Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae)

Frontiers in Cellular and Infection Microbiology

Cellular and Infection Microbiology

Bruno Maras¹  Giuseppina Mignogna¹  Alessandra Giorgi¹  Maria Eugenia Schinin๠ Tiziana Castrignanò²  Marialetizia Palomba²  Valentina Pinna²  Aurelia Rughetti³  Hassan Rahimi³  Laura Masuelli³  Chiara Napoletano³  Mario Santoro⁴  Simonetta Mattiucci⁵ 

[1] Department of Biochemistry Science, Sapienza University of Rome, Rome, Italy;Department of Ecological and Biological Sciences, University of Tuscia, Viterbo, Italy;Department of Experimental Medicine, Sapienza University of Rome, Rome, Italy;Department of Integrative Marine Ecology, Stazione Zoologica Anton Dohrn, Naples, Italy;Department of Public Health and Infectious Diseases, Section of Parasitology, Sapienza University of Rome, Rome, Italy;

关键词: Anisakis pegreffii;    zoonotic parasite;    third stage larvae;    extracellular vesicles;    proteomics;    heat shock proteins;    metalloproteases;    allergenic proteins;   

DOI  :  10.3389/fcimb.2023.1079991

 received in 2022-10-25, accepted in 2023-02-28,  发布年份 2023

来源: Frontiers

【 摘 要 】

IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts.

【 授权许可】

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Copyright © 2023 Palomba, Rughetti, Mignogna, Castrignanò, Rahimi, Masuelli, Napoletano, Pinna, Giorgi, Santoro, Schininà, Maras and Mattiucci