A peptide with haemagglutination activity was isolated from the venom
of the Chinese bird spider Selenocosmia huwena by means of ion-exchang
e and reverse-phase high-performance liquid chromatography. This pepti
de, named SHLP-I, agglutinates human and mice erythrocytes at a minimu
m concentration of 125 mu g/ml and 31 mu g/ml, respectively. It consis
ts of 32 amino acid residues including 3 Trp and 6 Cys residues, the l
atter of which form three disulfide bounds. The complete amino acid se
quence 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
.