Transcriptomic-Proteomic Correlation in the Predation-Evoked Venom of the Cone Snail, Conus imperialis

Jin, Aihua; Dutertre, Sébastien; Dutt, Mriga; Lavergne, Vincent; Jones, Alun; Lewis, Richard J.; Alewood, Paul F.

doi:10.3390/md17030177

Cited by 19 publications

(38 citation statements)

References 40 publications

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“…As for other venoms (105, 126, 127), bee venom is very susceptible to variability, depending on bee age, species, social condition, geographic localization, amongst other factors (44). For instance, young worker bees (foragers/guards/nurses) have higher levels of apamin and lower levels of melittin compared to old workers (foragers/guards).…”

Section: Bee Sting and Venommentioning

confidence: 99%

Bee Updated: Current Knowledge on Bee Venom and Bee Envenoming Therapy

et al. 2019

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Honey bees can be found all around the world and fulfill key pollination roles within their natural ecosystems, as well as in agriculture. Most species are typically docile, and most interactions between humans and bees are unproblematic, despite their ability to inject a complex venom into their victims as a defensive mechanism. Nevertheless, incidences of bee stings have been on the rise since the accidental release of Africanized bees to Brazil in 1956 and their subsequent spread across the Americas. These bee hybrids are more aggressive and are prone to attack, presenting a significant healthcare burden to the countries they have colonized. To date, treatment of such stings typically focuses on controlling potential allergic reactions, as no specific antivenoms against bee venom currently exist. Researchers have investigated the possibility of developing bee antivenoms, but this has been complicated by the very low immunogenicity of the key bee toxins, which fail to induce a strong antibody response in the immunized animals. However, with current cutting-edge technologies, such as phage display, alongside the rise of monoclonal antibody therapeutics, the development of a recombinant bee antivenom is achievable, and promising results towards this goal have been reported in recent years. Here, current knowledge on the venom biology of Africanized bees and current treatment options against bee envenoming are reviewed. Additionally, recent developments within next-generation bee antivenoms are presented and discussed.

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Section: Bee Sting and Venommentioning

confidence: 99%

Bee Updated: Current Knowledge on Bee Venom and Bee Envenoming Therapy

et al. 2019

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“…The technique has been shown to be highly efficient as even rare transcripts are detected, but necessary controls on the quality and coverage of the assembled contigs need to be implemented to avoid potential artifacts that may overestimate conotoxin sequence diversity [7]. Moreover, analyzing venom gland transcriptomes in several individuals per species is useful for quantifying the differential expression of conotoxins [7] and for identifying peptide peaks obtained through advanced mass-spectrometry techniques directly from the venom [26,27].…”

Section: Introductionmentioning

confidence: 99%

Conotoxin Diversity in the Venom Gland Transcriptome of the Magician’s Cone, Pionoconus magus

et al. 2019

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The transcriptomes of the venom glands of two individuals of the magician’s cone, Pionoconus magus, from Okinawa (Japan) were sequenced, assembled, and annotated. In addition, RNA-seq raw reads available at the SRA database from one additional specimen of P. magus from the Philippines were also assembled and annotated. The total numbers of identified conotoxin precursors and hormones per specimen were 118, 112, and 93. The three individuals shared only five identical sequences whereas the two specimens from Okinawa had 30 sequences in common. The total number of distinct conotoxin precursors and hormones for P. magus was 275, and were assigned to 53 conotoxin precursor and hormone superfamilies, two of which were new based on their divergent signal region. The superfamilies that had the highest number of precursors were M (42), O1 (34), T (27), A (18), O2 (17), and F (13), accounting for 55% of the total diversity. The D superfamily, previously thought to be exclusive of vermivorous cones was found in P. magus and contained a highly divergent mature region. Similarly, the A superfamily alpha 4/3 was found in P. magus despite the fact that it was previously postulated to be almost exclusive of the genus Rhombiconus. Differential expression analyses of P. magus compared to Chelyconus ermineus, the only fish-hunting cone from the Atlantic Ocean revealed that M and A2 superfamilies appeared to be more expressed in the former whereas the O2 superfamily was more expressed in the latter.

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“…MS analysis of milked venom versus venom extracted from venom ducts has revealed differences in protein sequences between the two sets, which point to the influence of sampling or protein extraction methods in the resulting proteomes [ 20 ]. Recently, intraspecific variations in conopeptides expressed by different individuals of the same species have also been revealed [ 21 , 22 , 23 , 24 ]. Lastly, in addition to intraspecific variations, changes in the venom peptide composition of individuals during feeding events have also been observed through MS studies [ 25 ].…”

Section: Introductionmentioning

confidence: 99%

Identification of Conomarphin Variants in the Conus eburneus Venom and the Effect of Sequence and PTM Variations on Conomarphin Conformations

et al. 2020

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Marine cone snails belonging to the Conidae family make use of neuroactive peptides in their venom to capture prey. Here we report the proteome profile of the venom duct of Conus eburneus, a cone snail belonging to the Tesseliconus clade. Through tandem mass spectrometry and database searching against the C. eburneus transcriptome and the ConoServer database, we identified 24 unique conopeptide sequences in the venom duct. The majority of these peptides belong to the T and M gene superfamilies and are disulfide-bonded, with cysteine frameworks V, XIV, VI/VII, and III being the most abundant. All seven of the Cys-free peptides are conomarphin variants belonging to the M superfamily that eluted out as dominant peaks in the chromatogram. These conomarphins vary not only in amino acid residues in select positions along the backbone but also have one or more post-translational modifications (PTMs) such as proline hydroxylation, C-term amidation, and γ-carboxylation of glutamic acid. Using molecular dynamics simulations, the conomarphin variants were predicted to predominantly have hairpin-like or elongated structures in acidic pH. These two structures were found to have significant differences in electrostatic properties and the inclusion of PTMs seems to complement this disparity. The presence of polar PTMs (hydroxyproline and γ-carboxyglutamic acid) also appear to stabilize hydrogen bond networks in these conformations. Furthermore, these predicted structures are pH sensitive, becoming more spherical and compact at higher pH. The subtle conformational variations observed here might play an important role in the selection and binding of the peptides to their molecular targets.

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Transcriptomic-Proteomic Correlation in the Predation-Evoked Venom of the Cone Snail, Conus imperialis

Cited by 19 publications

References 40 publications

Bee Updated: Current Knowledge on Bee Venom and Bee Envenoming Therapy

Bee Updated: Current Knowledge on Bee Venom and Bee Envenoming Therapy

Conotoxin Diversity in the Venom Gland Transcriptome of the Magician’s Cone, Pionoconus magus

Identification of Conomarphin Variants in the Conus eburneus Venom and the Effect of Sequence and PTM Variations on Conomarphin Conformations

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