Recombinant Echis disintegrins reveal distinct inhibitory profiles on platelet aggregation and endothelial…

Abstract

Disintegrins are snake venom toxins that bind integrins and modulate platelet aggregation and cell migration. Isolation from venom often yields insufficient quantities for comprehensive study, making recombinant expression essential for detailed toxin characterisation. Here, we produced and characterised four disintegrins from Echis coloratus and Echis ocellatus in Escherichia coli. These homologous proteins contain distinct integrin-binding motifs: EcDis_RGD, EoDis_RGD, EcDis_KGD, and EcDis_VGD. Functional activities were evaluated using human platelet aggregation and endothelial cell scratch wound-healing assays. RGD-containing disintegrins exhibited the strongest inhibition of platelet aggregation, with EcDis_RGD showing the highest potency. The EcDis_KGD disintegrin inhibited platelet aggregation less potently, whereas EcDis_VGD showed no detectable activity in our assays. In endothelial cells, EcDis_RGD disintegrin markedly impaired cell migration, while EoDis_RGD displayed weaker anti-migratory activity. Neither KGD- nor VGD-containing disintegrins significantly affected wound closure. EoDis_RGD exhibited similar antiplatelet activity to the native, venom-purified disintegrin ocellatusin, validating our recombinant expression strategy. However, the corresponding PII-SVMP preparation displayed reduced inhibitory activity, consistent with incomplete generation of fully mature disintegrins species. Our findings demonstrate the importance of both integrin-binding motif identity and surrounding sequence context in determining disintegrin function, and support further use of recombinant toxins in toxinology and as therapeutic lead molecules.

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BibTeX RIS

BibTeX

@misc{cardoso2026recombinant,
  title = {{Recombinant Echis disintegrins reveal distinct inhibitory profiles on platelet aggregation and endothelial cell migration}},
  author = {I. A. Cardoso and S. Hall and T. Crasset and M. C. Wilkinson and A. Robinson and B. Rand and D. Shen and C. Webb and R. Stenner and D. Waterhouse and I. Hers and R. Vincentelli and I. Berger and N. R. Casewell and L. Quinton and A. Poole and C. Schaffitzel},
  howpublished = {bioRxiv},
  year = {2026},
  month = sep,
  doi = {10.64898/2026.09.05.749579},
  url = {https://www.biorxiv.org/content/10.64898/2026.09.05.749579v1},
  note = {CC BY},
}

RIS

TY  - UNPB
TI  - Recombinant Echis disintegrins reveal distinct inhibitory profiles on platelet aggregation and endothelial cell migration
AU  - I. A. Cardoso
AU  - S. Hall
AU  - T. Crasset
AU  - M. C. Wilkinson
AU  - A. Robinson
AU  - B. Rand
AU  - D. Shen
AU  - C. Webb
AU  - R. Stenner
AU  - D. Waterhouse
AU  - I. Hers
AU  - R. Vincentelli
AU  - I. Berger
AU  - N. R. Casewell
AU  - L. Quinton
AU  - A. Poole
AU  - C. Schaffitzel
PY  - 2026
DA  - 2026/09/05
PB  - bioRxiv
DO  - 10.64898/2026.09.05.749579
UR  - https://www.biorxiv.org/content/10.64898/2026.09.05.749579v1
AB  - Disintegrins are snake venom toxins that bind integrins and modulate platelet aggregation and cell migration. Isolation from venom often yields insufficient quantities for comprehensive study, making recombinant expression essential for detailed toxin characterisation. Here, we produced and characterised four disintegrins from Echis coloratus and Echis ocellatus in Escherichia coli. These homologous proteins contain distinct integrin-binding motifs: EcDis_RGD, EoDis_RGD, EcDis_KGD, and EcDis_VGD. Functional activities were evaluated using human platelet aggregation and endothelial cell scratch wound-healing assays. RGD-containing disintegrins exhibited the strongest inhibition of platelet aggregation, with EcDis_RGD showing the highest potency. The EcDis_KGD disintegrin inhibited platelet aggregation less potently, whereas EcDis_VGD showed no detectable activity in our assays. In endothelial cells, EcDis_RGD disintegrin markedly impaired cell migration, while EoDis_RGD displayed weaker anti-migratory activity. Neither KGD- nor VGD-containing disintegrins significantly affected wound closure. EoDis_RGD exhibited similar antiplatelet activity to the native, venom-purified disintegrin ocellatusin, validating our recombinant expression strategy. However, the corresponding PII-SVMP preparation displayed reduced inhibitory activity, consistent with incomplete generation of fully mature disintegrins species. Our findings demonstrate the importance of both integrin-binding motif identity and surrounding sequence context in determining disintegrin function, and support further use of recombinant toxins in toxinology and as therapeutic lead molecules.
ER  -

Abstract

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