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Text Content

Article


COMPUTATIONAL EXPLORATION OF B AND T-CELL EPITOPES IN THE DEVELOPMENT OF A
MULTI-EPITOPE SUBUNIT VACCINE AGAINST ALONGSHAN VIRUS

 * March 2024
 * Journal of Biomolecular Structure and Dynamics

Authors:
Hassan Ayaz


Hassan Ayaz
 * This person is not on ResearchGate, or hasn't claimed this research yet.



Faisal Ahmad
 * Quaid-i-Azam University



Bushra Rehman
 * BACHA KHAN UNIVERSITY CHARSADDA



Sajjad Ahmad
 * Abasyn University



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ABSTRACT

Alongshan virus (ALSV), a tick-borne phlebovirus discovered in China, has also
been reported in Russia, Mongolia, Finland, and Germany. While few human cases
primarily experience fever, headache, accompanied by fatigue, coma, depression,
nausea, myalgia/arthralgia, and skin rash, ALSV's high prevalence in domestic
animals and ticks raises concerns about its potential for wider human
transmission in the future. Since most viral infections lack effective drug
treatments, vaccination remains a crucial strategy for preventing viral spread.
This study aimed to design an in-silico multi-epitope vaccine (MEV) against ALSV
using its essential structural proteins (VP1a, VP1b, and VP3). Immunoinformatics
methods were employed to predict T and B cell antigenic determinants within
these proteins, paving the way for a potential ALSV vaccine. The MEV candidate
was constructed by linking selected B and T cell epitopes with suitable linkers
and incorporating beta-defensin as an adjuvant. Following structure prediction
and refinement, the vaccine candidate exhibited an impressive ERRAT stability
score of 97.45% and a minimal RMSD value of only 0.241. Docking simulations with
TLR-4 revealed numerous interacting residues, further confirming the vaccine's
potential interaction with the immune system. In-silico cloning using E. coli as
the host yielded a favorable codon adaptation index (CAI) value of 0.93,
indicating optimal protein expression within this chosen host. Additionally,
molecular dynamics simulations of the vaccine-complex during a 150ns run
suggested a stable environment. Analyses like RMSD, radius of gyration, and RMSF
confirmed minimal changes, primarily in the active site loop region. Moreover,
MMGBSA/PBSA calculations yielded high binding affinities (-226.15 and 227.18
kcal/mol), signifying a strong interaction between the vaccine and its target.
While this study showcases a promising in-silico vaccine design, experimental
validation remains crucial to confirm its efficacy and safety for further
development.

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