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Table 1 Pre-identification of proteins from N. fodiens venom and S. araneus saliva based on tandem mass spectrometry analysis

From: Evaluation of the physiological activity of venom from the Eurasian water shrew Neomys fodiens

Sample Protein name Species Accession Matched peptides Protein sequence coverage [%] Ion score m/z Identified peptides Possible toxic activity
Neomys fodiens
extract calmodulin-like protein Mus musculus Q9D6P8 25 37 64 955 K.EAFSLFDK.D Acute and chronic effects on cardiac function by regulation of the intracellular Ca2+ concentration [38]
37 4086 R.SLGQNPTEAELQGMVNEIDKDGNGTVDFPEFLTMMSR.K + Oxidation (M)
57 4102 R.SLGQNPTEAELQGMVNEIDKDGNGTVDFPEFLTMMSR.K + 2 Oxidation (M)
97 1351 K.MKDTDSEEEIR.E
81 1367 K.MKDTDSEEEIR.E + Oxidation (M)
65 1092 K.DTDSEEEIR.E
hyaluronidase-2 Bos taurus Q8SQG8 14 8 24 980 HKMPLDPK Facilitates spread of other venom proteins [36, 42]
thymosin β-10 Bos taurus P21752 11 11 22 862 KTETQEK Improves cardiac function, promotes vascularization and contractility in heart tissue [52, 53]
β-nerve growth factor Mus musculus P01139 8 6 68 1153 K.LQHSLDTALR.R Unknown [36, 54]
37 764 R.RLHSPR.V
fraction no. 5 cystatin-C Rattus norvegicus P14841 14 8 28 1207 GTHTLTKSSCK Inhibits cysteine proteases, failures in biological mechanisms controlling protease activities may led to many diseases such as neuro-degeneration or cardiovascular diseases [39]
coagulation factor VIII Sus scrofa P12263 18 5 22 1427 ISALGKSAAGPLASGK Acts as an anti-hemophilic factor [55]
lysozyme C-1 Sus scrofa P12067 6 8 24 930 YWCNDGK Involved in an antimicrobial defence [10, 56]
fraction no. 31 hyaluronidase PH-20 Myotis brandtii gi|521028001 14 11 47 1152 KDIEFYIPK See above
fraction no. 34 chain E, leech-derived tryptase inhibitor Trypsin Complex Sus scrofa gi|3318722 48 21 177 2210 R.LGEHNIDVLEGNEQFINAAK.I Prolongs the blood clotting time by thrombin and trypsin inhibition [57]
115 2282 K.IITHPNFNGNTLDNDIMLIK.L
93 1045 K.LSSPATLNSR.V
77 841 R.VATVSLPR.S
108 1515 K.SSGSSYPSLLQCLK.A
98 1051 K.APVLSDSSCK.S
fraction no. 39 coagulation factor VIII Sus scrofa P12263 19 7 23 1427 ISALGKSAAGPLASGK See above
lactyloglutathione lyase Rattus norvegicus Q6P7Q4 17 25 78 1264 K.DFLLQQTMLR.I Involved in inflammation [58]
54 1028 K.KSLDFYTR.V
44 900 K.SLDFYTR.V
57 976 K.RFEELGVK.F
65 2288 K.GLAFVQDPDGYWIEILNPNK.M
fraction no. 40 phospholipase A2 Oryctolagus cuniculus P14422 6 6 27 1002 FAKFLSYK Exhibits cardio-, myo- and neurotoxicity, as well as pro- and anticoagulant effects [40, 41]
calmodulin-like protein Mus musculus Q9D6P8 14 5 25 1367 MKDTDSEEEIR See above
Sorex araneus
extract thymosin β-10 Rattus norvegicus P63312 7 34 56 862 K.KTETQEK.N See above
37 734 K.TETQEK.N
48 875 K.ETIEQEK.R
77 1031 K.ETIEQEKR.S
coagulation factor XI Mus musculus Q91Y47 10 11 21 846 MICAGYK Involved in blood clotting [59]
fraction no. 23 thymosin β-4 Oryctolagus cuniculus P34032 69 88 46 1245 M.ADKPDMAEIEK.F See thymosin β-10
47 1652 M.ADKPDMAEIEKFDK.S + Oxidation (M)
34 862 K.KTETQEK.N
38 734 K.TETQEK.N
83 1371 K.TETQEKNPLPSK.E
89 1512 K.NPLPSKETIEQEK.Q
43 875 K.ETIEQEK.Q
72 1348 K.ETIEQEKQAGES.-
cystatin-C Rattus norvegicus P14841 14 8 27 1207 GTHTLTKSSCK See above
fraction no. 28 cystatin-C Rattus norvegicus P14841 11 6 43 1207 K.GTHTLTKSSCK.N See above
lysozyme C-1 Sus scrofa P12067 10 19 22 787 AWVAWR See above
kallikrein 1-related peptidase b24 Mus musculus Q61754 10 6 33 1204 K.DKSNDLMLLR.L Might act as an inflammatory agent (increasing vascular permeability and lowering blood pressure) [8, 9]
fraction no.29 cystatin-C Rattus norvegicus P14841 14 8 27 1207 GTHTLTKSSCK See above
α-amylase 1 Mus musculus P00687 8 11 25 780 DYVRTK Unknown
β-defensin 7 Mus musculus Q91V70 8 11 24 760 FQIPEK Exhibits a significant myo- and neurotoxic activity, modifying voltage-sensitive Na+ channels, resulting in a potent analgesic effect [36]