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Inactivation of C5a Anaphylatoxin by a Peptide That Is Complementary to a Region of C5a ¹

Emiko Fujita^*, Imre Farkas^*,, William Campbell, Lajos Baranyi, Hidechika Okada and Noriko Okada^2,*

^* Department of Biodefense, Nagoya City University Graduate School of Medical Sciences, Nagoya, Japan; Choju Medical Institute, Fukushimura Hospital, Toyohashi, Japan; and Department of Endocrine Neurobiology, Institute of Experimental Medicine, Hungarian Academy of Science, Budapest, Hungary

PL37 (RAARISLGPRCIKAFTE) is an antisense homology box peptide composed of aa 37–53 of C5a-anaphylatoxin and is considered to be the region essential for C5a function. Using a computer program, we designed the complementary peptides ASGAPAPGPAGPLRPMF (Pep-A) and ASTAPARAGLPRLPKFF (Pep-B). Pep-A bound to PL37 and to C5a with very slow dissociation as determined by analysis using surface plasmon resonance, whereas Pep-B failed to bind at all. C5a was inactivated by concentrations of 7 nM or more of Pep-A, and this concentration of Pep-A inhibited induction of intracellular Ca²⁺ influx in neutrophils. Patch clamp electrophysiology experiments also showed the effectiveness of Pep-A in C5aR-expressing neuroblastoma cells. Furthermore, Pep-A administration prevented rats from C5a-mediated rapid lethal shock induced by an Ab to a membrane inhibitor of complement after LPS sensitization.