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. 1985 Apr;82(8):2240–2243. doi: 10.1073/pnas.82.8.2240

Molecular cloning, cDNA sequencing, and chemical synthesis of cecropin B from Hyalophora cecropia.

P van Hofsten, I Faye, K Kockum, J Y Lee, K G Xanthopoulos, I A Boman, H G Boman, A Engström, D Andreu, R B Merrifield
PMCID: PMC397532  PMID: 3857578

Abstract

Two cDNA clones containing coding information for cecropin B from the Cecropia moth (Hyalophora cecropia) were identified by means of a synthetic probe. Sequencing of the two inserts showed that cecropin B is processed from a 62-amino acid residue precursor molecule including a 26-residue leader peptide and a COOH-terminal glycine residue. The latter presumably donates the nitrogen of the amide group present on the COOH-terminal leucine residue of the mature cecropin B. The sequence deduced for the mature cecropin B differed in the COOH-terminal region from the tentative structure previously determined by carboxypeptidase digestion. To settle the discrepancy, cecropin B was synthesized according to the cDNA sequence with an amidated COOH-terminal leucine. Natural and synthetic cecropin B were found to be indistinguishable with respect to electrophoretic mobility and antibacterial activity against seven different bacteria. The COOH-terminal tetrapeptides were isolated from both natural and synthetic cecropin B and found to be indistinguishable. The correct sequence for cecropin B is (formula; see text).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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