Echinococcus granulosus:An Intraperitoneal Diffusion Chamber Model of Secondary Infection in Mice

Breijo, Martı́n; Spinelli, Pablo; Sim, Robert B.; Ferreira, Ana Maria da Costa

doi:10.1006/expr.1998.4338

Cited by 20 publications

(20 citation statements)

References 15 publications

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“…Also, the spectrum of inflammatory conditions observed in hydatid disease is not reproduced in this model, in which resolution is always observed (Richards et al 1983;Breijo et al 1998). In addition, as mentioned, rodents do not encode S100A12 in their genomes.…”

Section: R E S U L T Smentioning

confidence: 83%

Phagocyte-specific S100 proteins in the local response to theEchinococcus granulosuslarva

et al. 2012

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SUMMARYInfection by larvalEchinococcus granulosusis usually characterized by tight inflammatory control. However, various degrees of chronic granulomatous inflammation are also observed, reaching a high point in infection of cattle by the most prevalent parasite strain worldwide, which is not well adapted to this host species. In this context, epithelioid and multinucleated giant macrophages surround the parasite, and the secreted products of these cells often associate with the larval wall. The phagocyte-specific S100 proteins, S100A8, S100A9 and S100A12, are important non-conventionally secreted amplifiers of inflammatory responses. We have analysed by proteomics and immunohistochemistry the presence of these proteins at theE. granulosuslarva-host interface. We found that, in the context of inflammatory control as observed in human infections, the S100 proteins are not abundant, but S100A9 and S100A8 can be expressed by eosinophils distal to the parasite. In the granulomatous inflammation context as observed in cattle infections, we found that S100A12 is one of the most abundant host-derived, parasite-associated proteins, while S100A9 and S100A8 are not present at similarly high levels. As expected, S100A12 derives mostly from the epithelioid and multinucleated giant cells. S100A12, as well as cathepsin K and matrix metalloproteinase-9, also expressed byE. granulosus-elicited epithelioid cells, are connected to the Th17 arm of immunity, which may therefore be involved in this granulomatous response.

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Section: R E S U L T Smentioning

confidence: 83%

Phagocyte-specific S100 proteins in the local response to theEchinococcus granulosuslarva

et al. 2012

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“…Although protoscoleces are not directly exposed to the intermediate host in the hydatid cyst, their surface proteins are accessible to interaction with host molecules that permeate the cyst and can become directly accessible for interactions with host tissues upon cyst rupture and consequent cyst content leakage. In this later scenario, protoscolex tegumental proteins are assumed to be important for the recognition of host molecules and mediate the activation of signaling pathways involved in dedifferentiation of protoscoleces into secondary hydatid cysts (Breijo et al, 1998). Similarly, upon ingestion by the definitive host, tegumental proteins are likely to be important for protoscolex fixation in the small intestine and differentiation into the adult worm.…”

Section: Discussionmentioning

confidence: 98%

Fructose-bisphosphate aldolase and enolase from Echinococcus granulosus: Genes, expression patterns and protein interactions of two potential moonlighting proteins

Lorenzatto

Monteiro

Paredes

et al. 2012

Gene

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Glycolytic enzymes, such as fructose-bisphosphate aldolase (FBA) and enolase, have been described as complex multifunctional proteins that may perform non-glycolytic moonlighting functions, but little is known about such functions, especially in parasites. We have carried out in silico genomic searches in order to identify FBA and enolase coding sequences in Echinococcus granulosus, the causative agent of cystic hydatid disease. Four FBA genes and 3 enolase genes were found, and their sequences and exon-intron structures were characterized and compared to those of their orthologs in Echinococcus multilocularis, the causative agent of alveolar hydatid disease. To gather evidence of possible non-glycolytic functions, the expression profile of FBA and enolase isoforms detected in the E. granulosus pathogenic larval form (hydatid cyst) (EgFBA1 and EgEno1) was assessed. Using specific antibodies, EgFBA1 and EgEno1 were detected in protoscolex and germinal layer cells, as expected, but they were also found in the hydatid fluid, which contains parasite's excretory-secretory (ES) products. Besides, both proteins were found in protoscolex tegument and in vitro ES products, further suggesting possible non-glycolytic functions in the host-parasite interface. EgFBA1 modeled 3D structure predicted a F-actin binding site, and the ability of EgFBA1 to bind actin was confirmed experimentally, which was taken as an additional evidence of FBA multifunctionality in E. granulosus. Overall, our results represent the first experimental evidences of alternative functions performed by glycolytic enzymes in E. granulosus and provide relevant information for the understanding of their roles in host-parasite interplay.

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“…Using Balb/c mice strain, secondary cystic echinococcosis can be divided into two stages: an early stage (until day 20–30 pi) in which the infection establishes (protoscoleces develop into hydatid cysts) [7], followed by a late or chronic stage in which already differentiated cysts grow and eventually become fertile cysts. There is scarce information regarding early immune responses in the peritoneal cavity of infected mice [8]–[10]. Breijo et al .…”

Section: Introductionmentioning

confidence: 99%

Early Peritoneal Immune Response during Echinococcus granulosus Establishment Displays a Biphasic Behavior

et al. 2011

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BackgroundCystic echinococcosis is a worldwide distributed helminth zoonosis caused by the larval stage of Echinococcus granulosus. Human secondary cystic echinococcosis is caused by dissemination of protoscoleces after accidental rupture of fertile cysts and is due to protoscoleces ability to develop into new metacestodes. In the experimental model of secondary cystic echinococcosis mice react against protoscoleces producing inefficient immune responses, allowing parasites to develop into cysts. Although the chronic phase of infection has been analyzed in depth, early immune responses at the site of infection establishment, e.g., peritoneal cavity, have not been well studied. Because during early stages of infection parasites are thought to be more susceptible to immune attack, this work focused on the study of cellular and molecular events triggered early in the peritoneal cavity of infected mice.Principal FindingsData obtained showed disparate behaviors among subpopulations within the peritoneal lymphoid compartment. Regarding B cells, there is an active molecular process of plasma cell differentiation accompanied by significant local production of specific IgM and IgG2b antibodies. In addition, peritoneal NK cells showed a rapid increase with a significant percentage of activated cells. Peritoneal T cells showed a substantial increase, with predominance in CD4+ T lymphocytes. There was also a local increase in Treg cells. Finally, cytokine response showed local biphasic kinetics: an early predominant induction of Th1-type cytokines (IFN-γ, IL-2 and IL-15), followed by a shift toward a Th2-type profile (IL-4, IL-5, IL-6, IL-10 and IL-13).ConclusionsResults reported here open new ways to investigate the involvement of immune effectors players in E. granulosus establishment, and also in the sequential promotion of Th1- toward Th2-type responses in experimental secondary cystic echinococcosis. These data would be relevant for designing rational therapies based on stimulation of effective responses and blockade of evasion mechanisms.

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Echinococcus granulosus:An Intraperitoneal Diffusion Chamber Model of Secondary Infection in Mice

Cited by 20 publications

References 15 publications

Phagocyte-specific S100 proteins in the local response to theEchinococcus granulosuslarva

Phagocyte-specific S100 proteins in the local response to theEchinococcus granulosuslarva

Fructose-bisphosphate aldolase and enolase from Echinococcus granulosus: Genes, expression patterns and protein interactions of two potential moonlighting proteins

Early Peritoneal Immune Response during Echinococcus granulosus Establishment Displays a Biphasic Behavior

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