.png){kind=icon}
.png){kind=icon}
Return
An in-silico study exploring the differences between the G protein of Chandipura virus isolates with respect to their antigenic sites and their interaction with vimentin
.png){kind=icon}
PRE
AI
D
P
S
M
R
D
S
R
D
C
B
DOI：10.1016/j.ijmmb.2026.101083.png)
.png){kind=icon}
Original request for help.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
Purpose: Chandipura virus (CHPV), belonging to the Rhabdoviridae family, is an emerging pathogen linked to encephalitis outbreaks, especially in children under 15 years of age. CHPV is primarily spread by sandflies and has led to several outbreaks in India, but CHPV strains from African nations namely Senegal, Kenya and Nigeria are not associated with human infections. This study involved an in-silico analysis aimed at exploring the differences in the G protein between the Indian and African CHPV isolates which would explain the above anomaly. Methods: Multiple Sequence Alignment was carried out to identify the amino acid substitution sites between all the Indian and the African CHPV isolates. Additionally, Profile Sequence Alignment (PSA) analysis was also conducted to localize the identified conserved amino acid substitutions between the Indian and the African CHPV G protein, focusing on potential antigenic sites and critical viral domains. Furthermore, an in-silico analysis has been carried out to assess the binding affinity of the CHPV G protein of different countries with the host coreceptor vimentin that is known to be involved in virus entry. Results: Our results indicated that the Indian and the African CHPV G protein sequences exhibited amino acid variations at 19 conserved sites, which were localized within the antigenic sites and other critical viral domains, including the fusogenic site of the CHPV G protein. Furthermore, our analysis predicted significant alterations in either solvent accessibility or torsional angle rotation stemming from the amino acid variations at the aforementioned sites. Additional in-silico analysis also revealed that the Indian CHPV G protein exhibited a markedly superior binding affinity with vimentin compared to its African counterparts. Conclusion: Therefore, the current study provides important findings regarding the variations of the CHPV G protein and highlighting essential amino acid residues that may be targeted for development of future antiviral therapies.
Keywords:
Chandipura
India
Africa
Mutations
In-silico
Journal
IF:
1.3
Papers:
91
Citations:
2.0K