Characterization of Angiostrongylus cantonensis excretory–secretory proteins as potential diagnostic targets

Morassutti, Alessandra Loureiro; Levert, Keith; Pinto, Paulo Marcos; Silva, Alexandre J. da; Wilkins, Patricia P.; Graeff-Teixeira, Carlos

doi:10.1016/j.exppara.2011.10.003

Cited by 40 publications

(49 citation statements)

References 29 publications

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“…Obviously, consistent with the infective stage of L3 is an intense staining of AC-cathBs in the esophagus and excretory. So, the results in this report further supported our previous observations resulting from Signal-P, RT-PCR, and western blot analyses (Fang et al, 2010;Ni et al, 2012), and from electrospray ionization mass spectrometry (Morassutti et al, 2012). There is a big difference in the structure between larvae and adults, no lateral glands and lateral alae could be seen in the body wall of adult A. cantonensis, while they were more obvious in L1 and L3 (Xu et al, 1989;Ding et al, 1990).…”

Section: Discussionsupporting

confidence: 94%

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Yu¹,

Wang²,

Zhang³

et al. 2014

Experimental Parasitology

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Section: Discussionsupporting

confidence: 94%

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Yu¹,

Wang²,

Zhang³

et al. 2014

Experimental Parasitology

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“…A lone study characterized a H. longicornis tick serine carboxypeptidase that is predominantly expressed in midgut and up regulated in response to tick feeding with the yeast expressed recombinant protein cleaving substrates similar to those of human serine carboxypeptidase cathepsin A [109]. Indirect evidence in helminth parasites, Strongyloides ratti [110] and Angiostrongylus cantonensis [111], excretory-secretory proteomes suggests that serine carboxypeptidases are part of the protein complex that regulates helminth parasite and host interactions. The presence of serine carboxypeptidases in A. americanum tick saliva may indicate that similar to other parasites, ticks use this class of proteins to regulate tick-host interactions.…”

Section: Resultsmentioning

confidence: 99%

A 24-48 h fed Amblyomma americanum tick saliva immuno-proteome

et al. 2014

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BackgroundMultiple tick saliva proteins, the majority of which are unknown, confer tick resistance in repeatedly infested animals. The objective of this study was to identify the 24-48 h fed Amblyomma americanum tick saliva immuno-proteome. The 24-48 h tick-feeding phase is critical to tick parasitism as it precedes important events in tick biology, blood meal feeding and disease agent transmission. Fed male, 24 and 96 h fed female phage display cDNA expression libraries were biopanned using rabbit antibodies to 24 and 48 h fed A. americanum female tick saliva proteins. Biopanned immuno-cDNA libraries were subjected to next generation sequencing, de novo assembly, and bioinformatic analysis.ResultsMore than 800 transcripts that code for 24-48 h fed A. americanum immuno-proteins are described. Of the 895 immuno-proteins, 52% (464/895) were provisionally identified based on matches in GenBank. Of these, ~19% (86/464) show high level of identity to other tick hypothetical proteins, and the rest include putative proteases (serine, cysteine, leukotriene A-4 hydrolase, carboxypeptidases, and metalloproteases), protease inhibitors (serine and cysteine protease inhibitors, tick carboxypeptidase inhibitor), and transporters and/or ligand binding proteins (histamine binding/lipocalin, fatty acid binding, calreticulin, hemelipoprotein, IgG binding protein, ferritin, insulin-like growth factor binding proteins, and evasin). Others include enzymes (glutathione transferase, cytochrome oxidase, protein disulfide isomerase), ribosomal proteins, and those of miscellaneous functions (histamine release factor, selenoproteins, tetraspanin, defensin, heat shock proteins).ConclusionsData here demonstrate that A. americanum secretes a complex cocktail of immunogenic tick saliva proteins during the first 24-48 h of feeding. Of significance, previously validated immunogenic tick saliva proteins including AV422 protein, calreticulin, histamine release factor, histamine binding/lipocalins, selenoproteins, and paramyosin were identified in this screen, supporting the specificity of the approach in this study. While descriptive, this study opens opportunities for in-depth tick feeding physiology studies.Electronic supplementary materialThe online version of this article (doi:10.1186/1471-2164-15-518) contains supplementary material, which is available to authorized users.

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“…Although actin is a cytoskeletal protein, it has been detected in the ESP of different helminths such as Echinostoma caproni or Angiostrongylus cantonensis (54,55). Recently, parasitic trematodes were shown to secrete extracellular microvesicles that resembled mammalian exosomes (51), and accounts for the secretion of some proteins that lack a signal peptide.…”

Section: Discussionmentioning

confidence: 99%

Secreted Proteomes of Different Developmental Stages of the Gastrointestinal Nematode Nippostrongylus brasiliensis

Sotillo

Sánchez-Flores

Cantacessi

et al. 2014

Molecular & Cellular Proteomics

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ʈʈHookworms infect more than 700 million people worldwide and cause more morbidity than most other human parasitic infections. Nippostrongylus brasiliensis (the rat hookworm) has been used as an experimental model for human hookworm because of its similar life cycle and ease of maintenance in laboratory rodents. Adult N. brasiliensis, like the human hookworm, lives in the intestine of the host and releases excretory/secretory products (ESP), which represent the major host-parasite interface. We performed a comparative proteomic analysis of infective larval (

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Characterization of Angiostrongylus cantonensis excretory–secretory proteins as potential diagnostic targets

Cited by 40 publications

References 29 publications

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

A 24-48 h fed Amblyomma americanum tick saliva immuno-proteome

Secreted Proteomes of Different Developmental Stages of the Gastrointestinal Nematode Nippostrongylus brasiliensis

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