Anticoagulation factor I, a snaclec (snake C-type lectin) from Agkistrodon acutus venom binds to FIX as well as FX: Ca2+ induced binding data

Zhang, Yan; Xu, Xiao-lei; Shen, Dengke; Song, Jiajia; Guo, Mingchun; Yan, Xincheng

doi:10.1016/j.toxicon.2012.03.006

Cited by 22 publications

(10 citation statements)

References 26 publications

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“…The first one includes toxic components that can induce a hemolytic effect or hemorrhaging, such as venom plasminogen activator, snaclec, lectoxin-Enh4, and fibrinogenase brevinase (Family A). Eight unigenes were classified into this family, three of which were matched well with snaclec (identity 32–35%), a snake C-type lectin from snake venom that binds specifically with activated factor X (FXa) and prolongs the blood-clotting time in vitro15. This kind of toxin can lead to severe nephrotoxicity and hypovolemia.…”

Section: Resultsmentioning

confidence: 99%

Deciphering the Venomic Transcriptome of Killer-Wasp Vespa velutina

Liu

Chen

Zhou

et al. 2015

Sci Rep

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Wasp stings have been arising to be a severe public health problem in China in recent years. However, molecular information about lethal or toxic factors in wasp venom is extremely lacking. In this study, we used two pyrosequencing platforms to analyze the transcriptome of Vespa velutina, the most common wasp species native in China. Besides the substantial amount of transcripts encoding for allergens usually regarded as the major lethal factor of wasp sting, a greater abundance of hemostasis-impairing toxins and neurotoxins in the venom of V. velutina were identified, implying that toxic reactions and allergic effects are envenoming strategy for the dangerous outcomes. The pattern of differentially expressed genes before and after venom extraction clearly indicates that the manifestation of V. velutina stings depends on subtle regulations in the metabolic pathway required for toxin recruitment. This comparative analysis offers timely clues for developing clinical treatments for wasp envenoming in China and around the world.

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Section: Resultsmentioning

confidence: 99%

Deciphering the Venomic Transcriptome of Killer-Wasp Vespa velutina

Liu

Chen

Zhou

et al. 2015

Sci Rep

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“…Halyxin from Agkistrodon/Gloydius halys brevicaudus binds to both FIX and FX, but not to other Gla-containing coagulation factors [87]. Factor X-binding protein (FX-bp) from Agkistrodon acutus binds with higher affinity to factor X than to factor IX, with the dissociation constants differing by a factor of about 7 [88,89]. In contrast, factor IX-binding protein (FIX-bp) from Echis carinatus leucogaster clearly prefers binding to factor IX over factor X, with a ratio of dissociation constants even approaching a value of 20 [81].…”

Section: Snake Venom-c-type Lectin-related Protein (Sv-clrps)/snacmentioning

confidence: 99%

Structurally Robust and Functionally Highly Versatile—C-Type Lectin (-Related) Proteins in Snake Venoms

Eble

2019

Toxins

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Snake venoms contain an astounding variety of different proteins. Among them are numerous C-type lectin family members, which are grouped into classical Ca2+- and sugar-binding lectins and the non-sugar-binding snake venom C-type lectin-related proteins (SV-CLRPs), also called snaclecs. Both groups share the robust C-type lectin domain (CTLD) fold but differ in a long loop, which either contributes to a sugar-binding site or is expanded into a loop-swapping heterodimerization domain between two CLRP subunits. Most C-type lectin (-related) proteins assemble in ordered supramolecular complexes with a high versatility of subunit numbers and geometric arrays. Similarly versatile is their ability to inhibit or block their target molecules as well as to agonistically stimulate or antagonistically blunt a cellular reaction triggered by their target receptor. By utilizing distinct interaction sites differentially, SV-CLRPs target a plethora of molecules, such as distinct coagulation factors and receptors of platelets and endothelial cells that are involved in hemostasis, thrombus formation, inflammation and hematogenous metastasis. Because of their robust structure and their high affinity towards their clinically relevant targets, SV-CLRPs are and will potentially be valuable prototypes to develop new diagnostic and therapeutic tools in medicine, provided that the molecular mechanisms underlying their versatility are disclosed.

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“…The function of FREPs in the snail hemolymph is analogous to that of calcium-dependent lectins [ 37 – 38 ]. The snake C-type lectin binds specifically with activated factor X, which functions as anticoagulation factor [ 39 ]. FREP1 may also play diverse roles in mosquito biology having similar functions as other FBG-containing proteins in other organisms, and this gene’s inactivation could thereby have directly impacted on various developmental processes.…”

Section: Discussionmentioning

confidence: 99%

CRISPR/Cas9 -mediated gene knockout of Anopheles gambiae FREP1 suppresses malaria parasite infection

et al. 2018

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Plasmodium relies on numerous agonists during its journey through the mosquito vector, and these agonists represent potent targets for transmission-blocking by either inhibiting or interfering with them pre- or post-transcriptionally. The recently developed CRISPR/Cas9-based genome editing tools for Anopheles mosquitoes provide new and promising opportunities for the study of agonist function and for developing malaria control strategies through gene deletion to achieve complete agonist inactivation. Here we have established a modified CRISPR/Cas9 gene editing procedure for the malaria vector Anopheles gambiae, and studied the effect of inactivating the fibrinogen-related protein 1 (FREP1) gene on the mosquito’s susceptibility to Plasmodium and on mosquito fitness. FREP1 knockout mutants developed into adult mosquitoes that showed profound suppression of infection with both human and rodent malaria parasites at the oocyst and sporozoite stages. FREP1 inactivation, however, resulted in fitness costs including a significantly lower blood-feeding propensity, fecundity and egg hatching rate, a retarded pupation time, and reduced longevity after a blood meal.

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Anticoagulation factor I, a snaclec (snake C-type lectin) from Agkistrodon acutus venom binds to FIX as well as FX: Ca2+ induced binding data

Cited by 22 publications

References 26 publications

Deciphering the Venomic Transcriptome of Killer-Wasp Vespa velutina

Deciphering the Venomic Transcriptome of Killer-Wasp Vespa velutina

Structurally Robust and Functionally Highly Versatile—C-Type Lectin (-Related) Proteins in Snake Venoms

CRISPR/Cas9 -mediated gene knockout of Anopheles gambiae FREP1 suppresses malaria parasite infection

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