Effects of Manduca sexta allatostatin and an analog on the pea aphid Acyrthosiphon pisum (Hemiptera: Aphididae) and degradation by enzymes from the aphid gut

The C-type allatostatin, Manduca sexta allatostatin (Manse-AS) and the analog δR 3δR 5Manse-AS, where R residues were replaced by their d-isomers, were tested for oral toxicity against the pea aphid Acyrthosiphon pisum (Harris) by incorporation into an artificial diet. Both peptides had significant...

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Veröffentlicht in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2010-03, Vol.31 (3), p.489-497
Hauptverfasser: Down, Rachel E., Matthews, H. June, Audsley, Neil
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Sprache:eng
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Zusammenfassung:The C-type allatostatin, Manduca sexta allatostatin (Manse-AS) and the analog δR 3δR 5Manse-AS, where R residues were replaced by their d-isomers, were tested for oral toxicity against the pea aphid Acyrthosiphon pisum (Harris) by incorporation into an artificial diet. Both peptides had significant dose-dependent feeding suppression effects, resulting in mortality, reduced growth and fecundity compared with control insects. The δR 3δR 5Manse-AS analog had an estimated LC 50 of 0.18 μg/μl diet, and was more potent than Manse-AS. At a dose of 0.35 μg δR 3δR 5Manse-AS/μl diet, 98% of aphids were dead within 3 days, at a rate similar to those aphids that had been starved (no diet controls). On comparison, it required 13 days and three times the dose of Manse-AS fed to aphids to attain 96% mortality. It is possible that the feeding suppression effects of Manse-AS on aphids are due to the inhibition of gut motility. The estimated half-life of Manse-AS when incubated with a gut extract from A. pisum was 54 min. Degradation was most likely due to cathepsin L cysteine and/or trypsin-like proteases, by an unidentified glutamine-specific protease and by a carboxypeptidase-like enzyme. The d-isomers of R in the Manse-AS analog appeared to prevent hydrolysis by cathepsin L cysteine and trypsin-like enzymes, and enhance its half-life (145 min). However δR 3δR 5Manse-AS was cleaved by enzymes with carboxypeptidase-like and chymotrypsin-like activity. The increased stability of the Manse-AS analog may explain its enhanced feeding suppression effects when continually fed to aphids, and demonstrates the potential use of Manse-AS in a strategy to control aphid pests.
ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2009.06.017