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Journals / Türk Biyokimya Dergisi / 2018 / Cilt: 43 - Sayı: 6

Molecular cloning and in silico characterization of two alpha-like neurotoxins and one metalloproteinase from the maxilllipeds of the centipede Scolopendra subspinipes mutilans

İki alfa benzeri nörotoksinlerin ve bir adet metalloproteinazın silico karakterizasyonunda kırkayak klonlanması ve kırkayak ekstraktlarının maksilet spp.

Yang LIU
Xichao XIA
Xinhua ZHENG
Zhiguo CHEN
Shipeng XUE
Fuan WANG
Junfeng ZHANG
Jianxin HUANG
Xiaozhu YU
Zhaofei CHENG
Pages
651–661
Publication Date
2022-11-05
DOI
—
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⚡ TL;DR(Too Long; Didn't Read)

Phylogenetic analysis revealed earlydivergence and independent evolution of SsuTA1 andSsuTA2 from other α-neurotoxins.Conclusion: The results suggested that centipede S. subspinipesmutilans is an ancient member of venomousarthropods, but its venom exhibits novel scenario.

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Objective & Hypothesis:Aims: In order to shed light of characterizations of centipedeScolopendra subspinipes mutilans venom, a twonovel full-lengths of alpha-like-neurotoxin and one metalloproteinasecDNAs derived from the maxilllipeds RNAof centipede S. subspinipes mutilans were isolated, and,respectively, named as SsuTA1, SsuTA2 and SsuMPs.Materials and methods: The SsuTA1, SsuTA2 and SsuMPswere cloned from the S. subspinipes mutilans using therapid amplification of cDNA ends methods.Results: In the current study, SsuTA1 and SsuTA2 were,respectively, composed of 82 amino acid residues and106 amino acid residues.
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Key Findings & Data:Deduced protein sequence ofSsuTA1 shared high homology with that of SsuTA2, onemajor difference was the C-terminal 24-residue extensionin SsuTA2.
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Conclusion & Impact:Phylogenetic analysis revealed earlydivergence and independent evolution of SsuTA1 andSsuTA2 from other α-neurotoxins.Conclusion: The results suggested that centipede S. subspinipesmutilans is an ancient member of venomousarthropods, but its venom exhibits novel scenario.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

Aims: In order to shed light of characterizations of centipedeScolopendra subspinipes mutilans venom, a twonovel full-lengths of alpha-like-neurotoxin and one metalloproteinasecDNAs derived from the maxilllipeds RNAof centipede S. subspinipes mutilans were isolated, and,respectively, named as SsuTA1, SsuTA2 and SsuMPs.Materials and methods: The SsuTA1, SsuTA2 and SsuMPswere cloned from the S. subspinipes mutilans using therapid amplification of cDNA ends methods.Results: In the current study, SsuTA1 and SsuTA2 were,respectively, composed of 82 amino acid residues and106 amino acid residues. Deduced protein sequence ofSsuTA1 shared high homology with that of SsuTA2, onemajor difference was the C-terminal 24-residue extensionin SsuTA2. An abundance of cysteine residues andseveral adjacent beta-sheets were observed in SsuTA1and SsuTA2. SsuMPs had 594 amino acid residues containingwith a molecular mass of 68.29 kDa. The primarysequence analysis indicated that the SsuMPs contains azinc-bindingmotif (HEIGHSLGLAHS) and methionineturnmotif (YIM). Phylogenetic analysis revealed earlydivergence and independent evolution of SsuTA1 andSsuTA2 from other α-neurotoxins.Conclusion: The results suggested that centipede S. subspinipesmutilans is an ancient member of venomousarthropods, but its venom exhibits novel scenario.

Özet

Amaçlar: Kırkayak çağı scolopendra subspinipes mutilans venomunun karakterizasyonlarının ışığında, iki adet tam uzunlukta alfa-benzeri-nörotoksin ve santrifüj S. subspinipes mutilansının maksilllipre RNA’sından türetilmiş bir metalloproteinaz cDNA’sı izole edildi ve sırasıyla SsuTA1, SsuTA2 ve SsuMPs. Gereç ve Yöntemler: SsuTA1, SsuTA2 ve SsuMP’ler, S. subspinipes mutilanslarından cDNA uçlarının hızlı amplifikasyonu kullanılarak klonlanmıştır. Bulgular: Mevcut çalışmada SsuTA1 ve SsuTA2 sırasıyla 82 amino asit artığı ve 106 amino asit kalıntısından oluşmaktadır. SsuTA1’in indirgenmiş protein sekansı, SsuTA2’ninki ile yüksek benzerlik paylaştı, önemli bir fark SsuTA2’deki C-terminali 24-artık uzantısıydı. SsuTA1 ve SsuTA2’de çok sayıda sistein kalıntısı ve birkaç bitişik p-tabaka gözlenmiştir. SsuMPs, 68.29 kDa’lık bir moleküler kütle içeren 594 amino asit tortusuna sahipti. Birincil dizi analizi SsuMP’lerin bir çinko bağlayıcı motif (HEIGHSLGLAHS) ve metiyonin dönüş motifi (YIM) içerdiğini göstermiştir. Filogenetik analizler SsuTA1 ve SsuTA2’nin diğer α-nörotoksinlerden erken ayrışmasını ve bağımsız evrimini ortaya çıkardı. Sonuç: Sonuçlar sentipede S. subspinipes mutilans’ın eski bir zehirli artropod üyesi olduğunu, ancak zehirinin yeni bir senaryo sergilediğini ortaya koymuştur.

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Cite This Article

LIU, Y., XIA, X., ZHENG, X., CHEN, Z., XUE, S., WANG, F., ZHANG, J., HUANG, J., YU, X., CHENG, Z. (2022). Molecular cloning and in silico characterization of two alpha-like neurotoxins and one metalloproteinase from the maxilllipeds of the centipede Scolopendra subspinipes mutilans. Türk Biyokimya Dergisi, Cilt: 43 - Sayı: 6, 651–661. https://ajindex.com/articles/620964

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