Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A

Karine Lugardon, Roselyne Raffner, Yannick Goumon, Angelo Corti, Agnès Delmas, Philippe Bulet, Dominique Aunis, Marie Hélène Metz-Boutigue

Research output: Contribution to journalArticlepeer-review

Abstract

Vasostatin-1, the natural N-terminal 1-76 chromogranin A (CGA)-derived fragment in bovine sequence, has been purified from chromaffin secretory granules and identified by sequencing and matrix-assisted laser desorption time-of-flight mass spectrometry. This peptide, which displays antibacterial activity against Gram-positive bacteria at micromolar concentrations, is also able to kill a large variety of filamentous fungi and yeast cells in the 1-10 μM range. We have found that the C-terminal moiety of vasostatin-1 is essential for the antifungal activity, and shorter active peptides have been synthesized. In addition, from the comparison with the activity displayed by related peptides (human recombinant and rat synthetic fragments), we could determine that antibacterial and antifungal activities have different structural requirements. To assess for such activities in vivo, CGA and CGA- derived fragments were identified in secretory material released from human polymorphonuclear neutrophils upon stimulation. Vasostatin-1, which is stored in a large variety of cells (endocrine, neuroendocrine, and neurons) and which is liberated from stimulated chromaffin and immune cells upon stress, may represent a new component active in innate immunity.

Original languageEnglish
Pages (from-to)10745-10753
Number of pages9
JournalJournal of Biological Chemistry
Volume275
Issue number15
DOIs
Publication statusPublished - Apr 14 2000

ASJC Scopus subject areas

  • Biochemistry

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