The major capsid protein VP2 of human parvovirus B19, when studied in a denatured form exhibiting linear epitopes, is recognized exclusively by immunoglobulin G (IgG) antibodies of patients with acute or recent B19 infection. By contrast, conformational epitopes of VP2 are recognized both by IgG of the acute phase and by IgG of past immunity. In order to localize the VP2 linear epitope(s) specific for acute-phase IgG, the entire B19 capsid protein sequence was mapped by peptide scanning using well-characterized acute-phase and control sera. A unique heptapeptide epitope showing strong and selective reactivity with the acute-phase IgG was detected and characterized. By using this linear epitope (VP2 amino acids 344 to 350) and virus-like particles exhibiting conformational VP2 epitopes, an innovative approach, second-generation epitope-typing enzyme immunoassay, was set up for improved diagnosis of primary infections by human parvovirus B19.

Temporin A is a small, basic, highly hydrophobic, antibacterial peptide found in the skin of the European red frog, Rana temporaria. It was synthesized twice by the FastMoc solid phase method using amino acids protected at the N K -position with either 9-fluorenylmethoxycarbonyl or 2-(4-nitrophenylsulfonyl)ethoxycarbonyl. The syntheses of temporin A demonstrates the difference between 2-(4-nitrophenylsulfonyl)ethoxycarbonyl and 9-fluorenylmethoxycarbonyl amino acids. The purified peptide showed also antibacterial activity against clinically important Gram-positive bacteria. It was found to have a moderately good activity against both methicillin resistant and sensitive strains of Staphylococcus aureus, but a weaker activity against vancomycin resistant strains of Enterococcus faecium.z 1999 Federation of European Biochemical Societies.

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