Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-6-30
pubmed:abstractText
A new myotoxin was isolated from the venom of Bothrops atrox from Colombia. B. atrox myotoxin I is a homodimer, with a subunit molecular mass of 13,826, and a pI of 8.9. Its complete nucleotide sequence was obtained by cDNA cloning, indicating a mature product of 122 residues that belongs to the family of Lys49 phospholipase A(2) (PLA(2)) homologues, a subgroup of catalytically inactive proteins within the group IIA. Accordingly, the toxin was devoid of phospholipase and anticoagulant activities, in vitro. In mice, it induced conspicuous local myonecrosis, edema, and a systemic interleukin-6 response. In vitro, it was cytolytic upon myoblasts, and weakly bactericidal. The toxin showed highest homology with other Lys49 PLA(2)s, both in its primary and three-dimensional modeled structure, although with an evident difference in the C-terminal region. Unlike Lys49 proteins of American crotalids having 121 residues, this toxin presents an insertion (Asn) between positions 118 and 119. Despite several substitutions within the C-terminal region 115-129 between B. atrox myotoxin I and B. asper myotoxin II, antibodies against synthetic peptide 115-129 of the latter were strongly cross-reactive to the former, indicating the antigenic conservation of this site, known to be critical for the membrane-damaging activities of Lys49 myotoxins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
91-101
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15225567-Amino Acid Sequence, pubmed-meshheading:15225567-Animals, pubmed-meshheading:15225567-Antibodies, pubmed-meshheading:15225567-Base Sequence, pubmed-meshheading:15225567-Bothrops, pubmed-meshheading:15225567-Cross Reactions, pubmed-meshheading:15225567-Crotalid Venoms, pubmed-meshheading:15225567-DNA, Complementary, pubmed-meshheading:15225567-Edema, pubmed-meshheading:15225567-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15225567-Group II Phospholipases A2, pubmed-meshheading:15225567-Immunoenzyme Techniques, pubmed-meshheading:15225567-Interleukin-6, pubmed-meshheading:15225567-Mice, pubmed-meshheading:15225567-Molecular Sequence Data, pubmed-meshheading:15225567-Muscle, Skeletal, pubmed-meshheading:15225567-Myoblasts, pubmed-meshheading:15225567-Necrosis, pubmed-meshheading:15225567-Neurotoxins, pubmed-meshheading:15225567-Phospholipases A, pubmed-meshheading:15225567-Phospholipases A2, pubmed-meshheading:15225567-Protein Conformation, pubmed-meshheading:15225567-Reptilian Proteins, pubmed-meshheading:15225567-Sequence Alignment, pubmed-meshheading:15225567-Sequence Analysis, DNA
pubmed:year
2004
pubmed:articleTitle
Structural and functional characterization of myotoxin I, a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops atrox.
pubmed:affiliation
Programa de Ofidismo, Facultad de Medicina, Universidad de Antioquia, A.A. 1226, Medellin, Colombia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't