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Volume 271, Number 45, Issue of November 8, 1996 pp. 28533-28540
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Antibacterial Activity of Glycosylated and Phosphorylated Chromogranin A-derived Peptide 173-194 from Bovine Adrenal Medullary Chromaffin Granules

(Received for publication, April 8, 1996)

Jean-Marc Strub , Yannick Goumon , Karine Lugardon , Calliope Capon ^§ , Michel Lopez ^§ , Marc Moniatte ^¶ , Alain Van Dorsselaer ^¶ , Dominique Aunis and Marie-Hélène Metz-Boutigue

From the  INSERM, Unité 338 de Biologie de la Communication Cellulaire, Strasbourg, 67084 France, the ^§ CNRS, Laboratoire de Chimie Biologique, UMR 111, Villeneuve d'Ascq, 59655 France, and the ^¶ CNRS, Laboratoire de Spectrométrie de Masse Bioorganique, URA 31, Chimie Organique des Substances Naturelles, 67084 Strasbourg, France

Recently, we have isolated from bovine chromaffin granules and identified two natural peptides possessing antibacterial activity: secretolytin (chromogranin B 614-626) and enkelytin (proenkephalin-A 209-237). Here, we characterize a large natural fragment, corresponding to chromogranin A 79-431, that inhibits growth of both Gram-positive and Gram-negative bacteria. The aim of the present work was to determine the shortest active peptide located in the 79-431 chromogranin A region. Three peptides, which shared the same 173-194 chromogranin A sequence (YPGPQAKEDSEGPSQGPASREK) but differed in post-translational modifications, including O-glycosylation and tyrosine phosphorylation, were isolated. A detailed study using microsequencing and mass spectrometry allowed us to correlate their antibacterial activity with these post-translational modifications. The chromogranin A precursor fragment (79-431) and the active glycosylated and phosphorylated peptides were, respectively, named prochromacin and chromacin (P, G, and PG for phosphorylated, glycosylated, and phosphorylated-glycosylated form).

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