Abstract:
:C-type lectins are calcium-dependent sugar binding proteins and are distributed ubiquitously amongst vertebrate organisms. As part of a wider study on Australian snake venom components, we have identified and characterised a C-type lectin from the venom of Oxyuranus scutellatus (Australian coastal taipan) with mannose-binding activity. This protein exhibited a subunit molecular mass of 15 kDa and was found to bind mannose and also bind to and agglutinate erythrocytes in a Ca(2+)-dependent manner. cDNA transcripts coding for C-lectin proteins were cloned and sequenced from six Australian elapid snake species and an antibody generated against the O. scutellatus mannose-binding C-lectin identified C-lectin proteins in the venom of 13 Australian elapid snakes by immunoblotting. Experimental evidence and molecular modelling also suggest that this protein exhibits a unique dimeric structure. This is the first confirmed example of a snake venom C-lectin with mannose-binding activity.
journal_name
Biochimiejournal_title
Biochimieauthors
Earl ST,Robson J,Trabi M,de Jersey J,Masci PP,Lavin MFdoi
10.1016/j.biochi.2010.11.006subject
Has Abstractpub_date
2011-03-01 00:00:00pages
519-27issue
3eissn
0300-9084issn
1638-6183pii
S0300-9084(10)00412-8journal_volume
93pub_type
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