Abstract
A peptide with haemagglutination activity was isolated from the venom of the Chinese bird spider Selenocosmia huwena by means of ion-exchange and reverse-phase high-performance liquid chromatography. This peptide, named SHLP-I, agglutinates human and mice erythrocytes at a minimum concentration of 125 μg/ml and 31 μg/ml, respectively. It consists of 32 amino acid residues including 3 Trp and 6 Cys residues, the latter of which form three disulfide bounds. The complete amino acid sequence was determined. The N-terminal and C-terminal residues were Gly and Trp, respectively. SHLP-I shows homology with a fragment of great nettle lectin and with huwentoxin-I from the venom of the same spider.
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