Fig 1.
Relative distribution of the sequences found in the V. intrepidus, V. mexicanus, V. subcristatus and V. punctatus libraries with respect to the putative function of their encoded peptides.
Fig 2.
Putative toxin sequences derived from the precursors found in the Vaejovis libraries.
The peptide length (aa) always refers to the confirmed (when the peptide has been isolated from the venom) or software-predicted mature peptides. The identity (%I) is always relative to the first sequence of the alignment, and considers only the mature peptide regions. When present, the signal peptides are shown underlined and the propeptides are in italics and bold. The conserved cysteine arrangement typical of each family is highlighted. A) Sequence alignment of the putative sodium channel toxins. The precursor sequences of ViNaTx1 from V. intrepidus, VpNaTx1 and VpNaTx2 from V. punctatus, VsNaTx1 and VsNaTx2 from V. subcristatus, and VmNaTx1 from V. mexicanus are compared to the known sodium channel-specific ß-toxins Birtoxin (UniProt:P58752), Ikitoxin (UniProt:P0C1B8) and Altitoxin (UniProt:P0C1B5) from Parabuthus transvaalicus. B) Comparative alignments of the sequences found that belong to the two families of potassium channel-specific α-toxins. First, the precursor sequences of the six-cysteines α-toxins ViKTx1 form V. intrepidus and VpKTx4 from V. punctatus aligned to KTX-2 (Kaliotoxin-2, UniProt:P45696) from Androctonus australis and TdK1 (UniProt:P59925) from Tityus discrepans as references. Second, the precursor sequences coding for the toxins belonging to the family of the eight-cysteines α-toxins VmKTx1 from V. mexicanus and VpKTx3 from V. punctatus, aligned to Vm24 (UniProt:P0DJ31) from V. mexicanus and HgeTx1 (UniProt:P84864) from Hadrurus gertschi as references. C) The precursor sequence of VmKTx2 from V. mexicanus compared to the precursor sequence of HelaTx1 (UniProt:P0DJ41) from Heterometrus laoticus and κ-HfTx1 (UniProt:P82850) plus κ-HfTx2 (UniProt:P82851) from Heterometrus fulvipes, all belonging to the family of potassium channel-specific κ-toxins. D) The scorpine-like sequences ViScplp1–3 from V. intrepidus, VmScplp1–3 from V. mexicanus, VpScplp1 from V. punctatus, and the partial sequences of VsScplp1–2 from V. subcristatus are aligned. For comparison, the sequences of scorpine (UniProt:P56972) from P. imperator, HgeScplp1 (UniProt:Q0GY40) and HgeScplp2 (UniProt:P0C8W5) from H. gertschi are also included in the alignment.
Fig 3.
Putative calcium channel toxins found in Vaejovis.
The peptide length (aa) always refers to the confirmed (when the peptide has been isolated from the venom) or software-predicted mature peptides. The given percentages of identity (%I) correspond to the mature peptides only, and refer to the first sequence. The predicted signal peptides are shown underlined, the propeptides in italics and bold. A) Sequence alignment of the three-disulfide-bridged putative calcinsVpCaTx1 from V. punctatus and ViCaTx1 from V. intrepidus with imperatoxin (UniProt:P59868) from P. imperator, maurocalcin (UniProt:P60254) from S. maurus palmatus, opicalcin-1 (UniProt:P60252) and opicalcin-2 (UniProt:P60253) from Opistophthalmus carinatus, UyCaTx20 (Calcium-channel toxin-like 20, UniProt:AGA82762) from U. yaschenkoi and hadrucalcin (UniProt:B8QG00) from H. gertschi. B) The precursors of the two-disulfide-bridged putative calcins VmCaTx1 and VmCaTx2 from V. mexicanus and VpCaTx2 from V. punctatus, are compared to previously reported sequences of their kind: LaIT1 (UniProt:P0C5F2) from L. australasiae, and U1-LITX-Lw1a (UniProt:P0DJ08) from L. waigiensis.
Fig 4.
Sequence alignment of the La1-like peptides found in the Vaejovis libraries.
The precursor sequences of VmLa1lp1 from V. mexicanus, VsLa1lp1 from V. subcristatus and VpLa1lp1 from V. punctatus are aligned to the previously reported precursors of La1lp-15 (UniProt:AGA82761) from U. yaschenkoi, HsTx1 (UniProt:K7WMX6) from H. spinifer, VenPepPc (UniProt:H2CYP1) from P. cavimanus, and the mature La1 (UniProt:P0C5F3) from L. australasiae. The peptide length (aa) always refers to the confirmed (when the peptide has been isolated from the venom) or software-predicted mature peptides. The given percentages of identity (%I) correspond to the mature peptides only, and are relative to the first sequence. The predicted signal peptides are shown underlined, the propeptides in italics and bold.
Fig 5.
Multiple alignment of the sequences corresponding to the peptidic precursors belonging to the NDBP-4 subfamily found in the Vaejovis libraries.
Separate alignments are shown for the signal peptides, the mature peptides and the propeptides, with the number of residues (aa) and the percentage of identity (%I) indicated for each segment. For the mature peptide the prominent sequence features are highlighted with colors and in bold typeface (see text) and the theoretical molecular weight (MW) and net charge (CHG) are also given. In the propeptide region, the post-translational cleavage and amidation substrate sequence is underlined. For comparison, the sequences of IsCT (UniProt:Q8MMJ7.1), IsCT2 (UniProt:Q8MTX2.1), UyCT1 (UniProt:L0GCV8.1), UyCT3 (UniProt:L0GCI6.1), UyCT5 (UniProt:L0GAZ8.1), Hp1090 (UniProt:P0DJ02.1), Pantinin 1 (UniProt:R4JNJ5), Pantinin 2 (UniProt:R4JQZ0), Pantinin 3 (UniProt:R4JJN6), Meucin-13 (UniProt:E4VP07.1), BmKn2(UniProt:Q6JQN2.1) and StCT2 (UniProt:P0DJO4.1) were used.
Fig 6.
Multiple alignment of the sequences corresponding to the precursors of the peptides belonging to the NDBP-2 subfamily found in the Vaejovis libraries.
The peptide length (aa) refers to the confirmed (when the peptide has been isolated from the venom) or software-predicted mature peptides. The identity (%I) is relative to the first sequence of the alignment, and considers only the mature peptide region. When present, the signal peptides are shown underlined and the propeptides are in italics and bold typeface. The theoretical molecular weight (MW) and net charge (CHG) are also given for each mature peptide. Fully conserved residues are highlighted with color and bold. For comparison purposes, the sequences of vejovine (UniProt:ADZ24463.1), hadrurin (UniProt:P82656.1), opistoporin-1 (UniProt:P83313.2), opistoporin-2 (UniProt:P83314.1), pandinin1 (UniProt:P83239.1), parabutoporin (UniProt:P83312.1), and BmKbpp (UniProt:Q9Y0X4.1) were used.