Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon actus venom

Ayako Tani, Tomohisa Ogawa, Takeru Nose, Nikolai N. Nikandrov, Masanobu Deshimaru, Takahito Chijiwa, Chun Chang Chang, Yasuyuki Fukumaki, Motonori Ohno

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

An anticoagulant protein named AaACP was isolated from Agkistrodon actus (hundred-pace snake of Taiwan, Viperidae) venom. AaACP inhibited the factor Xa-induced plasma coagulation in a concentration-dependent manner. Thus, AaACP seems to bind to factor Xa in prothrombinase complex. AaACP was composed of A and B chains linked by disulphide bond(s). The amino acid sequences of A and B chains of AaACP were analysed with a few residues unidentified which were complemented from the nucleotide sequences of their cDNAs. The A chain consisted of 129 amino acid residues and the B chain 123 amino acid residues. Their amino acid sequences were highly similar to those of A and B chains of a series of anticoagulant proteins which had been purified from the venoms of some Viperidae snakes. The A and B chains structurally belong to C-type lectin-like protein family of snake venom origin. Construction of phylogenetic tree of C-type lectins and C-type lectin-like proteins based on their amino acid sequences indicated that their A and B chains diverged before speciation of snake species. The comparison of the nucleotide sequences of the cDNAs encoding A and B chains of AaACP and of Trimeresurus flavoviridis (Viperidae) venom-gland factors IX/X-binding protein and factor IX-binding protein showed that the mature protein-coding region is much more variable than the signal peptide-coding domain and the 5′- and 3′-untranslated regions, being in contrast to the case of the ordinary isoprotein genes. The ratios of the numbers of nucleotide substitutions per nonsynonymous site (KA) and per synonymous site (KS) in the mature protein-coding region in the cDNA pairs were about three times greater than those for the ordinary isoprotein genes, suggesting that these genes have been evolving in an accelerated manner. Taking account of the functional diversities of venom-gland C-type lectins and C-type lectin-like proteins including factors IX and/or X-binding proteins, it can be said that their functional diversities have been acquired by accelerated evolution.

Original languageEnglish
Pages (from-to)803-813
Number of pages11
JournalToxicon
Volume40
Issue number6
DOIs
Publication statusPublished - May 6 2002

Fingerprint

C-Type Lectins
Molecular Evolution
Anticoagulants
Venoms
Factor IX
Snakes
Viperidae
Amino Acid Sequence
Carrier Proteins
Factor Xa
Amino Acids
Complementary DNA
Proteins
Open Reading Frames
Nucleotides
Genes
Trimeresurus
Agkistrodon
Factor X
Snake Venoms

All Science Journal Classification (ASJC) codes

  • Toxicology

Cite this

Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon actus venom. / Tani, Ayako; Ogawa, Tomohisa; Nose, Takeru; Nikandrov, Nikolai N.; Deshimaru, Masanobu; Chijiwa, Takahito; Chang, Chun Chang; Fukumaki, Yasuyuki; Ohno, Motonori.

In: Toxicon, Vol. 40, No. 6, 06.05.2002, p. 803-813.

Research output: Contribution to journalArticle

Tani, A, Ogawa, T, Nose, T, Nikandrov, NN, Deshimaru, M, Chijiwa, T, Chang, CC, Fukumaki, Y & Ohno, M 2002, 'Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon actus venom', Toxicon, vol. 40, no. 6, pp. 803-813. https://doi.org/10.1016/S0041-0101(01)00289-6
Tani, Ayako ; Ogawa, Tomohisa ; Nose, Takeru ; Nikandrov, Nikolai N. ; Deshimaru, Masanobu ; Chijiwa, Takahito ; Chang, Chun Chang ; Fukumaki, Yasuyuki ; Ohno, Motonori. / Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon actus venom. In: Toxicon. 2002 ; Vol. 40, No. 6. pp. 803-813.
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abstract = "An anticoagulant protein named AaACP was isolated from Agkistrodon actus (hundred-pace snake of Taiwan, Viperidae) venom. AaACP inhibited the factor Xa-induced plasma coagulation in a concentration-dependent manner. Thus, AaACP seems to bind to factor Xa in prothrombinase complex. AaACP was composed of A and B chains linked by disulphide bond(s). The amino acid sequences of A and B chains of AaACP were analysed with a few residues unidentified which were complemented from the nucleotide sequences of their cDNAs. The A chain consisted of 129 amino acid residues and the B chain 123 amino acid residues. Their amino acid sequences were highly similar to those of A and B chains of a series of anticoagulant proteins which had been purified from the venoms of some Viperidae snakes. The A and B chains structurally belong to C-type lectin-like protein family of snake venom origin. Construction of phylogenetic tree of C-type lectins and C-type lectin-like proteins based on their amino acid sequences indicated that their A and B chains diverged before speciation of snake species. The comparison of the nucleotide sequences of the cDNAs encoding A and B chains of AaACP and of Trimeresurus flavoviridis (Viperidae) venom-gland factors IX/X-binding protein and factor IX-binding protein showed that the mature protein-coding region is much more variable than the signal peptide-coding domain and the 5′- and 3′-untranslated regions, being in contrast to the case of the ordinary isoprotein genes. The ratios of the numbers of nucleotide substitutions per nonsynonymous site (KA) and per synonymous site (KS) in the mature protein-coding region in the cDNA pairs were about three times greater than those for the ordinary isoprotein genes, suggesting that these genes have been evolving in an accelerated manner. Taking account of the functional diversities of venom-gland C-type lectins and C-type lectin-like proteins including factors IX and/or X-binding proteins, it can be said that their functional diversities have been acquired by accelerated evolution.",
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