Combined Peptidomic and Proteomic Analysis of Electrically Stimulated and Manually Dissected Venom from the South American Bullet Ant Paraponera clavata
2D-page
Proteomics
0301 basic medicine
[SDV]Life Sciences [q-bio]
610
venon
[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry
03 medical and health sciences
Tandem Mass Spectrometry
[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN]
peptidome
MALDI-TOF MS
Animals
bullet ant
Electrophoresis, Gel, Two-Dimensional
Molecular Biology/Genomics [q-bio.GN]
Ant Venoms
Ants
proteone
[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate Zoology
electrical simulation
maldi-tof ms
dissection
Insect Proteins
Peptides
DOI:
10.1021/acs.jproteome.6b00948
Publication Date:
2017-01-24T18:21:50Z
AUTHORS (8)
ABSTRACT
Ants have evolved venoms rich in peptides and proteins used for predation, defense, and communication. However, they remain extremely understudied due to the minimal amount of venom secreted by each ant. The present study investigated the differences in the proteome and peptidome of the venom from the bullet ant, Paraponera clavata. Venom samples were collected from a single colony either by manual venom gland dissection or by electrical stimulation and were compared using proteomic methods. Venom proteins were separated by 2D-PAGE and identified by nanoLC-ESI-QTOF MS/MS. Venom peptides were initially separated using C18 reversed-phase high-performance liquid chromatography, then analyzed by MALDI-TOF MS. The proteomic analysis revealed numerous proteins that could be assigned a biological function (total 94), mainly as toxins, or roles in cell regulation and transport. This investigation found that ca. 73% of the proteins were common to venoms collected by the two methods. The peptidomic analysis revealed a large number of peptides (total 309) but with <20% shared by the two collection methods. There was also a marked difference between venoms obtained by venom gland dissection from different ant colonies. These findings demonstrate the rich composition and variability of P. clavata venom.
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