Document Detail


Amino acid sequence of a basic aspartate-49-phospholipase A2 from Trimeresurus flavoviridis venom and phylogenetic analysis of Crotalinae venom phospholipases A2.
MedLine Citation:
PMID:  15972222     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Trimeresurus flavoviridis snakes inhabit the southwestern islands of Japan: Amami-Oshima, Tokunoshima and Okinawa. A phospholipase A2 (PLA2) of basic nature (pI 8.5) was isolated from the venom of Amami-Oshima T. flavoviridis. Its amino acid sequence determined by the ordinary procedures was completely in accord with that predicted from the nucleotide sequence of the cDNA previously cloned from Amami-Oshima T. flavoviridis venom gland, which was named PLA-B'. It consists of 122 amino acid residues and has aspartate at position 49. It induced edema in a mouse footpad assay and caused necrosis in mouse skeletal muscles. PLA-B' is similar in sequence to PLA-B (Tokunoshima) and PL-Y (Okinawa), both basic [Asp49]PLA2s, with a few amino acid substitutions, indicating occurrence of interisland mutation. Although PLA2s of Crotalinae subfamily were phylogenetically classified into four types, PLA2 (acidic or neutral [Asp49]PLA2) type, basic [Asp49]PLA2 type, neurotoxic [Asp49]PLA2 type and [Lys49]PLA2 type, it was ascertained that PLA2s of PLA2 type and [Lys49]PLA2 type are most essential as toxic components for Crotalinae snake venoms and that basic [Asp49]PLA2-type PLA2s are uniquely contained only in the venoms of T. flavoviridis species. Prediction of physiological activities of some PLA2s was made based on their location in the phylogenetic tree. Relationship of divergence of PLA2s via accelerated evolution followed by less rapid mutation and physiological activities was discussed.
Authors:
Takahito Chijiwa; Kazuki Abe; Tomohisa Ogawa; Nikolai N Nikandrov; Shosaku Hattori; Naoko Oda-Ueda; Motonori Ohno
Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Toxicon : official journal of the International Society on Toxinology     Volume:  46     ISSN:  0041-0101     ISO Abbreviation:  Toxicon     Publication Date:  2005 Aug 
Date Detail:
Created Date:  2005-07-12     Completed Date:  2005-10-20     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  1307333     Medline TA:  Toxicon     Country:  England    
Other Details:
Languages:  eng     Pagination:  185-95     Citation Subset:  IM    
Affiliation:
Department of Applied Life Science, Faculty of Engineering, Sojo University, Kumamoto 860-0082, Japan. chijiwa@life.sojo-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence / genetics*
Animals
Base Sequence
Cluster Analysis
Crotalid Venoms / enzymology,  genetics*
Electrophoresis, Polyacrylamide Gel
Japan
Molecular Sequence Data
Phospholipases A / genetics*
Phospholipases A2
Phylogeny*
Sequence Analysis, DNA
Trimeresurus / genetics*
Chemical
Reg. No./Substance:
0/Crotalid Venoms; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Phospholipases A2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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