AdDLP, a bacterial defensin-like peptide, exhibits anti-Plasmodium activity

Biochemical and Biophysical Research Communications

Volumn 387, Issue 2, 2009, Pages 393-398

  Gao, Bin ^a   Rodriguez, Maria del Carmen ^b   Lanz Mendoza, Humberto ^b   Zhu, Shunyi ^a  

^a INSTITUTE OF ZOOLOGY   (China)

^b INSTITUTO NACIONAL DE SALUD PÚBLICA   (Mexico)

Author keywords

Antimalarial peptide; Circular dichroism; Cysteine stabilized helical and sheet; Defensin; In vitro folding; Innate immunity; Myxobacterium; Plasmodium; Recombinant expression; Structural prediction

Indexed keywords

ANTIMALARIAL AGENT; CYSTEINE; DEFENSIN; PEPTIDE ADDLP; UNCLASSIFIED DRUG;

AB INITIO CALCULATION; ALGORITHM; ALPHA HELIX; ANAEROMYXOBACTER DEHALOGENANS; ANIMAL CELL; ANTIMALARIAL ACTIVITY; ANTIPROTOZOAL ACTIVITY; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONTROLLED STUDY; DOSE TIME EFFECT RELATION; DRUG DESIGN; ERYTHROCYTE; ESCHERICHIA COLI; GROWTH INHIBITION; MYXOCOCCALES; NONHUMAN; PLASMODIUM; PLASMODIUM BERGHEI; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIMALARIALS; DEFENSINS; DRUG DESIGN; MOLECULAR SEQUENCE DATA; PLASMODIUM; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

ANAEROMYXOBACTER DEHALOGENANS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; MAMMALIA; PLASMODIUM (APICOMPLEXA); PLASMODIUM BERGHEI; PLASMODIUM FALCIPARUM;

EID: 67949089532     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.07.043     Document Type: Article

References (28)

1. Thevissen K., Kristensen H.H., Thomma B.P., Cammue B.P., and François I.E. Therapeutic potential of antifungal plant and insect defensins. Drug Discov. Today 12 (2007) 966-971
2. Zhu S. Discovery of six families of defensin-like peptides in fungi provides insights for origin and evolution of the CSαβ-type defensins. Mol. Immunol. 45 (2008) 828-838
3. Carvalho Ade O., and Gomes V.M. Plant defensins-prospects for the biological functions and biotechnological properties. Peptides 30 (2009) 1007-1020
4. Shahabuddin M., Fields I., Bulet P., Hoffmann J.A., and Miller L.H. Plasmodium gallinaceum: differential killing of some mosquito stages of the parasite by insect defensin. Exp. Parasitol. 89 (1998) 103-112
5. Lowenberger C.A., Kamal S., Chiles J., Paskewitz S., Bulet P., Hoffmann J.A., and Christensen B.M. Mosquito-Plasmodium interactions in response to immune activation of the vector. Exp. Parasitol. 91 (1999) 59-69
6. Boulanger N., Lowenberger C., Volf P., Ursic R., Sigutova L., Sabatier L., Svobodova M., Beverley S.M., Späth G., Brun R., Pesson B., and Bulet P. Characterization of a defensin from the sand fly Phlebotomus duboscqi induced by challenge with bacteria or the protozoan parasite Leishmania major. Infect. Immun. 72 (2004) 7140-7146
7. Cociancich S., Ghazi A., Hetru C., Hoffmann J.A., and Letellier L. Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J. Biol. Chem. 268 (1993) 19239-19245
8. Blandin S., Moita L.F., Köcher T., Wilm M., Kafatos F.C., and Levashina E.A. Reverse genetics in the mosquito Anopheles gambiae: targeted disruption of the Defensin gene. EMBO Rep. 3 (2002) 852-856
9. Cornet B., Bonmatin J.M., Hetru C., Hoffmann J.A., Ptak M., and Vovelle F. Refined three-dimensional solution structure of insect defensin A. Structure 3 (1995) 435-448
10. Landon C., Barbault F., Legrain M., Guenneugues M., and Vovelle F. Rational design of peptides active against the gram positive bacteria Staphylococcus aureus. Proteins 72 (2008) 229-239
11. Mygind P.H., Fischer R.L., Schnorr K.M., Hansen M.T., Sönksen C.P., Ludvigsen S., Raventós D., Buskov S., Christensen B., De Maria L., Taboureau O., Yaver D., Elvig-Jørgensen S.G., Sørensen M.V., Christensen B.E., Kjærulff S.K., Frimodt-Moller N., Lehrer R.I., Zasloff M., and Kristensen H.-H. Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature 437 (2005) 975-980
12. Conde R., Zamudio F.Z., Rodríguez M.H., and Possani L.D. Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion venom. FEBS Lett. 471 (2000) 165-168
13. Klaudiny J., Albert S., Bachanová K., Kopernický J., and Simúth J. Two structurally different defensin genes, one of them encoding a novel defensin isoform, are expressed in honeybee Apis mellifera. Insect Biochem. Mol. Biol. 35 (2005) 11-22
14. Zhu S. Evidence for myxobacterial origin of eukaryotic defensins. Immunogenetics 59 (2007) 949-954
15. Gao B., Sherman P., Luo L., Bowie J., and Zhu S. Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides. FASEB J. 23 (2009) 1230-1245
16. Gao B., Tian C., and Zhu S. Inducible antibacterial response of scorpion venom gland. Peptides 28 (2007) 2299-2305
17. Yuan Y., Gao B., and Zhu S. Functional expression of a Drosophila antifungal peptide in Escherichia coli. Protein Expr. Purif. 52 (2007) 457-462
18. Rodriguez M.C., Zamudio F., Torres J.A., Gonzalez-Ceron L., Possani L.D., and Rodriguez M.H. Effect of a cecropin-like synthetic peptide (Shiva-3) on the sporogonic development of Plasmodium berghei. Exp. Parasitol. 80 (1995) 596-604
19. Trager W., and Jensen J.B. Human malaria parasites in continuous culture. Science 193 (1976) 673-675
20. Zhang Y. Progress and challenges in protein structure prediction. Curr. Opin. Struc. Biol. 18 (2008) 342-348
21. Heinig M., and Frishman D. STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins. Nucleic Acids Res. 32 (2004) W500-W502
22. Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) W668-W673
23. Tamaoki H., Miura R., Kusunoki M., Kyogoku Y., Kobayashi Y., and Moroder L. Folding motifs induced and stabilized by distinct cystine frameworks. Protein Eng. 11 (1998) 649-659
24. Tian C., Gao B., Rodriguez M.C., Lanz-Mendoza H., Ma B., and Zhu S. Gene expression, antiparasitic activity, and functional evolution of the drosomycin family. Mol. Immunol. 45 (2008) 3909-3916
25. Tsuji N., and Fujisaki K. Longicin plays a crucial role in inhibiting the transmission of Babesia parasites in the vector tick Haemaphysalis longicornis. Future Microbiol. 2 (2007) 575-578
26. Boisbouvier J., Prochnicka-Chalufour A., Nieto A.R., Torres J.A., Nanard N., Rodriguez M.H., Possani L.D., and Delepierre M. Structural information on a cecropin-like synthetic peptide, Shiva-3 toxic to the sporogonic development of Plasmodium berghei. Eur. J. Biochem. 257 (1998) 263-273
27. Vizioli J., Bulet P., Hoffmann J.A., Kafatos F.C., Müller H.M., and Dimopoulos G. Gambicin: a novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae. Proc. Natl. Acad. Sci. USA 98 (2001) 12630-12635
28. Carballar-Lejarazú R., Rodríguez M.H., de la Cruz Hernández-Hernández F., Ramos-Castañeda J., Possani L.D., Zurita-Ortega M., Reynaud-Garza E., Hernández-Rivas R., Loukeris T., Lycett G., and Lanz-Mendoza H. Recombinant scorpine: a multifunctional antimicrobial peptide with activity against different pathogens. Cell. Mol. Life Sci. 65 (2008) 3081-3092