New proline-rich oligopeptides from the venom of African adders: Insights into the hypotensive effect of the venoms

Kodama, Roberto Tadashi; Cajado-Carvalho, Daniela; Kuniyoshi, Alexandre Kazuo; Kitano, Eduardo S.; Barna, Bárbara; Takakura, Ana C.; Serrano, Solange M.T.; Dias-Da-Silva, W.; Tambourgi, Denise V.; Portaro, Fernanda Vieira

doi:10.1016/j.bbagen.2015.02.005

Cited by 24 publications

(23 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…venoms. This mixture has been enriched by the inclusion of purified B. arietans blood pressure-hypotensive factor (Kodama et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Souza¹,

Magnoli²,

Silva³

2015

Afr. J. Biotechnol.

View full text Add to dashboard Cite

Better characterization of individual snake venom toxins is useful for analyzing the association of their toxic domains and relevant antigenic epitopes. Here we analyzed the Bitis arietans hemorrhagicinducing toxin present in a representative venom sample. Among the 1´ to 5´ protein peaks isolated using a Sephacryl S 100 HR chromatography column, hemorrhagic activity was expressed by all according to the following intensity, P´5 > P´3 > P´2 >, P´4. The proteins were recognized and measured with antibodies present in polyvalent horse F(ab)´2 anti-B. arietans, Bitis spp., Lachesis muta, B. atrox, Bothrops spp., Crotalus spp., and Naja spp. or in IgY anti-B. arietans and anti-Bitis spp. using enzymelinked immunosorbent assays and western blotting. In addition, in an in vitro-in vivo assay these antivenoms were able to block hemorrhagic-inducing activity. The evident cross-reactivity expressed by different specific anti-venoms indicates that metalloproteinases induce an immunological signature indicating the presence of similar antigenic epitopes for several snake venoms.

show abstract

“…venoms. This mixture has been enriched by the inclusion of purified B. arietans blood pressure-hypotensive factor (Kodama et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

“…The introduction of toxins responsible for hemorrhage Gutiérrez et al, 2005), complement system activating factors and hypotension-inducing components (Kodama et al, 2015) present in Bitis sp. venom into an immunogenic mixture is considered essential to obtain high quality mono-specific anti-venom.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Souza¹,

Magnoli²,

Silva³

2015

Afr. J. Biotechnol.

View full text Add to dashboard Cite

show abstract

“…First, only proteins and large peptides are retained in the electrophoretic gels, while peptides smaller than 2-3 kDa are lost. Short peptides can be abundant components of some snake venoms, and may display relevant bioactivities [35]. An additional drawback of the gel-based strategies is the limited dynamic range of protein concentrations in the original sample that can be resolved electrophoretically into non-overlapping spots, which also bears a relationship to the maximal limits in sample loads of the 2DE technique.…”

Section: Proteomic Approaches Pro Et Contramentioning

confidence: 99%

Strategies in ‘snake venomics’ aiming at an integrative view of compositional, functional, and immunological characteristics of venoms

Lomonte

Calvete

2017

J Venom Anim Toxins Incl Trop Dis

116

View full text Add to dashboard Cite

This work offers a general overview on the evolving strategies for the proteomic analysis of snake venoms, and discusses how these may be combined through diverse experimental approaches with the goal of achieving a more comprehensive knowledge on the compositional, toxic, and immunological characteristics of venoms. Some recent developments in this field are summarized, highlighting how strategies have evolved from the mere cataloguing of venom components (proteomics/venomics), to a broader exploration of their immunological (antivenomics) and functional (toxicovenomics) characteristics. Altogether, the combination of these complementary strategies is helping to build a wider, more integrative view of the life-threatening protein cocktails produced by venomous snakes, responsible for thousands of deaths every year.

show abstract

“…Until now, according to the literature, some toxins have been isolated from the Bitis arietans venom including: hemorrhagic [24–26], and non-hemorrhagic metalloproteases [27]; serine proteases with kinin-releasing and fibrinogenolytic activities [28], a fibrinogenase which is able to inhibit platelet aggregation [29]; phospholipases A 2 like bitanarina which blocks ionic channels [30] and bitiscetina that induces platelet aggregation [31, 32]; a pro-coagulant C-type lectin-like [33]; and bitistatin [acession number: P17497], also known as arietin, that inhibited platelets aggregation [34]. Recently, a family of peptides from this venom with angiotensin-converting enzyme (ACE) inhibitory activity, the BPPs (Bradykinin-potentiating peptides), was described as presenting hypotensive activity in vivo [35] .…”

Section: Introductionmentioning

confidence: 99%

Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities

Megale

Magnoli

Kuniyoshi

et al. 2018

J Venom Anim Toxins Incl Trop Dis

Self Cite

View full text Add to dashboard Cite

BackgroundBitis arietans is a venomous snake found in sub-Saharan Africa and in parts of Morocco and Saudi Arabia. The envenomation is characterized by local and systemic reactions including pain, blistering, edema and tissue damage, besides hemostatic and cardiovascular disturbances, which can cause death or permanent disabilities in its victims. However, the action mechanisms that provoke these effects remain poorly understood, especially the activities of purified venom components. Therefore, in order to elucidate the molecular mechanisms that make the Bitis arietans venom so potent and harmful to human beings, this study reports the isolation and biochemical characterization of a snake venom serine protease (SVSP).MethodsSolubilized venom was fractionated by molecular exclusion chromatography and the proteolytic activity was determined using fluorescent substrates. The peaks that showed serine protease activity were determined by blocking the proteolytic activity with site-directed inhibitors. In sequence, the fraction of interest was submitted to another cycle of molecular exclusion chromatography. The purified serine protease was identified by mass spectrometry and characterized biochemically and immunochemically.ResultsA serine protease of 33 kDa with fibrinogen-degrading and kinin-releasing activities was isolated, described, and designated herein as Kn-Ba. The experimental Butantan Institute antivenom produced against Bitis arietans venom inhibited the Kn-Ba activity.ConclusionsThe in vitro activities of Kn-Ba can be correlated with the capacity of the venom to provoke bleeding and clotting disorders as well as hypotension, which are common symptoms presented by envenomed victims. Obtaining satisfactory Kn-Ba inhibition through the experimental antivenom is important, given the WHO’s recommendation of immunotherapy in cases of human accidents with venomous snakes.Electronic supplementary materialThe online version of this article (10.1186/s40409-018-0176-5) contains supplementary material, which is available to authorized users.

show abstract

New proline-rich oligopeptides from the venom of African adders: Insights into the hypotensive effect of the venoms

Abstract: Although proline-rich oligopeptides are known molecules, we present here 32 new sequences that are inhibitors of the angiotensin-converting enzyme and consistent with the symptoms of the victims of Bitis spp, who display severe hypotension.

Cited by 24 publications

References 38 publications

Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Strategies in ‘snake venomics’ aiming at an integrative view of compositional, functional, and immunological characteristics of venoms

Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities

Contact Info

Product

Resources

About