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However, evolutionary relation of these immune molecules remains unresolved. Venoms, as key weapons of venomous arthropods for prey and defense, receive increasing recognition as an emerging source of such peptides. From a cDNA library prepared from the venom gland of the scorpion\n                    <jats:italic>Mesobuthus eupeus<\/jats:italic>\n                    , clones encoding precursors of two new AMPs, named meucin\u201013 (IFGAIAGLLKNIF\u2010NH\n                    <jats:sub>2<\/jats:sub>\n                    ) and meucin\u201018 (FFGHLFKLATKIIPSLFQ), have been isolated. The precursor of meucins consists of a signal peptide, a mature peptide, and an acidic propeptide, in which dibasic residues as the typical processing signal are located between the mature and propeptide. Meucin\u201013 is an ortholog of several previously described AMPs from scorpion venom and has also detectable sequence similarity to temporins, a large family of AMPs from frog skin, whereas meucin\u201018 displays some similarity to AMPs from diverse origin including arthropod venoms, fish mast cells, and frog skins. These two meucin peptides form \u03b1\u2010helical structure in the presence of 50% trifluoroethanol (TFE), a membrane\u2010mimicking environment, as identified by circular dichroism (CD) spectroscopy. This finding is further verified by their NMR structures that show a typical \u03b1\u2010helical amphipathic design, a structural prerequisite for cytolytic activity. Meucins exhibit extensive cytolytic effects on both prokaryotic and eukaryotic cells (gram\n                    <jats:sup>+<\/jats:sup>\n                    and gram\n                    <jats:sup>\u2010<\/jats:sup>\n                    bacteria, fungi, yeasts, rabbit erythrocytes, and rat dorsal root ganglion cells) at micromolar concentrations. It is remarkable that muecin\u201018 was 2\u2010 to &gt; 14\u2010fold more potent than meucin\u201013 against nearly all the cells tested. Structural differences in hydrophilic\/hydrophobic balance and cationic amino acid location between two meucins could account for their differential potency. Despite these differences, commonalities at precursor organization, three\u2010dimensional structure, and biological function suggests that meucins are two evolutionarily related AMPs and likely originated from a common ancestor by gene duplication. Our work presented here also provides new insights into an evolutionary link among AMPs from invertebrates and vertebrates and clues for evolutionary convergence between AMPs and virus fusion domains.\u2014Gao, B., Sherman, P., Luo, L., Bowie, J., Zhu, S. Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides.\n                    <jats:italic>FASEB J<\/jats:italic>\n                    . 23, 1230\u20131245 (2009)\n                  <\/jats:p>","DOI":"10.1096\/fj.08-122317","type":"journal-article","created":{"date-parts":[[2008,12,16]],"date-time":"2008-12-16T22:59:28Z","timestamp":1229468368000},"page":"1230-1245","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":74,"title":["Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides"],"prefix":"10.1096","volume":"23","author":[{"given":"Bin","family":"Gao","sequence":"first","affiliation":[{"name":"Group of Animal Innate Immunity State Key Laboratory of Integrated Management of Pest Insects and Rodents Institute of Zoology Chinese Academy of Sciences Beijing China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"Sherman","sequence":"additional","affiliation":[{"name":"Department of Chemistry The University of Adelaide Adelaide South Australia Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lan","family":"Luo","sequence":"additional","affiliation":[{"name":"Group of Animal Innate Immunity State Key Laboratory of Integrated Management of Pest Insects and Rodents Institute of Zoology Chinese Academy of Sciences Beijing China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Bowie","sequence":"additional","affiliation":[{"name":"Department of Chemistry The University of Adelaide Adelaide South Australia Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shunyi","family":"Zhu","sequence":"additional","affiliation":[{"name":"Group of Animal Innate Immunity State Key Laboratory of Integrated Management of Pest Insects and Rodents Institute of Zoology Chinese Academy of Sciences Beijing China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,16]]},"reference":[{"key":"e_1_2_4_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/415389a"},{"key":"e_1_2_4_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.0105-2896.2004.0124.x"},{"key":"e_1_2_4_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/35104690"},{"key":"e_1_2_4_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.molimm.2008.01.007"},{"key":"e_1_2_4_6_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/17.5.1217"},{"key":"e_1_2_4_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.peptides.2007.10.004"},{"key":"e_1_2_4_8_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2796.2003.01228.x"},{"key":"e_1_2_4_9_1","doi-asserted-by":"publisher","DOI":"10.1517\/13543784.15.8.933"},{"key":"e_1_2_4_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro1098"},{"key":"e_1_2_4_11_1","doi-asserted-by":"crossref","unstructured":"Zhu S. andGao B.(2008)A fossil antibacterial peptide gives clues to structural diversity of cathelicidin-derived host defense peptides. 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