Clavaspirin, an antibacterial and haemolytic peptide from Styela clava.

  title={Clavaspirin, an antibacterial and haemolytic peptide from Styela clava.},
  author={I. H. Lee and C. Zhao and T. Nguyen and Lorenzo P. Menzel and Alan J. Waring and Mark A. Sherman and Robert I. Lehrer},
  journal={The journal of peptide research : official journal of the American Peptide Society},
  volume={58 6},
  • I. LeeC. Zhao R. Lehrer
  • Published 1 December 2001
  • Biology, Chemistry
  • The journal of peptide research : official journal of the American Peptide Society
We cloned the precursor of a novel peptide from a cDNA library prepared from pharyngeal tissues of the tunicate, Styela clava. Its sequence predicted a histidine-rich, amidated 23-residue peptide (FLRF(IG)SVIHGIGHLVHHIGVAL-NH2) that we named clavaspirin. A synthetic clavaspirin was prepared and it was found that it killed Gram-positive and Gram-negative bacteria, permeabilized the outer and inner membranes of Escherichia coli, lysed phosphatidylglycerol (POPG) liposomes, and was potently… 

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New antimicrobial peptide kills drug-resistant pathogens without detectable resistance

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Halocyntin and papillosin, two new antimicrobial peptides isolated from hemocytes of the solitary tunicate, Halocynthia papillosa

Five marine invertebrate species from two taxa (tunicates and echinoderms) are screened for the presence of cationic antimicrobial peptides (AMP) in defence cells (hemocytes) and two novel peptides from H. papillosa hemocytes are isolation and characterization.

Natural Peptide Antibiotics from Tunicates: Structures, Functions and Potential Uses1

The diverse array of antimicrobial peptides in S. clava hemocytes constitutes an effective host defense mechanism and is associated with osmotic disregulation.

Paradoxical Bactericidal Effects of Hydrophobic Lung Surfactant Proteins and Their Peptide Mimics Using Liposome Molecular Trojan.

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Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava.

  • I. LeeY. ChoR. Lehrer
  • Biology
    Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
  • 1997

Membrane activity of the peptide antibiotic clavanin and the importance of its glycine residues.

The combined hydrophobicity, overall state of charge, and conformational flexibility of the peptide determine the (membrane) activity of clavanin A and its Gly --> Ala mutants.

Effects of pH and salinity on the antimicrobial properties of clavanins

Because clavanins exert substantial antimicrobial activity in 0.1 to 0.3 M NaCl, they provide templates for designing broad-spectrum peptide antibiotics intended to function in extracellular environments containing normal or elevated NaCl concentrations, and may allow the design of agents that would function selectively in acidic compartments, such as the gastric lumen, or within phagolysosomes.

Styelin D, an Extensively Modified Antimicrobial Peptide from Ascidian Hemocytes*

The isolated styelin D, a 32-residue, C-terminally amidated antimicrobial peptide, from the blood cells of the solitary ascidian, Styela clava, exhibited activity against Gram-negative and Gram-positive bacteria, and this activity was retained in 200 mm NaCl.

Activities of LL-37, a Cathelin-Associated Antimicrobial Peptide of Human Neutrophils

The broad-spectrum antimicrobial properties of LL-37, its presence in neutrophils, and its inducibility in keratinocytes all suggest that this peptide and its precursor (hCAP-18) may protect skin and other tissues from bacterial intrusions and LPS-induced toxicity.

Anticandidal activity of major human salivary histatins

The results obtained establish the functional relationship of the major histatins with respect to both their fungicidal and fungistatic activities and provide insights into their activities under ionic and pH conditions likely to be encountered in vivo in the oral cavity.