A saliva α-glucosidase MpAgC2-2 enhance the feeding of green peach aphid Myzus persicae via extra-intestinal digestion.
Phloem sap
RNAi
Saliva
Sucrose hydrolysis
α-glucosidase
Journal
Insect biochemistry and molecular biology
ISSN: 1879-0240
Titre abrégé: Insect Biochem Mol Biol
Pays: England
ID NLM: 9207282
Informations de publication
Date de publication:
11 2022
11 2022
Historique:
received:
14
07
2022
revised:
15
09
2022
accepted:
15
09
2022
pubmed:
7
10
2022
medline:
9
11
2022
entrez:
6
10
2022
Statut:
ppublish
Résumé
Aphids feed on plant phloem sap that contains massive amounts of sucrose; this not only provides vital nutrition for the aphids but also produces high osmotic pressure. To utilize this carbon source and overcome the osmotic pressure, sucrose is hydrolyzed into the monosaccharides, glucose and fructose. In the green peach aphid (Myzus persicae), we show that this process is facilitated by a key α-glucosidase (MpAgC2-2), which is abundant in the aphid salivary gland and is secreted into leaves during feeding. MpAgC2-2 has a pH optimum of 8.0 in vitro, suggesting it has adapted to the environment of plant cells. Silencing MpAgC2-2 (but not the gut-specific MpAgC3-4) significantly increased the amount of sucrose ingested and hindered aphid feeding on the phloem of tobacco seedlings, resulting in a smaller body size, as well as lower α-glucosidase activity and glucose levels. These effects could be rescued by feeding aphids on tobacco plants transiently expressing MpAgC2-2. The transient expression of MpAgC2-2 also led to the hydrolysis of sucrose in tobacco leaves. Taken together, these results demonstrate that MpAgC2-2 is a salivary protein that facilitates extra-intestinal feeding via sucrose hydrolysis. Our findings provide insight into the ability of aphids to digest the high concentration of sucrose in phloem, and the underlying mechanism of extra-intestinal digestion.
Identifiants
pubmed: 36202385
pii: S0965-1748(22)00128-X
doi: 10.1016/j.ibmb.2022.103846
pii:
doi:
Substances chimiques
alpha-Glucosidases
EC 3.2.1.20
Sucrose
57-50-1
Glucose
IY9XDZ35W2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
103846Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare they have no conflicts of interests.