Table 1.
General characterization of components from V. berus berus venom.
| Component name | Mass (kDa) | pI | Function/substrates | References |
|---|---|---|---|---|
| Enzymes | ||||
| Phosphodiesterase | 100 | 4.0; 6.3 | Hydrolysis of nucleic acids and nucleotides, depletion of cyclic, di- and trinucleotides | Siigur et al. (1979) |
| 5′-nucleotidase | 100 | 5.6 | Hydrolysis of 5′-nucleotides, nucleoside liberation | Siigur et al., 1979; Aird, 2002 |
| Phosphomonoesterase | 150 | nd | Hydrolysis of phosphomonoester bonds | Siigur et al., 1979; Rael, 1998 |
| Hyaluronidase | 73 | nd | Hydrolysis of interstitial hyaluronan, diffusion of venom components | Siigur et al., 1979; Kudo and Tu (2001) |
| L-amino acid oxidase (homodimer) | 57.7 126 |
4.8 | Oxidative deamination of L-amino acids, induction of apoptosis, cell damage | Siigur et al., (1979), Samel et al. (2006) |
| Metalloproteinases | ||||
| Haemorrhagic metallo-proteinase (HMP) | 56.3 | 6.3 | Hydrolysis of proteins, haemorrhage, myonecrosis prey pre-digestion | Samel and Siigur (1990) |
| VBFXAE | 38 | 3.5–4.5 | Factor X activator, oxidized insulin B chain | Samel and Siigur (1995) |
| VBFXAEI | 95.5 | nd | Factor X activator, oxidized insulin B chain | Siigur et al. (2002) |
| VBFXAEII | 126 | nd | Factor X activator, oxidized insulin B chain, asocasein, gelatin, fibrinogen | Samel et al. (2003) |
| Serine proteinases | ||||
| Arginine esterase E1 | 38.5 | 4.0–4.6 | Hydrolysis of BAEE, TAME, Pro-Phe-Arg-MCA | Samel et al. (1987) |
| Arginine esterase EII | 41.0 | 3.3–3.9 | Hydrolysis of BAEE, TAME, Pro-Phe-Arg-MCA, kinin-releasing activity | Samel et al. (1987) |
| Phospholipase A2 (France) | 13.4 | 9.2 | Hydrolysis of 2-acyl groups in 3-sn- phospho-glycerides, lipid membrane damage | Boffa et al. (1976) |
| Phospholipase A2 (Russia) | 13.824 | 9.3 | Hydrolysis of 2-acyl groups in 3-sn- phospho-glycerides, lipid membrane damage | Križaj et al., 1993 |
| Phospholipase A2 (Hungary) | 13.548–14.340a | nd |
Hydrolysis of 2-acyl groups in 3-sn- phospho-glycerides, lipid membrane damage | Malina et al. (2017) |
| Phospholipase A2(Austria) | 13.550–14.2832a | nd |
Hydrolysis of 2-acyl groups in 3-sn- phospho- glycerides, lipid membrane damage | Malina et al. (2017) |
| Phospholipase A2 (France) | 13.824b | nd |
Hydrolysis of 2-acyl groups in 3-sn- phospho-glycerides, lipid membrane damage, anticoagulant | Guillemin et al. (2003) |
| Nonenzymatic proteins/peptides | ||||
| CRISP | 24.555 | nd | Possibly blocks cNTP gated channels, Induces hypothermia, prey immobilization | Ramazanova et al. (2009); Yamazaki and Morita, 2004 |
| Nerve growth factor | 35 | 9.1–9.7 | Promotes nerve fiber growth, differentiation of pheochromocytoma PC-12 cells | Siigur et al. (1986) |
| Dimeric disintegrin VB7 | 13.969 | nd | Inhibits binding integrins to receptors, blocks the function of integrin α5β1 | Calvete et al. (2003) |
| Trypsin inhibitor | 7.3 | >10 | Inhibits trypsin Ki = 6.7 × 10−11 | Siĭgur et al., 1988 |
| Chymotrypsin inhibitor | 7.3 | 9.9 | Inhibits chymotrypsin Ki = 4.6 × 10−10 | Siĭgur et al., 1988 |
nd – not detected.
a
- 4–7 isoforms detected by MALDI-TOF MS in Hungarian V. b. berus venom; Austrian venom showed 5 isoforms with molecular masses between 13.550 and 14.2832.
b
- The molecular mass of anticoagulant PLA2 has been detected by amino acid sequence of the V. b. berus protein that was identical with that of the PLA2 purified from V. b. berus venom (Križaj et al., 1993).