Proteolytic activity in the adult and larval stages of the human roundworm parasite Angiostrongylus costaricensis

Rebello, Karina M.; Siqueira, Caroline Reis de; Ribeiro, Erika Louise; Valente, Richard H.; Mota, Eduardo; Perales, Jonás; Neves-Ferreira, Ana Gisele C.; Lenzi, Henrique Leonel

doi:10.1590/s0074-02762012000600008

Cited by 10 publications

(13 citation statements)

References 73 publications

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“…Our experiments used PBS and only 48 hours of incubation at RT. It has been reported that the culture media, stage of differentiation, and host are all important in the induction of proteases in nematodes (Rebello et al, 2012), so it the 50 and 56 kDa bands were induced in our conditions but not in those used by Caballero-Garcia et al (2005), even though the culture conditions they utilized were more suitable for the survival and production of the EPS of these larva since they contained more nutrients and the presence of CO2. On the other hand, the ESP showed proteolytic activity at RT against human fibronectin, sheep and human gamma globulins.…”

Section: Resultscontrasting

confidence: 58%

Proteases secreted by Gnathostoma binucleatum degrade fibronectin and antibodies from mammals

Vibanco-Pérez¹,

Durán‐Avelar²,

Zambrano‐Zaragoza³

et al. 2015

Helminthologia

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SummaryGnathostomiasis is a prevalent zoonosis in humans in some regions of the world. The genus Gnathostoma is considered an accidental parasite for humans; G. binucleatum is the endemic species in Nayarit, Mexico. This work was designed to determine the proteolytic activity of the excretory-secretory products (ESP) of advanced third-stage larvae (ADVL3) of Gnathostoma binucleatum against human fibronectin and antibodies from human and sheep. Our findings showed protease activity against human fibronectin as well as sheep and human gamma globulins of the ESP at molecular weights of 80 and 56 kDa. The proteases found in the ESP of G. binucleatum are thus candidate molecules for consideration as pathogenic elements, owing to the fact that they destroy proteins of the host tissue, which probably allows them to migrate through those tissues and degrade molecules involved in the humoral immune response.

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Section: Resultscontrasting

confidence: 58%

Proteases secreted by Gnathostoma binucleatum degrade fibronectin and antibodies from mammals

Vibanco-Pérez¹,

Durán‐Avelar²,

Zambrano‐Zaragoza³

et al. 2015

Helminthologia

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“…Indeed these molecules are not as redundant as mammalian ones could be [15, 38]. In addition, it remains to be determined if any proteinase(s) contained in TES might act towards hemoglobin, a major blood component, albeit hemoglobinolytic activities in helminths extracts are more easily detected using in solution assays than in gel ones and aspartic-type proteinases are more likely related to these activities [39]. However the virtually exclusive presence of serine proteinases in TES would be related to the restricted host specificity of T. canis (dogs and humans) as compared to other nematode organisms with lack of host specificity such as Trichinella spiralis where the ES products from infective larvae contain serine, aspartic, cysteine, and metalloproteinases [40].…”

Section: Discussionmentioning

confidence: 99%

Proteinases in Excretory-Secretory Products ofToxocara canisSecond-Stage Larvae: Zymography and Modeling Insights

González-Páez

Arenzana-Seisdedos

García-Tovar

et al. 2014

BioMed Research International

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Components released in excretory-secretory products of Toxocara canis larvae (TES) include phosphatidylethanolamine-binding proteins (TES26), mucins (TES120, MUC2-5), and C-type lectins (TES32, TES70) and their biochemical, immunological, and diagnostic properties have been extensively studied albeit proteinase activities towards physiological substrates are almost unknown. Proteolytic activities in TES samples were first analyzed by gel electrophoresis with gelatin as substrate. Major activities of ~400, 120, and 32 kDa in TES were relatively similar over a broad pH range (5.5–9.0) and all these were of the serine-type as leupeptin abolished gelatinolysis. Further, the ~400 kDa component degraded all physiological substrates tested (laminin, fibronectin, albumin, and goat IgG) and the 120 kDa component degraded albumin and goat IgG while proteinases of lower MW (45, 32, and 26 kDa) only degraded laminin and fibronectin, preferentially at alkaline pH (9.0). By protein modeling approaches using the known sequences of TES components, only TES26 and MUC4 displayed folding patterns significantly related to reference serine proteinases. These data suggest that most of serine proteinase activities secreted in vitro by infective larvae of T. canis have intriguing nature but otherwise help the parasite to affect multiple components of somatic organs and bodily fluids within the infected host.

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“…In addition according to McKerrow et al (2006) and Rebello et al (2012), these are key molecules for invasion of the host by the helminth during the infective larval stage; they are considered major virulence factors for the establishment and maintenance of an infection. The proteolytic enzymes assist in the evasion of the host immune system by degrading the mucus barrier of the gastrointestinal tract, preventing blood coagulation, facilitating the feeding process, and aiding in the invasion of connective tissue (McKerrow, 1989; Dzik, 2006; Hasnain et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Proteomic profile of Ortleppascaris sp.: A helminth parasite of Rhinella marina in the Amazonian region

Silva

Furtado

Santos

2014

International Journal for Parasitology: Parasites and Wildlife

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Proteolytic activity in the adult and larval stages of the human roundworm parasite Angiostrongylus costaricensis

Cited by 10 publications

References 73 publications

Proteases secreted by Gnathostoma binucleatum degrade fibronectin and antibodies from mammals

Proteases secreted by Gnathostoma binucleatum degrade fibronectin and antibodies from mammals

Proteinases in Excretory-Secretory Products ofToxocara canisSecond-Stage Larvae: Zymography and Modeling Insights

Proteomic profile of Ortleppascaris sp.: A helminth parasite of Rhinella marina in the Amazonian region

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