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An immunoinformatics approach to promiscuous peptides design for Plasmodium falciparum erythrocyte membrane protein-1

Abstract

Plasmodium falciparum erythrocyte membrane protein-1 (Pfemp-1) a variant adhesion molecule can acts as key component of immunity against malaria. In the current scenario of malaria vaccines, no efficient vaccines are available that can be employed for its proper treatment. Unfortunately, resistance to post-infection treatments is increasing and therefore there is pressing need to develop an efficient vaccine. Peptide-based vaccines can also be an effective tool against malaria but HLA restriction is major hindrance which can be conquer by promiscuous peptides. In this work, we employed a combine in silico and experimental approach to identify promiscuous peptide towards the treatment of malaria. At first, using the immunoinformatics approach, promiscuous peptides were predicted from two conserved domains CIDR-1 and DBL-3γ of Pfemp-1 antigen. These peptides were selected on the basis of predicted binding affinity with different HLA Class-I & Class-II alleles. A total of 13 peptides were selected based on their predicted IFN-γ and IL-4 inducer as well as hydrophobicity attribute. Out of these 13, the peptide C6 was synthesised and experimental evaluated for further rationalization, HLA-peptide complex modelling and binding interaction analysis. Interestingly, the peptide C6 (SFIHIYLYRNIRIQL) showed an encouraging immunological response and T-cell proliferation in immunological assay. Those valuable content can add in better designing of more potent and selective vaccine candidates against infectious diseases.

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Publication details

The article was received on 03 Jun 2017, accepted on 10 Aug 2017 and first published on 11 Aug 2017


Article type: Paper
DOI: 10.1039/C7MB00332C
Citation: Mol. BioSyst., 2017, Accepted Manuscript
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    An immunoinformatics approach to promiscuous peptides design for Plasmodium falciparum erythrocyte membrane protein-1

    N. khan, R. kumar, S. Chauhan and U. Farooq, Mol. BioSyst., 2017, Accepted Manuscript , DOI: 10.1039/C7MB00332C

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