The interaction of<i>Trypanosoma congolense</i>with endothelial cells

Hemphill, Andrew; Frame, I. A.; Ross, C. A.

doi:10.1017/s0031182000076514

Cited by 37 publications

(28 citation statements)

References 31 publications

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“…Here, proteins involved in host cell adhesion are unknown. It has been hypothesized that candidates should bind to sugars 9, but this has to be experimentally proven. Concerning T. b. brucei , it is even more complicated.…”

Section: Discussionmentioning

confidence: 99%

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A multigene family encoding surface glycoproteins in Trypanosoma congolense

2017

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Trypanosoma congolense, the causative agent of the most important livestock disease in Africa, expresses specific surface proteins involved in its parasitic lifestyle. Unfortunately, the complete repertoire of such molecules is far from being deciphered. As these membrane components are exposed to the host environment, they could be used as therapeutic or diagnostic targets. By mining the T. congolense genome database, we identified a novel family of lectin-like glycoproteins (TcoClecs). These molecules are predicted to have a transmembrane domain, a tandem repeat amino acid motif, a signal peptide and a C-type lectin-like domain (CTLD). This paper depicts several experimental arguments in favor of a surface localization in bloodstream forms of T. congolense. A TcoClec gene was heterologously expressed in U-2 OS cells and the product could be partially found at the plasma membrane. TcoClecs were also localized at the surface of T. congolense bloodstream forms. The signal was suppressed when the cells were treated with a detergent to remove the plasma membrane or with trypsin to « shave » the parasites and remove their external proteins. This suggests that TcoClecs could be potential diagnostic or therapeutic antigens of African animal trypanosomiasis. The potential role of these proteins in T. congolense as well as in other trypanosomatids is discussed.

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Section: Discussionmentioning

confidence: 99%

“…In the mammalian host, T. congolense adheres to endothelial cells and red blood cells, whereas T. b. brucei does not 9. Interestingly, in vitro T. congolense BSF adhere directly to the flask but not T. b. brucei .…”

Section: Introductionmentioning

confidence: 98%

A multigene family encoding surface glycoproteins in Trypanosoma congolense

2017

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“…In the vertebrate host, T. congolense parasites remain confined to the vascular system, where they bind to circulating erythrocytes (Banks, 1979) and to endothelial cells (Hemphill et al 1994) through their flagellum, causing damage at the adhesion site (Banks, 1980). Attachment of the bloodstream form is also observed in in vitro culture, where parasites adhere to the bottom of the flask, a phenotype unique to T. congolense among trypanosome species (Coustou et al 2010).…”

Section: Animal Trypanosome Species: Virulence Tissue Distibution Bmentioning

confidence: 99%

The animal trypanosomiases and their chemotherapy: a review

et al. 2016

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SUMMARYPathogenic animal trypanosomes affecting livestock have represented a major constraint to agricultural development in Africa for centuries, and their negative economic impact is increasing in South America and Asia. Chemotherapy and chemoprophylaxis represent the main means of control. However, research into new trypanocides has remained inadequate for decades, leading to a situation where the few compounds available are losing efficacy due to the emergence of drug-resistant parasites. In this review, we provide a comprehensive overview of the current options available for the treatment and prophylaxis of the animal trypanosomiases, with a special focus on the problem of resistance. The key issues surrounding the main economically important animal trypanosome species and the diseases they cause are also presented. As new investment becomes available to develop improved tools to control the animal trypanosomiases, we stress that efforts should be directed towards a better understanding of the biology of the relevant parasite species and strains, to identify new drug targets and interrogate resistance mechanisms.

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“…The coverslips were then washed three times with ice-cold PBS and fixed in 3% paraformaldehyde-0.5% glutaraldehyde in 100 mM phosphate buffer for 1 h at 4°C. Subsequently, free aldehyde groups were blocked by incubation in 120 mM ethanolamine (pH 8) at 4°C overnight (23).…”

Section: Methodsmentioning

confidence: 99%

Neospora caninum Microneme Protein NcMIC3: Secretion, Subcellular Localization, and Functional Involvement in Host Cell Interaction

et al. 2001

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In apicomplexan parasites, host cell adhesion and subsequent invasion involve the sequential release of molecules originating from secretory organelles named micronemes, rhoptries, and dense granules. Microneme proteins have been shown to be released at the onset of the initial contact between the parasite and the host cell and thus mediate and establish the physical interaction between the parasite and the host cell surface. This interaction most likely involves adhesive domains found within the polypeptide sequences of most microneme proteins identified to date. NcMIC3 is a microneme-associated protein found in Neospora caninum tachyzoites and bradyzoites, and a large portion of this protein is comprised of a stretch of four consecutive epidermal growth factor (EGF)-like domains. We determined the subcellular localization of NcMIC3 prior to and following host cell invasion and found that NcMIC3 was secreted onto the tachyzoite surface immediately following host cell lysis in a temperature-dependent manner. Surface-exposed NcMIC3 could be detected up to 2 to 3 h following host cell invasion, and at later time points the distribution of the protein was again restricted to the micronemes. In vitro secretion assays using purified tachyzoites showed that following secretion onto the surface, NcMIC3 was largely translocated towards the posterior end of the parasite, employing a mechanism which requires a functional actin microfilament system. Following this, the protein remained bound to the parasite surface, since it could not be detected in a soluble form in respective culture supernatants. Secretion of NcMIC3 onto the surface resulted in an outward exposure of the EGF-like domains and coincided with an increased capacity of N. caninum tachyzoites to adhere to Vero cell monolayers in vitro, a capacity which could be inhibited by addition of antibodies directed against the EGF-like domains. NcMIC3 is a prominent component of Triton X-100 lysates of tachyzoites, and cosedimentation assays employing prefixed Vero cells showed that the protein binds to the Vero cell surface. In addition, the EGF-like domains, expressed as recombinant proteins in Escherichia coli, also interacted with the Vero cell surface, while binding of NcSRS2 and NcSAG1, the major immunodominant surface antigens, was not as efficient. Our data are indicative of a functional role of NcMIC3 in host cell infection.Neospora caninum was isolated in 1988 by Dubey and colleagues from a dog suffering from severe neuromuscular disorders (18). Subsequently, extensive investigations (reviewed in references 19 and 29) showed that N. caninum represents the most important causative agent of bovine abortion worldwide. More recently, a second species in the genus Neospora was discovered, Neospora hughesi, which causes equine protozoal myeloencephalitis (34). Although N. caninum and N. hughesi exhibit many similarities to Toxoplasma gondii and the phylogenetic status of the genus Neospora is still a matter of discussion, several studies have now confirmed that N. ...

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The interaction ofTrypanosoma congolensewith endothelial cells

Cited by 37 publications

References 31 publications

A multigene family encoding surface glycoproteins in Trypanosoma congolense

A multigene family encoding surface glycoproteins in Trypanosoma congolense

The animal trypanosomiases and their chemotherapy: a review

Neospora caninum Microneme Protein NcMIC3: Secretion, Subcellular Localization, and Functional Involvement in Host Cell Interaction

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