key: cord-1003165-f7fgvttt
authors: Moghri, Seyed Amir Hossein Mohammadzadeh Hosseini; Ranjbar, Mojtaba; Hassannia, Hadi; Khakdan, Fatemeh
title: Designing a Novel Multi-Epitope Vaccine against SARS-CoV-2; Implication for Viral Binds and Fusion Inhibition through Inducing Neutralizing Antibodies
date: 2021-06-17
journal: bioRxiv
DOI: 10.1101/2021.06.16.448772
sha: 831be9d20aa5ea6d566722fa352a3f7ebf540cbc
doc_id: 1003165
cord_uid: f7fgvttt

Recently the prevalence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has become a pervasive threat to public health so it is an emergency to vaccine development. The SARS-CoV-2 spike (S) glycoprotein plays a vital role in binds and fusion to the angiotensin-converting enzyme 2 (ACE2). The multi-epitope peptide vaccines are capable of inducing the specific humoral or cellular immune responses. In this regard, the RBD and spike cleavage site is the most probable target for vaccine development to inducing binds and fusion inhibitors neutralizing antibodies. In the present study, several immunoinformatics tools are used for analyzing the spike (S) glycoprotein sequence including the prediction of the potential linear B-cell epitopes, B-cell multi-epitope design, secondary and tertiary structures, physicochemical properties, solubility, antigenicity, and allergenicity for the promising vaccine candidate against SARS-CoV-2.

The amino acid residues of the RBD including 254 amino acids with residues ranging from 330 to 583 121 were selected. I-TASSER generated 3D-model was used to represent the RBD residues of trimeric spike 122 (S) glycoprotein ( Figure 1A ) based on the surface exposed and S-ACE2 ( Figure 1B 

The ABCpred server predicts 25 Linear B cell epitopes, of which 18 had a significant VaxiJen score.

However, among the 18 predicted linear B cell epitopes, 7 epitopes, including "APGQTGKIADYNYK",

"KCYGVSPTKLNDLC","VKNKCVNFNFNGLT","GVGYQPYRVVVLSF","NFNFNGLTGTGVLT",

"PYRVVVLSFELLHA", and "PTKLNDLCFTNVYA" have the VaxiJen score of more than 1. This

suggests the high antigenicity nature of these epitopes and could be considered as the most potential 137 antigenic B cell epitopes that would interact with B lymphocytes and induce neutralizing antibodies 138 ( 

The predicted PSIPRED secondary structure of the final chimeric peptide, which was obtained from PSI-

BLAST, was submitted in FASTA format. Overall, the predicted secondary structure revealed that the 220 protein has 24% alpha-helix, 7% beta-strand, and 68% coil (Fig. 4A) . Besides, taking into account the 221 amino acids solvent accessibility, it was predicted that 43, 21, and 34% of the acids were exposed, 222 medium exposed, and buried, respectively. The RaptorX Property server predicted a total of 17 residues 223 (14%) to be located in disordered domains. 

Recently the prevalence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has become a 275 pervasive threat to public health so it is an emergency to vaccine development (1). As mentioned the RBD 276 protein located in the S1 subunit is responsible for binds to the ACE2 receptor and then due to S1/S2 (38) . In this current study, we constructed six surface-exposed linear B-cell epitopes with AAY linkers. Furthermore, the 680-SPRRAR-685 residue targeting by host proteases at S1/S2 cleavage site was added at the N- 

Immunoinformatics Approach to 397 design T-cell epitope-based vaccine against hendra virus

A novel design of a multi-antigenic, multistage 400 and multi-epitope vaccine against Helicobacter pylori: an in silico approach

Receptor-binding domain as a target for developing SARS 402 vaccines