Lentivirus-derived antimicrobial peptides: Increased potency by sequence engineering and dimerization

Journal of Antimicrobial Chemotherapy

Volumn 44, Issue 1, 1999, Pages 33-41

  Tencza, Sarah Burroughs ^a,d   Creighton, Donald J ^a   Yuan, Tao ^b   Vogel, Hans J ^b   Montelaro, Ronald C ^a,c   Mietzner, Timothy A ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALGARY   (Canada)

^c Biomedical Science Tower ^*  (United States)

^d Cellomics Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CYSTEINE; DISULFIDE; ENVELOPE PROTEIN; GLUTAMIC ACID; PEPTIDE;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACTERICIDAL ACTIVITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; EUKARYOTIC CELL; GENETIC ENGINEERING; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; HEMOLYSIS; HUMAN; HUMAN CELL; LENTIVIRINAE; PROTEIN SECONDARY STRUCTURE; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTI-BACTERIAL AGENTS; ANTI-INFECTIVE AGENTS; CIRCULAR DICHROISM; DIMERIZATION; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; HIV ENVELOPE PROTEIN GP41; HIV-1; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0032815922     PISSN: 03057453     EISSN: None     Source Type: Journal    
DOI: 10.1093/jac/44.1.33     Document Type: Article

References (44)

1. von Hofsten, P., Faye, I., Kockum, K., Lee, J. Y., Xanthopoulos, K. G., Boman, I. A. et al. (1985). Molecular cloning, cDNA sequencing, and chemical synthesis of cecropin B from Hyalophora cecropia. Proceedings of the National Academy of Sciences of the USA 82, 2240-3.
2. Christensen, B., Fink, J., Merrifield, R. B. & Mauzerall, D. (1988). Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proceedings of the National Academy of Sciences of the USA 85, 5072-6.
3. Ganz, T., Selsted, M. E., Szklarek, D., Harwig, S. S., Daher, K., Bainton, D. F. et al. (1985). Defensins. Natural peptide antibiotics of human neutrophils. Journal of Clinical Investigation 76, 1427-35.
4. Agerberth, B., Gunne, H., Odeberg, J., Kogner, P., Boman, H. G. & Gudmundsson, G. H. (1995). FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proceedings of the National Academy of Sciences of the USA 92, 195-9.
5. Miyasaki, K. T., Qu, X. D., Harwig, S. S., Cho, Y. & Lehrer, R. I. (1995). Identification of CG-1, a natural peptide antibiotic derived from human neutrophil cathepsin G. Advances in Dental Research 9, 63-6.
6. Boman, H. G. (1995). Peptide antibiotics and their role in innate immunity. Annual Review of Immunology 13, 61-92.
7. Nicolas, P. & Mor, A. (1995). Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annual Review of Microbiology 49, 277-304.
8. Zasloff, M. (1992). Antibiotic peptides as mediators of innate immunity. Current Opinion in Immunology 4, 3-7.
9. Kelley, K. J. (1996). Using host defenses to fight infectious diseases. Nature Biotechnology 14, 587-90.
10. Stinson, S. C. (1996). Drug firms restock antibacterial arsenal. Chemical and Engineering News 75-100.
11. Jacob, L. & Zasloff, M. (1994). Potential therapeutic applications of magainins and other antimicrobial agents of animal origin. Ciba Foundation Symposia 186, 197-216.
12. Tencza, S. B., Douglass, J. P., Creighton, D. J., Montelaro, R. C. & Mietzner, T. A. (1997). Novel antimicrobial peptides derived from human immunodeficiency virus type 1 and other lentivirus envelope proteins. Antimicrobial Agents and Chemotherapy 41, 2394-8.
13. Hancock, R. E. W. (1997). Peptide antibiotics. Lancet 349, 418-22.
14. Zasloff, M. (1987). Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proceedings of the National Academy of Sciences of the USA 84, 5449-53.
15. Diamond, G., Zasloff, M., Eck, H., Brasseur, M., Maloy, W. L. & Bevins, C. L. (1991). Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA. Proceedings of the National Academy of Sciences of the USA 88, 3952-6.
16. Kokryakov, V. N., Harwig, S. S., Panyutich, E. A., Shevchenko, A. A., Aleshina, G. M., Shamova, O. V. et al. (1993). Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Letters 327, 231-6.
17. Maloy, W. L. & Kari, U. P. (1995). Structure-activity studies on magainins and other host defense peptides. Biopolymers 37, 105-22.
18. Merrifield, R. B., Juvvadi, P., Andreu, D., Ubach, J., Boman, A. & Boman, H. G. (1995). Retro and retroenantio analogs of cecropin-melittin hybrids. Proceedings of the National Academy of Sciences of the USA 92, 3449-53.
19. Wade, D., Andreu, D., Mitchell, S. A., Silviera, A. M. V., Boman, A. & Merrifield, R. B. (1992). Antibacterial peptides designed as analogs or hybrids of cecropins and melittin. International Journal of Peptide and Protein Research 40, 429-36.
20. Miller, M. A., Garry, R. F., Jaynes, J. M. & Montelaro, R. C. (1991). A structural correlation between lentivirus transmembrane proteins and natural cytolytic peptides. AIDS Research and Human Retroviruses 7, 511-19.
21. Miller, M. A., Cloyd, M. W., Liebmann, J., Rinaldo, C. R., Islam, K. R., Wang, S. Z. et al. (1993). Alterations in cell membrane permeability by the lentivirus lytic peptide (LLP-1) of HIV-1 transmembrane protein. Virology 196, 89-100.
22. Tencza, S. B., Miller, M. A., Islam, K., Mietzner, T. A. & Montelaro, R. C. (1995). Effect of amino acid substitutions on calmodulin binding and cytolytic properties of the LLP-1 peptide segment of human immunodeficiency virus type 1 transmembrane protein. Journal of Virology 69, 5199-202.
23. Yuan, T., Mietzner, T. A., Montelaro, R. C. & Vogel, H. J. (1995). Characterization of the calmodulin-binding domain of SIV transmembrane glycoprotein by NMR and CD spectroscopy. Biochemistry 34, 10690-6.
24. Srinivas, S. K., Srinivas, R. V., Anantharamaiah, G. M., Segrest, J. P. & Compans, R. W. (1992). Membrane interactions of synthetic peptides corresponding to amphipathic helical segments of the human immunodeficiency virus type-1 envelope glycoprotein. Journal of Biological Chemistry 267, 7121-7.
25. Comardelle, A. M., Norris, C. H., Plymale, D. R., Gatti, P. J., Choi, B., Fermin, C. D. et al. (1997). A synthetic peptide corresponding to the carboxy terminus of human immunodeficiency virus type 1 transmembrane glycoprotein induces alterations in the ionic permeability of Xenopus laevis oocytes. AIDS Research and Human Retroviruses 13, 1525-32.
26. Miller, M. A., Mietzner, T. A., Cloyd, M. W., Robey, W. G. & Montelaro, R. C. (1993). Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein. AIDS Research and Human Retroviruses 9, 1057-66.
27. Srinivas, S. K., Srinivas, R. V., Anantharamaiah, G. M., Compans, R. W. & Segrest, J. P. (1993). Cytosolic domain of the HIV envelope glycoproteins binds to calmodulin and inhibits calmodulin-regulated proteins. Journal of Biological Chemistry 268, 22895-9.
28. Tencza, S. B., Mietzner, T. A. & Montelaro, R. C. (1997). Calmodulin-binding function of LLP segments from the HIV-1 transmembrane protein is conserved among natural sequence variants. AIDS Research and Human Retroviruses 13, 263-9.
29. Fontenot, J. D., Ball, J. M., Miller, M. A., David, C. M. & Montelaro, R. C. (1991). A survey of potential problems and quality control in peptide synthesis by the fluorenylmethoxycarbonyl procedure. Peptide Research 4, 19-25.
30. Tam, J. P., Wong, C.-R., Liu, W. & Zhang, J.-W. (1991). Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications. Journal of the American Chemical Society 113, 6657-62.
31. Schagger, H. & von Jagow, G. (1987). Tricine-sodium dodecyl sullate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analytical Biochemistry 166, 368-79.
32. Electrophoresis Technical Service Group. Ready Gels Application Guide. Number 161-0993. Bio-Rad, Hercules, CA.
33. Scholtz, J. M., Qian, H., York, E. J., Stewart, J. M. & Baldwin, R. L. (1991). Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers 31, 1463-70.
34. Chernomordik, L., Chanturiya, A. N., Suss-Toby, E., Nora, E. & Zimmerberg, J. (1994). An amphipathic peptide from the C-terminal region of the human immunodeficiency virus envelope glycoprotein causes pore formation in membranes. Journal of Virology 66, 7115-23.
35. Gawrisch, K., Han, K. H., Yang, J. S., Bergelson, L. D. & Ferretti, J. A. (1993). Interaction of peptide fragment 828-848 of the envelope glycoprotein of human immunodeficiency virus type I with lipid bilayers. Biochemistry 32, 3112-18.
36. Fujii, G., Horvath, S., Woodward, S., Eiserling, F. & Eisenberg, D. (1992). A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41. Protein Science 1, 1454-64.
37. Lee, I. H., Zhao, C., Cho, Y., Harwig, S. S., Cooper, E. L. & Lehrer, R. I. (1997). Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes. FEBS Letters 400, 158-62.
38. Lee, I. H., Cho, Y. & Lehrer, R. I. (1997). Effects of pH and salinity on the antimicrobial properties of clavanins. Infection and Immunity 65, 2898-903.
39. Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., Zasloff, M. & Wilson, J. M. (1997). Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88, 553-60.
40. Dathe, M., Wieprecht, T., Nikolenko, H., Handel, L., Maloy, W. L., MacDonald, D. L. et al. (1997). Hydrophobicity, hydrophobic moment, and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Letters 403, 208-12.
41. Selsted, M. E., Brown, D. M., DeLange, R. J. & Lehrer, R. I. (1983). Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. Journal of Biological Chemistry 256, 14485-9.
42. Hill, C. P., Yee, J., Selsted, M. E. & Eisenberg, D. (1991). Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science 251, 1481-5.
43. Zhang, X. L., Selsted, M. E. & Pardi, A. (1992). NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1. Biochemistry 31, 11348-56.
44. Fahrner, R. L., Dieckmann, T., Harwig, S. S., Lehrer, R. I., Eisenberg, D. & Feigon, J. (1996). Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chemistry and Biology 3, 543-50.