Anionic C-Terminal Proregion of Nematode Antimicrobial Peptide Cecropin P4 Precursor Inhibits Antimicrobial Activity of the Mature Peptide

Satoshi UENO; Kohtaro KUSAKA; Yasushi TAMADA; Masaomi MINABA; Hong ZHANG; Pi-Chao WANG; Yusuke KATO

doi:10.1271/bbb.80397

This article has now been updated. Please use the final version.

Anionic C-Terminal Proregion of Nematode Antimicrobial Peptide Cecropin P4 Precursor Inhibits Antimicrobial Activity of the Mature Peptide

Satoshi UENO, Kohtaro KUSAKA, Yasushi TAMADA, Masaomi MINABA, Hong ZHANG, Pi-Chao WANG, Yusuke KATO

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Keywords: cecropin, antimicrobial peptide, precursor, innate immunity, nematode

JOURNAL FREE ACCESS Advance online publication

Article ID: 80397

DOI https://doi.org/10.1271/bbb.80397

The final version of this article is now available: Vol. 72 (2008) , No. 12 p.3281

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Abstract

Recently, an anionic proregion was found to be conserved at the C terminus of the antimicrobial peptide, nematode cecropin. Our results suggest that the antimicrobial activity of mature peptide is suppressed by the proregion in its precursor and is released from inhibition after processing. Inhibition is not likely to be due to direct suppression of membrane disruption.

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