Glycoproteome in silkworm Bombyx mori and alteration by BmCPV infection.
BmCPV
Bombxy mori
Glycoproteome
O-glycans
Silkworm
Journal
Journal of proteomics
ISSN: 1876-7737
Titre abrégé: J Proteomics
Pays: Netherlands
ID NLM: 101475056
Informations de publication
Date de publication:
30 06 2020
30 06 2020
Historique:
received:
18
03
2020
revised:
19
04
2020
accepted:
27
04
2020
pubmed:
4
5
2020
medline:
22
6
2021
entrez:
4
5
2020
Statut:
ppublish
Résumé
The biological functions of protein glycosylation have been increasingly recognized but not yet been very well understood, especially in lower organisms. Silkworm as a model lepidopteran insect and important economic insect, has been widely studied in life science, however, the current knowledge on the glycosylation status of its proteome is not satisfactory, and little is known about how pathogenic infections could affect the glycosylation status. This study performed large scale glycosite mapping for the silkworm Bombyx mori P50 strain, and quantitatively compared with that infected with the Bombyx mori cytoplasmic polyhedrosis virus (BmCPV). Some 400 glycoproteins were mapped in the silkworm, including N- and O-glycoproteins. Upon virus infection, the glycosylation levels of 41 N-glycopeptides were significantly changed, some of them belonging to transmembrane glycoproteins. The O-glycosylation profiles were also affected. In addition, 4 BmCPV-encoded viral proteins were found to be glycosylated for the first time, including polyhedrin, P101, VP3, and the NS protein. This study drafted a silkworm protein glycosylation map and underlined the potential impact of virus infection on glycosylation. SIGNIFICANCE: This study reveals the characteristics of the glycoproteome in the silkworm strain P50, and quantitatively compared to that infected by the virus BmCPV, which underlines the impact of virus infection on the alteration of protein glycosylation in invertebrate species. Our findings add to the knowledge of the post translational modifications of this model organism, and also uncovered for the first time the glycosylation status of the viral proteins expressed by BmCPV.
Identifiants
pubmed: 32360640
pii: S1874-3919(20)30170-6
doi: 10.1016/j.jprot.2020.103802
pmc: PMC7194664
pii:
doi:
Substances chimiques
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
103802Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest None.
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