Green pit viper (Trimeresurus albolabris) venom contains a variety of C-type lectin-like proteins (CLPs) causing @entity1423 and consumptive @entity882 in biting victims. @entity68803 (AL-B), a heterodimeric glycoprotein (Gp) Ib-binding protein, was purified from the venom, but there is no reported cDNA sequence and the platelet agglutination mechanism is poorly understood. The full-length AL-B beta clone was obtained from T. albolabris venom gland cDNA library. @entity2928 was, later, derived using 3'-RACE based on the conserved sequence. In this study, purified AL-B dimer agglutinated @entity1 platelets with the EC(50) of 180 nM and was completely inhibited by anti GpIb antibody. MALDI ToF mass spectroscopy found no glycosylation. The peptide mass fingerprints were matched with deduced @entity535 sequences of cloned genes. @entity2928 and beta contained 156 and 146 @entity535 , respectively, including 23-residue signal peptides. AL-B beta showed the conserved hydrophilic patches, putative sites for GpIb binding. Furthermore, there was another conserved motif (SRTY) exclusively in platelet-agglutinating AL-B, @entity9100 -GPIb-BP and @entity68804 . We propose that these three CLPs may function as bivalent adhesive proteins linking two GpIb molecules on adjacent platelets.

Molecular cloning and sequence analysis of XXXX .

@entity1 :: ('9606', 'Species') :: ['human'] @entity882 :: ('MESH:D013921', 'Disease') :: ['thrombocytopenia'] @entity1423 :: ('MESH:D001791', 'Disease') :: ['platelet aggregation'] @entity535 :: ('CHEBI:33704', 'Chemical') :: ['amino acid'] @entity2928 :: ('173', 'Gene') :: ['AL-B alpha'] @entity68803 :: ('MESH:C112004', 'Chemical') :: ['Alboaggregin B'] @entity9100 :: ('12317', 'Species') :: ['TSV'] @entity68804 :: ('MESH:C114784', 'Chemical') :: ['Mamushigin']
@entity68803 :: (MESH:C112004,Chemical) :: ['alboaggregin B']
