Comprehensive proteomic profiling of adult Angiostrongylus costaricensis, a human parasitic nematode

Toxinology Laboratory, Oswaldo Cruz Institute (IOC), Fiocruz, Rio de Janeiro, Brazil.
Journal of proteomics (Impact Factor: 3.89). 05/2011; 74(9):1545-59. DOI: 10.1016/j.jprot.2011.04.031
Source: PubMed


Angiostrongylus costaricensis is a nematode helminth that causes an intestinal acute inflammatory process known as abdominal angiostrongyliasis, which is a poorly understood human disease occurring in Latin America. Our aim was to study the proteomic profiles of adult parasites focusing on immunogenic proteins. Total cellular extracts from both genders showed similar 2-DE profiles, with 60% of all protein spots focused between pH 5-7 and presenting molecular masses from 20.1 to 66 kDa. A total of 53 different dominant proteins were identified in our dataset and were mainly associated with the following over-represented Gene Ontology Biological Process terms: "macromolecule metabolic process", "developmental process", "response to stress", and "biological regulation". Female and male immunoblots showed similar patterns of reactive proteins. Immunoreactive spots identified by MALDI-PSD were found to represent heat shock proteins, a putative abnormal DAuer Formation family member, and galectins. To date, very few biochemical analyses have focused on the nematode Angiostrongylus costaricensis. As such, our results contribute to a better understanding of its biology and the mechanisms underlying the host-parasite relationship associated with this species. Moreover, our findings represent a first step in the search for candidate proteins for diagnostic assays and the treatment of this parasitic infection.

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Available from: Karina Rebello, Feb 24, 2014
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    • "In addition, this antigen was recently identified in Angiostrongylus costaricensis by Rebello et al. (2011) and in Angiostrongylus cantonensis by Morassutti et al. (2012). In the latter study, the authors also described peptide molecules with high homology to As37 in Baylisascaris schroederi and B. malayi. "
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    ABSTRACT: Ortleppascaris sp. is a helminth that, in its larval stage, infects the liver parenchyma of the amphibian Rhinella marina, resulting in severe physiological and pathological changes. This study used a proteomic approach to determine the overall profile of proteins expressed in a somatic extract from the nematodes to investigate the relationship between the parasite and its host. A total of 60 abundant proteins were selected from the two-dimensional electrophoresis, identified by peptide mass fingerprinting, and grouped based on their Gene Ontology by the biological processes in which they are potentially involved. Important helminthic derivatives, such as the immunoreactive As37 antigen, guanylyl cyclases, proteolytic enzymes, and other proteins conserved among different parasites, were identified through homology. This study represents a new approach to helminth-related proteomic studies using an amphibian animal model. Furthermore, this study identified protein markers that are important to the host-parasite relationship and the viability, development, infectivity, and virulence of helminths.
    International Journal for Parasitology: Parasites and Wildlife 08/2014; 3(2). DOI:10.1016/j.ijppaw.2014.03.003
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    • "Proteomics has been producing data on a large scale; however due to the scarcity of helminth genomes, there is a need for the production of more data on ''helminth-derived'' substances. This is especially true when considering the large number of species and the plasticity of these organisms in terms of their biology, morphology , development in different hosts and infection and transmission modes (Rebello et al., 2011; Mutapi, 2012). Despite this biological variety, the murines are the current animal models of choice in the biological sciences; however, other biological systems in vivo can be promising study models and also to contribute to the elucidation of the host–parasite relationship (Bolker, 2012; Sotillo et al., 2012; Robinson et al., 2013). "
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    ABSTRACT: The success of the helminth–host relationship depends on a biochemical molecular arsenal. Perhaps the proteome is the largest and most important set of this weaponry, in which the proteins have a crucial role in vital processes to the parasite/host relationship, from basic metabolism and energy production to complex immune responses. Nowadays, the bioproducts expressed by the parasites are under the “spotlight” of immunoassays and biochemical analysis in helminthology, especially in proteomic analysis, which has provided valuable information about the physiology of the infecting agent. Looking into this point of view, why not turn to the infected agent as well? This study characterised the proteomic profile of fluid-filled fibrous cysts of encapsulated Ortleppascaris sp. larvae in the hepatic parenchyma of their intermediate host, the amphibian Rhinella marina. The proteins were separated by two-dimensional electrophoresis and identified by MS with the aid of Peptide Mass Fingerprint. A total of 54 molecules were analysed in this system, revealing a complex protein profile with molecules related to basic metabolic processes of the parasite, energy production, oxi-reduction and oxidative stress processes as well as molecules related to the host response. This study contributes to proteomic studies of protein markers of the development, infectivity, virulence and co-existence of helminths and their hosts.
    International Journal for Parasitology: Parasites and Wildlife 08/2014; 3(2). DOI:10.1016/j.ijppaw.2014.05.004
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    • "The down-regulation of IDO, NEX1 annexin, and members of the TRRAP-like family observed in adult male A. cantonensis and the up-regulation observed in adult female A. cantonensis was coincidence with those published data. It may be related to the observation that female adults survived better than the male adults [47], [48]. However, these proteins were not found to be up-regulated in FL5 compared to ML5. "
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    ABSTRACT: Angiostrongyliasis is an emerging communicable disease. Several different hosts are required to complete the life cycle of Angiostrongylus cantonensis. However, we lack a complete understanding of variability of proteins across different developmental stages and their contribution to parasite survival and progression. In this study, we extracted soluble proteins from various stages of the A. cantonensis life cycle [female adults, male adults, the fifth-stage female larvae (FL5), the fifth-stage male larvae (ML5) and third-stage larvae (L3)], separated those proteins using two-dimensional difference gel electrophoresis (2D-DIGE) at pH 4-7, and analyzed the gel images using DeCyder 7.0 software. This proteomic analysis produced a total of 183 different dominant protein spots. Thirty-seven protein spots were found to have high confidence scores (>95%) by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). Comparative proteomic analyses revealed that 29 spots represented cytoskeleton-associated proteins and functional proteins. Eight spots were unnamed proteins. Twelve protein spots that were matched to the EST of different-stage larvae of A. cantonensis were identified. Two genes and the internal control 18s were chosen for quantitative real-time PCR (qPCR) and the qPCR results were consistent with those of the DIGE studies. These findings will provide a new basis for understanding the characteristics of growth and development of A. cantonensis and the host-parasite relationship. They may also assist searches for candidate proteins suitable for use in diagnostic assays and as drug targets for the control of eosinophilic meningitis caused by A. cantonensis.
    PLoS ONE 10/2013; 8(10):e76982. DOI:10.1371/journal.pone.0076982 · 3.23 Impact Factor
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