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. 2012 Jan;19(1):30–36. doi: 10.1128/CVI.05466-11

Fig 1.

Fig 1

Alignment of the amino acid residues of the coding regions of DBPII-SalI and DEKnull. The gene coding for the ligand domain of DBPII-SalI was used as a template to create a novel synthetic DBPII allele (DEKnull). The most highly variant cluster of polar charged residues within the dominant B-cell epitope (underlined) identified in a previous study (12) was mutated to either alanine, threonine, or serine. Asterisks show different polymorphic sites within the DBP region II (39).