Primary structure of two cytolysin isoforms from Stichodactyla helianthus differing in their hemolytic activity

Abstract:

Sticholysin I (St-I) and sticholysin II (St-II) are cytolysins purified from the sea anemone Stichodactyla helianthus with a high degree of sequence identity (93%) but clearly differenced in their hemolytic activity. In order to go further into the structural determinants for the different behavior of St-I and St-II, we report here the complete amino acid sequences and the consensus secondary structure pbkp_rediction of both proteins. The complete determination of St-II primary structure confirms the partial revision of cytolysin III amino acid sequence. All nonconservative changes between St-I and St-II are located at the N-terminal. According to our pbkp_rediction these changes could be located at the same face of an α-helix during pore formation events and could account for the observed differences in hemolytic activity between St-I and St-II. © 2001 Elsevier Science Ltd.

Año de publicación:

2001

Keywords:

• Secondary structure pbkp_rediction
• Cytolysin
• Sea anemone
• Primary structure

Fuente:

scopus