Abstract
Six invariant oligopeptide sequences of length 12 amino acids, or greater, were identified in GP1,2 of ZEBOV Zaire and SEBOV Sudan Ebola viruses. Five of these invariant peptides had positive scores for predicted B-cell epitope scores. In contrast, the amino acid positions of the remaining invariant peptide all displayed negative predicted epitope scores. Invariant regions of Ebola GP1,2 oligopeptides may reflect structural, functional and immunological constraints on the virus, and thus, may be useful as immunological and pharmacological targets.
Highlights
A bioinformatic analysis of Ebola virus (EBOV) glycoprotein (GP1,2) [1] is presented here based upon the combined distributions of information entropy [2] and predicted B-cell epitope score [3] in full length GP1,2 protein sequences
The glycosylated GP1, 2 protein of the EBOV virus is cleaved into a GP1 protein and a GP2 protein [9,10]
The immunologic activity predicted in this current study differs from that of a set of antigens originally reported by Wilson el al for EBOV GP1,2 [12]
Summary
A bioinformatic analysis of Ebola virus (EBOV) glycoprotein (GP1,2) [1] is presented here based upon the combined distributions of information entropy [2] and predicted B-cell epitope score [3] in full length GP1,2 protein sequences. Most recognized cases of human infection with EBOV have been caused by ZEBOV (Zaire) and SEBOV (Sudan) [4,5]. This study focuses on GP amino acid sequences of those two EBOV strains
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