF), and its primary vectors are the mosquitoes Aedes aegypti and Aedes albopictus. CHIKV was initially endemic to Africa but has spread globally in recent years and affected millions of people. According to a risk assessment by the World Health Organization, CHIKV has the potential seriously impact public health. A growing body of research suggests that mutations in the CHIKV gene that enhance viral fitness in the host are contributing to the expansion of the global CHIKF epidemic. In this article, we review the host-adapted gene mutations in CHIKV under natural evolution and laboratory transmission conditions, which can help improve our understanding of the adaptive evolution of CHIKV and provide a basis for monitoring and early warning of future CHIKV outbreaks.

Keywords: Chikungunya virus; adaptive mutation; arbovirus; evolution.

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Conflict of interest statement

No potential conflict of interest was reported by the author(s).

Figures

Figure 1.
Figure 1.
Genomic organization of CHIKV.
The 3’UTR structures, based on sequence alignment. Direct repeats are illustrated by different colored blocks, with each of the four colors representing a different homologous sequence region. Sequence gaps in the alignment are indicated by white blocks. The Caribbean strain contains a 177-nucleotide duplication of the 3’ end of 1+2a and complete 1+2b in 3’UTR.
Figure 2.
Lineage-specific structures of the CHIKV 3’UTR.
(a-i) Crystal structure of the mature envelope glycoprotein complex (spontaneous cleavage) of Chikungunya virus. (PDB entry 3N41) with green for E1; cyan for E2; grey for E3. (a) E1-A226V, E2-R198Q, E3-S18F co-mutation [33]. (b) E1-A226V, E1-N20Y, E1-M88L co-mutation [55]. (c) E1-A226V, E1-V80I, E1-A129V co-mutation [53]. (d) E1-A226V, E2- L210Q, E2- K252Q co-mutation [33]. (e) E1-A226V, E1:K211E, E2-V264A co-mutation [45]. (f) E1-A226V, E1-V156A, E1-K211T co-mutation [56]. (g) E1-A226V, E2-G60D, E2-I211T co-mutation [58]. (h) E1-A226V, E2-K233E/Q co-mutation [33]. (i) Map of residue positions before mutation of structural proteins.
Figure 3.
Structural visualization of structural proteins co-mutated residues.
See this image and copyright information in PMC

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