%0 Journal Article
%T Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms
%A Aili, S.R.
%A Touchard, A.
%A Koh, J.M.S.
%A Dejean, A.
%A Orivel, J.
%A Padula, M.P.
%A Escoubas, P.
%A Nicholson, G.M.
%J Journal of Proteome Research
%D 2016
%V 15
%N 9
%F Aili_etal2016
%O Export Date: 15 September 2016
%O exported from refbase (http://php.ecofog.gf/refbase/show.php?record=695), last updated on Tue, 17 Jan 2017 11:34:13 -0300
%X 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.
%K ant venom
%K Hymenoptera
%K Lc-Maldi-Tof Ms
%K mass spectrometry
%K nanoLC-ESI-QTOF MS/MS
%K peptidome
%K proteomic analysis
%K toxin
%U https://www.scopus.com/inward/record.uri?eid=2-s2.0-84986000861&partnerID=40&md5=9eea3812a11b3a955ce21e4bbea84e6f
%U http://dx.doi.org/10.1021/acs.jproteome.6b00182
%P 3039-3054