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Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
Open accessAbstract
Immune challenge to the insect Podisus maculiventris induces synthesis of a 21-residue peptide with sequence homology to frog skin antimicrobial peptides of the brevinin family. The insect and frog peptides have in common a C-terminally located disulfide bridge delineating a cationic loop. The peptide is bactericidal and fungicidal, exhibiting the largest antimicrobial spectrum observed so far for an insect defense peptide. An all-D-enantiomer is nearly inactive against Gram-negative bacteria and some Gram-positive strains but is fully active against fungi and other Gram-positive bacteria, suggesting that more than one mechanism accounts for the antimicrobial activity of this peptide. Studies with truncated synthetic isoforms underline the role of the C-terminal loop and flanking residues for the activity of this molecule for which we propose the name thanatin.
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Citations
Cited by
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168
Anti-microbial peptides: from invertebrates to vertebrates
Bulet, P., Stöcklin, R., & Menin, L. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.0124.x · Cited by 1,107
Self-citationAntimicrobial peptides in insects; structure and function
Bulet, P., Hetru, C., Dimarcq, J.-L., & Hoffmann, D. (1999) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(99)00015-4 · Cited by 1,041
Self-citationDestoumieux, D., Bulet, P., Loew, D., Van Dorsselaer, A., Rodriguez, J., & Bachère, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28398 · Cited by 441
Self-citationInnate immunity in higher insects
Hoffmann, J. A., Reichhart, J.-M., & Hetru, C. (1996) · Current Opinion in Immunology · doi:10.1016/s0952-7915(96)80098-7 · Cited by 358
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Metadata
- Authors
- Fehlbaum, P., Bulet, P., Chernysh, S., Briand, J. P., Roussel, J. P., Letellier, L., Hetru, C., & Hoffmann, J. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-02-06
- Volume
- 93
- Issue
- 3
- Pages
- 1221-1225
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2020374832
- Cited by
- 330
- References
- 0
- FWCI
- 9.85
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. https://app.cochat.ai/papers/10.1073/pnas.93.3.1221
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- Fehlbaum, P., Bulet, P., Chernysh, S., Briand, J. P., Roussel, J. P., Letellier, L., Hetru, C., & Hoffmann, J. A. (1996). Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.3.1221
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