CLUSTAL 2.1 multiple sequence alignment of diphospho mevalonate decarboxylases from <i>Brugia malayi</i> (<i>Bm</i>MVD), <i>Loa loa</i> (<i>Ll</i>MVD), <i>Homo sapiens</i> (<i>Hs</i>MVD) and <i>Saccharomyces cerevisiae</i> (<i>Sc</i>MVD), highlighting two regions in the published <i>Bm</i>MVD sequences that diverge from the consensus between the orthologous protein sequences. Elizabeth Bilsland Daniel M. Bean Eileen Devaney Stephen G. Oliver 10.1371/journal.pntd.0004401.g001 https://plos.figshare.com/articles/figure/_CLUSTAL_2_1_multiple_sequence_alignment_of_diphospho_mevalonate_decarboxylases_from_Brugia_malayi_Bm_MVD_Loa_loa_Ll_MVD_Homo_sapiens_Hs_MVD_and_Saccharomyces_cerevisiae_Sc_MVD_highlighting_two_regions_in_the_published_Bm_MVD_sequences_that_diverge_from_t/1642732 <p>These could be due to the presence of different splice variants of the <i>Brugia</i> enzyme, natural insertions or errors in the published sequence.* conserved residues;: chemically conserved changes;. non-conserved changes.</p> 2016-01-28 12:42:22 World Health Organization filarial compound aid antihelmintic drug development Brugia malayi drug targets contracting lymphatic filariasis complement yeast deletions Identify Novel Compounds Brugia malayi BackgroundLymphatic filariasis strain parasite enzymes worms Wuchereria bancrofti Brugia malayi enzymes