Application of Domain 4 of ILY for treatment and prevention of foreign ; pathogen infection

Summary Streptococcus intermedius intermedilysin (ILY) secreted by Streptococcus intermedius is a cholesterol-dependent cytolysin that shows the specific feature of hemolytic activity towards human cells, but not other animal cells. CDF9, a glycosylphosphatidylinostitol (CPI)-linked membrane protein is a key inhibitor for restricting the formation of the membrane attack complex of complement (MAC) by binding to complement proteins C8 and C9 and preventing C9 incorporation and polymerization. Complement is a main mediator for acquired immune (antibody) mediated response to kill foreign pathogens, such as viruses and parasites. ILY specifically binds human erythrocytes and lyses only cells that express hCD59 through binding to the hCD59 C8 and c9 binding site. Specifically, the a particular domain of ILY contains a critical binding site for hCD59. Therefore, this domain of ILY and complement proteins C8 and C9 recognize the same or overlapping regions of hCD59. Indeed, the small peptides derived from this domain of ILY inhibit the human cd59 function. Based on these results, we propose that the modified peptide derived from a domain ILY can be applied for blocking hCD59 function to enhance complement mediated immune reaction to foreign pathogens for the treatment and prevention of foreign pathogens such as virus and parasite infection.

Applications For Further Information Please Contact the Director of Business Development Alex Szidon Email: [email protected] Telephone: (617) 495-3067

Inventor(s): Qin, Xuebin

Type of Offer: Licensing



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