Amino acid sequence of neurotoxin II from <i>Naja naja oxiana</i> venom

Grishin, Eugene V.; Sukhikh, A.P.; Slobodyan, L.N.; Ovchinnikov, Yu.A.; Сорокин, В. М.

doi:10.1016/0014-5793(73)80340-0

Cited by 35 publications

(12 citation statements)

References 12 publications

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“…The variant amino acid residues of the P. textilis neurotoxins are highlighted and asterisked. PT, Pseudonaja textilis (this study); Nmm III, Naja mossambica mossambica [29]; Nk c‐6, Naja kaouthia [30]; Nns 1 and Nns 4, Naja naja sputatrix [17] ; Nnv δ, Naja nivea [31]; Nha α, Naja haje annulifera [32]; Nm D, Naja melanoleuca [33]; Nhh 6, Naja haje haje [34]; Tx α, Naja nigricollis [35]; Nnp, Naja naja philippinensis [36]; Nno II, Naja naja oxiana [37]; Ea, Laticauda semifasciata [38]; Lc d, Laticauda colubrina [39]; Taipan tx 1 and Taipan tx 2, Oxyuranus scutellatus scutellatus [12]; Aa c, Acanthophis antarcticus [10]; Pa a, Pseudechis australis [11]; Al d and Al b, Aipysurus laevis [40]; Lh, Lapemis hardwickii [41]; Ap a, Acalyptophis peronii [42]; As a, Astrotia stokesii [43].…”

Section: Resultsmentioning

confidence: 99%

Postsynaptic short‐chain neurotoxins from Pseudonaja textilis

Gong

Armugam

Jeyaseelan

1999

European Journal of Biochemistry

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Two lethal proteins, which specifically bind to the nAChR from Torpedo californica, were isolated from the venom of Pseudonaja textilis, the common brown snake from Australia. The isolated proteins have masses of 6236 and 6345 Da and are structurally related to short-chain neurotoxins from other elapids. Six cDNAs encoding isoforms of related neurotoxins were cloned using the RT-PCR of the venom gland mRNAs. The sequences of the corresponding proteins consist of 57±58 amino acid residues and display several unique features when compared with all known short-chain neurotoxins. Accordingly, they grouped separately in phylogenetic analysis. The six cDNAs were expressed in Escherichia coli and the recombinant proteins were characterized. They have similar masses and display similar toxicities and binding constants to the nAChR as the native toxins isolated from the venom. Thus, a new group of short-chain postsynaptic neurotoxins from the venom of an Australian elapid has been characterized.

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Section: Resultsmentioning

confidence: 99%

Postsynaptic short‐chain neurotoxins from Pseudonaja textilis

Gong

Armugam

Jeyaseelan

1999

European Journal of Biochemistry

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“…nigricollis toxin a', a toxin which differs from toxin a by two single residues at positions 1 and 2, and (3) N.n. oxiana toxin I1 which differs from N. nigricollis toxin a by eight residues at positions 18, 28, 30, 45, 50, 51, 56, and 59 (Grishin et al, 1973).…”

Section: Resultsmentioning

confidence: 99%

Neutralizing monoclonal antibody specific for Naja nigricollis toxin .alpha.: preparation, characterization and localization of the antigenic binding site

Boulain¹,

Ménèz²,

Couderc³

et al. 1982

Biochemistry

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One homogeneous population of high-affinity monoclonal antibodies (KD = 0.35 nM) specific for Naja nigricollis toxin alpha has been produced. It neutralizes the biological activity of the toxin under both the vivo and in vitro conditions. The molecular zone of the toxin to which the antibody binds has been precisely defined on the basis of cross-reaction experiments using five derivative of toxin alpha monomodified at a single amino group and two naturally occurring homologous toxins. The epitope is located at the base of the first beta-sheet loop of the toxin, involving the two positive charges at the N-terminal position and lysine-15 proline-18, and probably threonine-16. It is shown that this region is topographically distinct from the "toxic" site of toxin alpha. Several possibilities are offered to explain the mechanisms(s) of specific neutralization.

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“…It is a short single-chain polypeptide consisting of 61 amino acid residues, cross-linked with four disulfide bonds (Grishin et al, 1973). NtII is a typical representative of a family of homologous neurotoxins, classified either as short toxins with four disulfide bonds or long neurotoxins with five disulfide bonds (for reviews, see Endo and Tamiya, 1987 ; Karlsson, 1979).…”

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confidence: 99%

Two‐dimensional ¹H‐NMR study of the spatial structure of neurotoxin II from Naja naja oxiana

Golovanov

Lomize

Arseniev

et al. 1993

European Journal of Biochemistry

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The spatial structure of neurotoxin I1 from the venom of the central Asian cobra Nuju nuju oxiunu was determined by two-dimensional 'H-NMR techniques and computational analysis. Nearly complete proton resonance assignments for 61 amino acid residues have been made using twodimensional (2D) homonuclear total correlated spectroscopy, 2D homonuclear double-quantum-filtered correlated spectroscopy and 2D homonuclear NOE spectroscopy (NOESY) experiments. The cross-peak volumes in NOESY spectra spin-spin coupling constants of vicinal protons NH-CaH and CaH-CpH and the observation of slow deuterium exchange of amide protons were used to define local structure and a set of constraints for distance geometry program DIANA. The average rootmean-square deviations are 53 pm for backbone heavy atoms and 118 pm for all heavy atoms of 19 final neurotoxin I1 conformations. The spatial structure is characterized by a short double-stranded (residues 1-5 and 13-17) and a triple-stranded (residues 22-30, 33-41 and 50-54) antiparallel /I-sheets.

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Amino acid sequence of neurotoxin II from Naja naja oxiana venom

Cited by 35 publications

References 12 publications

Postsynaptic short‐chain neurotoxins from Pseudonaja textilis

Postsynaptic short‐chain neurotoxins from Pseudonaja textilis

Neutralizing monoclonal antibody specific for Naja nigricollis toxin .alpha.: preparation, characterization and localization of the antigenic binding site

Two‐dimensional ¹H‐NMR study of the spatial structure of neurotoxin II from Naja naja oxiana

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Amino acid sequence of neurotoxin II from Naja naja oxiana venom

Cited by 35 publications

References 12 publications

Postsynaptic short‐chain neurotoxins from Pseudonaja textilis

Postsynaptic short‐chain neurotoxins from Pseudonaja textilis

Neutralizing monoclonal antibody specific for Naja nigricollis toxin .alpha.: preparation, characterization and localization of the antigenic binding site

Two‐dimensional 1H‐NMR study of the spatial structure of neurotoxin II from Naja naja oxiana

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Two‐dimensional ¹H‐NMR study of the spatial structure of neurotoxin II from Naja naja oxiana