10.1371/journal.pntd.0004401.g001 Elizabeth Bilsland Elizabeth Bilsland Daniel M. Bean Daniel M. Bean Eileen Devaney Eileen Devaney Stephen G. Oliver Stephen G. Oliver 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. Public Library of Science 2016 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 2016-01-28 12:42:22 Figure 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>