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The earless monitor lizard Lanthanotus borneensis – a venomous animal?
(2021)
Based on its mandibular gland secretion, the earless monitor lizard, Lanthanotus borneensis, has been considered a venomous animal like other members of the Toxicofera group, including Heloderma. In the present study, the ...
Heterologous hyperimmune polyclonal antibodies against SARS-COV-2: A broad coverage, affordable, and scalable potential immunotherapy for Covid-19
(2021-09)
The emergence and dissemination of the severe acute respiratory syndrome coronavirus 2
(SARS-CoV-2) and the resulting COVID-19 pandemic triggered a global public health crisis.
Although several SARS-CoV-2 vaccines have ...
Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment
(2000)
The venom of the snake Bothrops asper, the most important poisonous snake in Central America, evokes an inflammatory response, the mechanisms of which are not well characterized. The objectives of this study were to ...
Phospholipases a2 from Viperidae snakes: Differences in membranotropic activity between enzymatically active toxin and its inactive isoforms
(Biochimica et Biophysica Acta - Biomembranes vol 1848: 463–468, 2015-02)
We describe the interaction of various phospholipases A2 (PLA2) from snake venoms of the family Viperidae
(Macrovipera lebetina obtusa, Vipera ursinii renardi, Bothrops asper) with giant unilamellar vesicles (GUVs)
composed ...
Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper
(2000-07-15)
Batimastat (BB-94), a synthetic hydroxamate peptidomimetic matrix metalloproteinase inhibitor, was tested for its ability to inhibit proteolytic and toxic effects induced by BaP1, a 24-kDa hemorrhagic metalloproteinase ...
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 ...
Critical role of TLR2 and MyD88 for functional response of macrophages to a group IIA-Secreted phospholipase A2 from snake venom
(PLoS One 9(4):e93741, 2014-04-09)
The snake venom MT-III is a group IIA secreted phospholipase A2 (sPLA2) enzyme with functional and structural similarities with mammalian pro-inflammatory sPLA2s of the same group. Previously, we demonstrated that MT-III ...
Half a century of research on Bothrops asper venom variation: biological and biomedical implications
(2022)
Snake venoms are a complex biological mixture of proteins with or without enzymatic activity, peptides, and nucleotides, among other components. It is produced in specialized secretory glands located in the maxillary region, ...
The lethality test used for estimating the potency of antivenoms against Bothrops asper snake venom: Pathophysiological mechanisms, prophylactic analgesia, and a surrogate in vitro assay
(2015-01)
The potency of antivenoms is assessed by analyzing the neutralization of venom-induced lethality, and is expressed as the Median Effective Dose (ED50). The present study was designed to investigate the pathophysiological ...
Comparative study of the efficacy and safety of two polyvalent, caprylic acid fractionated [IgG and F(ab0)2] antivenoms, in Bothrops asper bites in Colombia
(2012-02)
The efficacy and safety of two polyvalent horse-derived antivenoms in Bothrops asper envenomings were tested in a randomized, double-blind, clinical trial performed in Colombia. Both antivenoms were manufactured from the ...