Research Article

Computational Identification and Characterization of a Promiscuous T-Cell Epitope on the Extracellular Protein 85B of Mycobacterium spp. for Peptide-Based Subunit Vaccine Design

Figure 5

Multiple sequence alignment of amino acid sequences of HLA-DRB1 series. The T-Coffee server was used for multiple alignment of the N-terminal 90 amino acid residues of the HLA-DRB alleles. The HLA-DRB10101 sequence was chosen as reference. Identities of the residues are illustrated by dashes. Positions 15(C), 61(W), 64(Q), 66(D), and 82(N) are indicated as boxes to present no polymorphic binding site in the MHC protein. Binding residues are labeled red, bold, italic, and underlined. Identical binding residues in MHC proteins are indicated as red dashes.