Evidence map›Paper›PMID 39219422›Full record

ArticleProtein and peptide letters2024

Insights into the Evolutionary Dynamics: Characterization of Disintegrin and Metalloproteinase Proteins in the Venom Gland Transcriptome of the

Abbas Rami, Benjamin Damizadeh, Mahdi Behdani, Fatemeh Kazemi-Lomedasht

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Article in Protein and peptide letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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2 citing papers in PubMed.

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4 authors.

Abbas RamiVenom and Biotherapeutics Molecules Laboratory, Department of Biochemistry, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Benjamin DamizadehVenom and Biotherapeutics Molecules Laboratory, Department of Biochemistry, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Mahdi BehdaniVenom and Biotherapeutics Molecules Laboratory, Department of Biochemistry, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Fatemeh Kazemi-LomedashtVenom and Biotherapeutics Molecules Laboratory, Department of Biochemistry, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.

Funding

Pasteur Institute of Iran
6 · The paper itself

Abstract

backgroundThe Disintegrin and Metalloproteinase (ADAM) family, also known as the metalloproteinase/disintegrin/cysteine-rich (MDC) proteins, includes both secreted and transmembrane molecules involved in critical biological processes, such as cell migration, adhesion, and signaling. This study aimed to investigate the evolutionary relationships and structural characteristics of disintegrin and metalloproteinase proteins identified in the venom gland transcriptome of the scorpion Hemiscorpius lepturus.

methodsUsing bioinformatics tools, we analyzed the open reading frame, conserved motifs, and primary, secondary, and tertiary structures of these proteins. Five proteins, named HLDisMet1, HLDisMet2, HLDisMet3, HLDisMet4, and HLDisMet5, were identified. Their predicted 3-D structures were within normal ranges (Z-score between -4 to -9).

resultsPhylogenetic analysis revealed that HLDisMet1 shares similarities with proteins from various spider species

conclusionThese findings highlight the significant similarities between HLDisMet proteins and those found in other venomous species, suggesting a complex and diverse evolutionary pathway for venom components. The cross-species conservation observed may indicate a convergent evolutionary strategy, where different species independently develop similar venom components to adapt to similar ecological niches or prey types. This study highlights the evolutionary significance of venom diversification and its potential applications in understanding venom biology across different species.

Indexed as

DisintegrinsEvolution, MolecularMetalloproteasesPhylogenyScorpionsTranscriptomeAmino Acid SequenceAnimalsAnimals, PoisonousArthropod ProteinsScorpion VenomsArthropod ProteinsDisintegrinsMetalloproteasesScorpion VenomsdisintegrinHemiscorpius lepturusmetalloprotease.phylogenetictranscriptomevenom

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