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1.C.17 The Cecropin (Cecropin) Family

Many organisms synthesize proteins (or peptides) which are degraded to relatively small hydrophobic or amphipathic, bioactive peptides. These peptides exhibit antibiotic, fungicidal, virucidal, hemolytic and/or tumoricidal activities by interacting with membranes and forming transmembrane channels that allow the free flow of electrolytes, metabolites and water across the phospholipid bilayers. Most of these peptides appear to function in biological warfare. There are many designations given to these bioactive peptides. They include the magainins, cecropins, melittins, defensins, bacteriocidins, etc. The proteins in each family within this functional superfamily are homologous, but they exhibit little or no significant sequence similarity with members of the other families. Thus, each family may have evolved independently. However, certain common structural features observed between members of distinct families suggest that at least some of these families share a common ancestry.

The generalized transport reaction catalyzed by channel-forming amphipathic peptides is:

small solutes, electrolytes and water (in) small solutes, electrolytes and water (out).

Several families of eukaryotic channel-forming amphipathic peptide, each from a different group of organisms, are recognized. Other non-insect derived cecropin-like peptides are members of the Cecropin superfamily.

Cecropins are produced by insects, particularly under conditions of infection. Cecropins A, B and D are close homologues consisting of 35-39 residues. They are found in the pupae of the cecropin moth, but related homologues named lepodopteran, bactericidin, moricin and sarcotoxin are produced by other insects.

This family belongs to the: Cecropin Superfamily.

References associated with 1.C.17 family:

Bechinger, B. (1997). Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156: 197-211. 9096062
Bechinger, B., M. Zasloff and S.J. Opella (1993). Structure and orientation of the antibiotic peptide magainin in membrane by solid-state nuclear magnetic resonance spectroscopy. Prot. Sci. 2: 2077-2084. 8298457
Efimova, S.S., L.V. Schagina, and O.S. Ostroumova. (2014). Channel-forming activity of cecropins in lipid bilayers: effect of agents modifying the membrane dipole potential. Langmuir 30: 7884-7892. 24969512
Ganz, T., J.R. Rayner, E.V. Valore, A. Tumolo, K. Talmadge and F. Fuller (1989). The structure of the rabbit macrophage defensin genes and their organ-specific expression. J. Immunol. 143: 1358-1365. 2745983
Gudmundsson, G.H., D.A. Lidholm, B. Asling, R.B. Gan and H.G. Boman (1991). The cecropin locus–cloning and expression of a gene cluster encoding 3 antibacterial peptides in Hyalophora cecropia. J. Biol. Chem. 266: 11510-11517. 1711035
Hill, C.P., J. Yee, M.E. Selsted and D. Eisenberg (1991). Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science 251: 1481-1485. 2006422
Lee, I.H., C. Zhao, Y. Cho, S.S. Harwig, E.L. Cooper, and R.I. Lehrer. (1997). Clavanins, α-helical antimicrobial peptides from tunicate hemocytes. FEBS Lett. 400: 158-162. 9001389
Matsuzaki, K. (1998). Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta 1376: 391-400. 9804997
Nagaoka, I., A. Someya, K. Iwabuchi and T. Yamashita (1991). Characterization of cDNA clones encoding guinea pig neutrophil cationic peptides. FEBS Lett. 280: 287-291. 2013325
Pardi, A., X.L. Zhang, M.E. Selsted, J.J. Skalicky and P.F. Yip (1992). NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1. Biochemistry 31: 11357-11364. 1445873
Tamang, D.G. and M.H. Saier, Jr. (2006). The cecropin superfamily of toxic peptides. J. Mol. Microbiol. Biotechnol. 11: 94-103. 16825792
Taylor, S.W., A.G. Craig, W.H. Fischer, M. Park, and R.I. Lehrer. (2000). Styelin D, an extensively modified antimicrobial peptide from ascidian hemocytes. J. Biol. Chem. 275: 38417-38426. 10978343
Terwilliger, T.C. and D. Eisenberg (1982). The structure of melittin. II. Interpretation of the structure. J. Biol. Chem. 257: 6016-6022.
Vlasak, R., C. Unger-Ullmann, G. Kreil and A.M. Frischauf (1983). Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin. Eur. J. Biochem. 135: 123-126. 6309516
Zhang, X.L., M.E. Selsted and A. Pardi (1992). NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1. Biochemistry 31: 11348-11356. 1445872
Zhao, C., L. Liaw, I.H. Lee, and R.I. Lehrer. (1997). cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava. FEBS Lett. 412: 144-148. 9257708