Differential analysis of the haemolymph proteome of Carcinus maenas parasitized by Sacculina carcini (Cirripeda, Rhizocephala) reveals potential mechanisms of parasite control.
Carcinus maenas
Comparative proteomics
Mass spectrometry
Parasite cirriped rhizocephala
Sacculina carcini
Journal
Fish & shellfish immunology
ISSN: 1095-9947
Titre abrégé: Fish Shellfish Immunol
Pays: England
ID NLM: 9505220
Informations de publication
Date de publication:
Oct 2023
Oct 2023
Historique:
received:
22
07
2023
revised:
03
09
2023
accepted:
06
09
2023
medline:
29
9
2023
pubmed:
10
9
2023
entrez:
9
9
2023
Statut:
ppublish
Résumé
Sacculina carcini is an endoparasite of the green crab, Carcinus maenas. This parasite induces behavioural changes in its host and affects its metabolism by inhibiting moulting and reproduction. Using a proteomic approach in mass spectrometry, we studied the haemolymph proteomes of healthy and parasitized wild green crabs from Brittany, France to identify proteins that are differentially expressed as a consequence of parasitization. We also investigated specific proteins involved in reproduction, moulting, and immunity. We detected 77 proteins for females and 53 proteins for males that were differentially present between the healthy and parasitized crabs, some of which were sex-specific. Detection of these differentially expressed proteins suggests that the parasite can inhibit and promote different aspects of the immune response of the host. Sacculina appears to inhibit host melanisation for self-protection, while promoting the presence of immune factors, such as antimicrobial peptides to cope with possible bacterial superinfections. Moreover, one protein, juvenile hormone esterase-like carboxylesterase, was 17-times more abundant in parasitized crabs than in healthy crabs and may be responsible for inhibiting moulting and reproduction in parasitized crabs, thus ensuring the success of Sacculina reproduction.
Identifiants
pubmed: 37689227
pii: S1050-4648(23)00550-8
doi: 10.1016/j.fsi.2023.109064
pii:
doi:
Substances chimiques
Proteome
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109064Informations de copyright
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