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Molecular cloning, expression and immunological properties of LiD1, a protein from the dermonecrotic family of Loxosceles intermedia spider venom.
- Source :
-
Toxicon : official journal of the International Society on Toxinology [Toxicon] 2002 Dec; Vol. 40 (12), pp. 1691-9. - Publication Year :
- 2002
-
Abstract
- The present report describes the identification and molecular characterization of LiD1, a protein expressed in the venom gland of the brown spider Loxosceles intermedia. LiD1 belongs to a family of proteins with dermonecrotic activity and members of this family have been found in spiders from the genus Loxosceles. The necrotic lesions caused by this group of proteins may lead to serious socio-economic problems such as surgical tissue reconstitution and even patient death. LiD1 was cloned using a cDNA library constructed from the venom gland of L. intermedia and antibodies against proteins with dermonecrotic activity isolated from the crude venom of this spider. The amino acid sequence deduced from the cDNA revealed a mature protein of approximately 31 kDa, with a pI of 7.37. The cDNA also revealed the existence of a signal peptide, a propeptide and also an untranslated 3' region with 218 nucleotides. LiD1 was expressed as a protein fused with beta-galactoside protein using the vector pBK-CMV, resulting in the recombinant protein recLiD1 with important immunological properties. recLiD1 was strongly recognised by anti-dermonecrotic antibodies and was also able to generate reactive antibodies against native dermonecrotic proteins isolated from the venom of L. intermedia.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Chemical Fractionation
Cloning, Molecular
DNA, Complementary genetics
Gene Expression
Gene Library
Molecular Sequence Data
Recombinant Proteins genetics
Phosphoric Diester Hydrolases genetics
Phosphoric Diester Hydrolases immunology
Phosphoric Diester Hydrolases metabolism
Spider Venoms genetics
Spider Venoms immunology
Spider Venoms metabolism
Spiders physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0041-0101
- Volume :
- 40
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Toxicon : official journal of the International Society on Toxinology
- Publication Type :
- Academic Journal
- Accession number :
- 12457881
- Full Text :
- https://doi.org/10.1016/s0041-0101(02)00201-5