TY  - JOUR
AU  - Aili, S.R.
AU  - Touchard, A.
AU  - Koh, J.M.S.
AU  - Dejean, A.
AU  - Orivel, J.
AU  - Padula, M.P.
AU  - Escoubas, P.
AU  - Nicholson, G.M.
PY  - 2016//
TI  - Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms
T2  - Journal of Proteome Research
JO  - Journal of Proteome Research
SP  - 3039
EP  - 3054
VL  - 15
IS  - 9
KW  - ant venom
KW  - Hymenoptera
KW  - Lc-Maldi-Tof Ms
KW  - mass spectrometry
KW  - nanoLC-ESI-QTOF MS/MS
KW  - peptidome
KW  - proteomic analysis
KW  - toxin
N2  - Animal venom peptides are currently being developed as novel drugs and bioinsecticides. Because ants use venoms for defense and predation, venomous ants represent an untapped source of potential bioactive toxins. This study compared the protein and peptide components of the poneroid ants Neoponera commutata, Neoponera apicalis, and Odontomachus hastatus and the formicoid ants Ectatomma tuberculatum, Ectatomma brunneum, and Myrmecia gulosa. 1D and 2D PAGE revealed venom proteins in the mass range <10 to >250 kDa. NanoLC-ESI-QTOF MS/MS analysis of tryptic peptides revealed the presence of common venom proteins and also many undescribed proteins. RP-HPLC separation followed by MALDI-TOF MS of the venom peptides also revealed considerable heterogeneity. It was found that the venoms contained between 144 and 1032 peptides with 5-95% of peptides in the ranges 1-4 and 1-8 kDa for poneroid and formicoid ants, respectively. By employing the reducing MALDI matrix 1,5-diaminonapthalene, up to 28 disulfide-bonded peptides were also identified in each of the venoms. In particular, the mass range of peptides from poneroid ants is lower than peptides from other venoms, indicating possible novel structures and pharmacologies. These results indicate that ant venoms represent an enormous, untapped source of novel therapeutic and bioinsecticide leads. © 2016 American Chemical Society.
UR  - https://www.scopus.com/inward/record.uri?eid=2-s2.0-84986000861&partnerID=40&md5=9eea3812a11b3a955ce21e4bbea84e6f
UR  - http://dx.doi.org/10.1021/acs.jproteome.6b00182
N1  - Export Date: 15 September 2016
ID  - Aili_etal2016
ER  -