Table 1.

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

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]