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The Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roles
(2009)
A particular subgroup of toxins with phospholipase A2 (PLA2) structure, but devoid of this enzymatic activity, is commonly found in the venoms of snakes of the family Viperidae, and known as the PLA2 homologues. Among ...
Cytotoxicity induced in myotubes by a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops asper: Evidence of rapid plasma membrane damage and a dual role for extracellular calcium
(2007-12)
Acute muscle tissue damage, myonecrosis, is a typical consequence of envenomations by snakes of the family Viperidae. Catalytically-inactive Lys49 phospholipase A2 homologues are abundant myotoxic components in viperid ...
Stability, distribution and use of antivenoms for snakebite envenomation in Latin America: Report of a workshop
(2009-05)
The issues of antivenom stability and distribution, and the training of health staff in the correct use of antivenoms in Latin America were discussed in a workshop held at Instituto Clodomiro Picado, Costa Rica, in September ...
Snake venomics and antivenomics: Proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming
(2009-03-06)
Snakebite envenoming represents a neglected tropical disease that has a heavy public health impact, particularly in Asia, Africa and Latin America. A global initiative, aimed at increasing antivenom production and ...
Immunochemical properties of the N-terminal helix of myotoxin II, a lysine-49 phospholipase A2 from Bothrops asper snake venom
(2001)
Myotoxic class II phospholipases A2 from snake venoms can be divided into Asp49 and Lys49 types. The latter, including
Bothrops asper myotoxin II, exert membrane damage despite lacking catalytic activity. A heparin-binding, ...
Inhibitory effect of fucoidan on the activities of crotaline snake venom myotoxic phospholipases A2
(2003)
Myotoxic phospholipases A2 account for most of the muscle necrosis that results from envenenomation by crotaline snakes. In this study,
we investigated the protective effect of fucoidan, a natural sulfated polysaccharide ...
Comparative study of synthetic peptides corresponding to region 115-129 in Lys49 myotoxic phospholipases A2 from snake venoms
(2003)
Lys49 phospholipase A2 homologues constitute a group of catalytically-inactive proteins, present in the venoms of many
crotalid snakes, which induce myonecrosis. Current evidence supports the mapping of their toxic site ...
Crystallization of the Lys49 PLA2 homologue, myotoxin II from the venom of Atropoides nummifer
(2004-12)
Myotoxin II, a Lys49 catalytically inactive phospholipase A2 homologue from Atropoides nummifer venom, was purified, characterized
and crystallized. The crystals belongs to the tetragonal system, space group P43212, with ...
Identification of the myotoxic site of the Lys49 phospholipase A2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
(2001)
Group II phospholipase A2 (PLA2) myotoxins found in the venoms of Crotalidae snakes can be divided into `Asp49' and
`Lys49' isoforms, the latter being considered catalytically-inactive variants. Previous studies on one ...
Characterization of a basic phospholipase A2-homologue myotoxin isolated from the venom of the snake Bothrops neuwiedii (yarará chica) from Argentina
(1999)
A basic protein was isolated by CM-Sephadex C-25 chromatography from the venom of
Bothrops neuwiedii from Argentina, and named B. neuwiedii myotoxin I. This protein
exerted local myotoxic and edema-forming e ects in mice, ...