Literature DB >> 24602330

Proteomic analysis of the somatic and surface compartments from Dirofilaria immitis adult worms.

R Morchón1, J González-Miguel2, E Carretón3, L H Kramer4, L Valero5, J A Montoya-Alonso3, F Simón2, M Siles-Lucas6.   

Abstract

Dirofilaria immitis (hearthworm) is a filarial roundworm transmitted by mosquitoes to different vertebrate hosts (dogs, cats and humans, among others), causing dirofilariosis. The adult worms reside in the pulmonary arteries affecting vessels and tissues and resulting in different pathological manifestations. Worms migrate to the heart and surrounding major vessels in heavy infections. Dirofilariosis can result in serious damage to affected hosts. In the last few years, a re-emergence of the disease driven by the climate change has been pointed out. Very recently, the knowledge at molecular level of this parasite has been extended by the published studies on its genome and transcriptome. Nevertheless, studies on the expression of defined protein sets in different parasite compartments and the corresponding role of those proteins in the host-parasite relationship have been relatively scarce to date. These include the description of the adult worm secretome, and some of the proteins eliciting humoural immune responses and those related with plasminogen binding in secreted and surface extracts of the parasite. Here, we investigate by proteomics the somatic and surface compartments of the D. immitis adult worm, adding new information on protein expression and localization that would facilitate a deeper understanding of the host-parasite relationships in dirofilariosis.
Copyright © 2014 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Dirofilaria immitis; Proteomics; Somatic; Surface

Mesh:

Substances:

Year:  2014        PMID: 24602330     DOI: 10.1016/j.vetpar.2014.02.005

Source DB:  PubMed          Journal:  Vet Parasitol        ISSN: 0304-4017            Impact factor:   2.738


  5 in total

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4.  Fatty-binding protein and galectin of Baylisascaris schroederi: Prokaryotic expression and preliminary evaluation of serodiagnostic potential.

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Review 5.  Prospects of Using High-Throughput Proteomics to Underpin the Discovery of Animal Host-Nematode Interactions.

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Journal:  Pathogens       Date:  2021-06-30
  5 in total

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