## 2 Results
### Comparison of Identified Venom-Derived Polypeptides
#### 2.2.5 Hyaluronidase  
This protein was identified from gel band 7 (with peptide fragments covering 3% of the full sequence) and from the in-solution proteomic analysis protein 16 (with peptide fragments covering 16% of the full sequence). The peptides detected in the venom proteome corresponded to the translated protein product of the _D. quadriceps_ venom gland transcript contig385_B2-2 (1882 bp, Figure S5), which codes for the venom hyaluronidase that belongs to the family of glycosyl hydrolases 56 in the Hypmenoptera database. Such sequence is identical to the predicted product of the gene segment of _D. quadriceps_ genome [XP_014477391]. The protein precursor of _D. quadriceps_ hyaluronidase is 368 aa long, with a signal peptide of 25 residues and a mature protein of 343 aa (theoretical molecular mass 38844.96 Da), but the glycosylation-specific sites, which could cause the apparent distinct pattern of electrophoretic migration to diverge from the theoretical molecular mass, are identifiable (Figure 1, Table S1). The _D. quadriceps_ venom hyaluronases share high similarity (99%) with homologous sequences from the venoms of common wasp and honey bee (Figure 6). Figure 5: Alignment and structural model of _D. quadriceps_ venom phospholipase A1. (**A**) _D. quadriceps_ venom phospholipase A1 was aligned to some hypnopteran homologues: [PA1_SOLIN], PLA1 (Allergen Sol i 1) from _S. invicka_; [PA1_VESBA], Phospholipase A1 from black-bellied hornet _Vespa basalis_ and [PDB 14 QNN | A], sequence that generated the crystal structure of the A chain by X-ray diffraction; [PA1_VESMG], hornet wasp _Vespa magnifica_ phospholipase A1 magnificn; [PA12_DOLMA] phospholipase A1-2 (Allergen Dol m 1) from bald-faced hornet _Dolichovespa unculata_; [PA1_VESGE] phospholipase A1 (Allergen Ves g 1) form European wasp (German yellowjacket) _Vespa germanaia_; [PA1_VESMC], phospholipase A1 (Allergen Ves m 1) from Eastern yellow jacket _Vespa uncalifornos_. Glycosylated asparagine residues are indicated in emerald green. Dark green amino acids indicate natural variants. The amino acids from the enzymatic active site are indicated in light green and the consensus Gly-X-Ser-X-Gly motif, characteristic of the active serine hydrolases, is boxed in red. Moss  
green indicated divergent or conflictive residues. The signal peptide is indicated in brown and the pro-peptide in military green. Conserved cysteine residues that participate in the formation of disulfide bridges are indicated by purple boxes and connected by solid black lines, as determined for wasps' PLA1s. Unpaired cysteines are indicated in light purple and the connecting lines indicate the possible connectivity based on homology model of the mature PLA1 sequence of _D. quadriceps_. The conservation was estimated with the BLOSUM62 matrix. (**B**) Structural model of _D. quadriceps_ PLA1 predicted by homology modeling from venom gland transcript Contig27_B2-2 and the venom phospholipase A1 from hornet wasp _Vespa basalis_ (PDB 4 QNN), as template. This giant ant venom component was detected in-gel analysis (gel bands 6 and 7). Similarly, predicted from the transcripts consensus_20 Phospholipase A1-like 1_B04_E7_DVC2, that corresponds to gel bands 10 and 11. Also detected in-solution proteomic analysis: protein 7 (Contig27_B2-2); protein 17 (1_B04_E7_DVC2); Based on the structural analysis, this giant ant toxin is presumably a platelet activator, like in Vespidae venoms. Note: protein 12, from in-solution analysis, is a PLA2. 2.6 Major Venom Allergen 3, Cysteine-Rich Venom Protein Superfamily; Cysteine-Rich Secretary Protein (CRISP) Family  
This protein was identified from the SDS-PAGE gel band 9 (with peptide fragments covering 23% of the full sequence) and from the in-solution proteomic analysis protein 16 (with peptide fragments covering 52% and 47% of the full sequence). It corresponded with the major venom allergen 3, a cysteine-rich venom protein precursor encoded by the _D. quadriceps_ venom gland Contig12_B2-2 (Table S1).