Immunocytochemistry of cytoskeletal proteins in adult Schistosoma mansoni

MacGregor, A.; Shore, Sarah J.

doi:10.1016/0020-7519(90)90141-9

Cited by 29 publications

(21 citation statements)

References 27 publications

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“…Similar to these observations are reports describing the presence of muscle-associated proteins in the tegument of Schistosoma mansoni (39,40). Indeed, the tegumental localization of paramyosin was postulated to account for the successful immunization of mice against schistosome infection with the invertebrate muscle protein (39,41,42).…”

Section: Resultssupporting

confidence: 69%

“…Indeed, the tegumental localization of paramyosin was postulated to account for the successful immunization of mice against schistosome infection with the invertebrate muscle protein (39,41,42). Tropomyosin also has been localized to the tegument of S. mansoni by immunocytochemistry (40), but whether it plays a role in the nematode cuticle has not been established. Previous studies from this laboratory have revealed the presence of a lowabundance, cross-reactive 40-kDa antigen in larval secretions (13).…”

Section: Resultsmentioning

confidence: 99%

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Tropomyosin implicated in host protective responses to microfilariae in onchocerciasis

Jenkins

Taylor

Gilvary

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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A cDNA from adult female Onchocerca volvulus encoding the C-terminal portion of a tropomyosin isoform (termed MOv-14) has been shown previously to confer protective immunity in rodent models of onchocerciasis. The full-length sequence (designated Ov-tmy-1) obtained by PCR amplification, codes for a protein of 33 kDa and shares 91% identity with tropomyosins from other nematodes, falling to 57% identity with human ␣-tropomyosin. Ov-TMY-1 migrates with an apparent molecular mass of 42 kDa on SDS͞PAGE and is present in all life-cycle stages, as determined by immunoblotting. Immunogold electron microscopy identified antigenic sites within muscle blocks and the cuticle of microfilariae and infective larvae. Anti-MOv14 antibodies were abundant in mice exhibiting serum-transferable protection against microfilariae conferred by vaccination with a PBSsoluble parasite extract. In contrast, little or no MOv14-specific antibody was present in mice inoculated with live microfilariae, in which resistance is mediated by antibodyindependent mechanisms. In human infections, there was an inverse correlation between anti-tropomyosin IgG levels and densities of microfilariae in the skin. Seropositivity varied with the relative endemicity of infection. An immunodominant B cell epitope within Ov-TMY-1 (AQLLAEEADRKYD) was mapped to the N terminus of the MOv14 protein by using sera from protectively vaccinated mice. Intriguingly, the sequence coincides with an IgE-binding epitope within shrimp tropomyosin, believed to be responsible for hypersensitivity in individuals exhibiting allergy to shellfish. IgG and IgE antibodies reacting with the O. volvulus epitope were detected in human infections. It is concluded that antibody responses to tropomyosin may be important in limiting microfilarial densities in a proportion of individuals with onchocerciasis and have the potential to mediate hypersensitivity reactions to dead microfilariae, raising the possibility of a link with the immunopathology of infection.

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Section: Resultssupporting

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Tropomyosin implicated in host protective responses to microfilariae in onchocerciasis

Jenkins

Taylor

Gilvary

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…Evidence of an apical array of actin beneath the distal cytoplasmic membrane is not forthcoming, although there is evidence of subsurface microfilament-rich protuberances in S. mekongi, another human schistosome of the Lower Mekong River Basin in SE Asia. (57) Immunofluorescence data of the actin-binding molecules tropomyosin and a-actinin suggest both molecules are present in the distal cytoplasm, (47) thereby supporting a notion of a peripheral network of microtubules. Schistosoma mansoni tropomyosin is abundant in tegumentary tubercles and in the subtegumentary cytons and epidermal ridges of miracidia.…”

Section: Structure and Diversitymentioning

confidence: 91%

“…2). (46,47) The cytoplasmic bridges of the tegumentary cytoplasm, however, always possess a peripheral ring of microtubules (Figs. 2, 3).…”

Section: Structure and Diversitymentioning

confidence: 99%

The cytoskeleton and motor proteins of human schistosomes and their roles in surface maintenance and host–parasite interactions

et al. 2004

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Schistosomes are parasitic blood flukes, responsible for significant human disease in tropical and developing nations. Here we review information on the organization of the cytoskeleton and associated motor proteins of schistosomes, with particular reference to the organization of the syncytial tegument, a unique cellular adaptation of these and other neodermatan flatworms. Extensive EST databases show that the molecular constituents of the cytoskeleton and associated molecular systems are likely to be similar to those of other eukaryotes, although there are potentially some molecules unique to schistosomes and platyhelminths. The biology of some components, particular those contributing to host-parasite interactions as well as chemotherapy and immunotherapy are discussed. Unresolved questions in relation to the structure and function of the tegument relate to dynamic organization of the syncytial layer.

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“…Actin belongs to a highly conserved family of proteins found in all eukaryotes and is a critical component of the muscle system (45,46). It was shown to be present on the surface of schistosomula, in the muscle, tegumental tubercles and spines of male and female adult worms (47)(48)(49)(50). The movement of schistosomes is accomplished through welldeveloped muscular arrangements that are mainly facilitated by tubulin and actin molecules (51).…”

Section: Proteomics Analysis Of Schistosoma Japonicummentioning

confidence: 99%

Proteomic Analysis of Schistosoma japonicum Schistosomulum Proteins that are Differentially Expressed Among Hosts Differing in Their Susceptibility to the Infection

Hong

Peng

Jiang

et al. 2011

Molecular & Cellular Proteomics

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Schistosomiasis is a tropical, parasitic disease affecting humans and several animal species. The aim of this study was to identify proteins involved in the growth and survival of the parasitic forms inside a host. Schistosomula of Schistosoma japonicum were isolated from three different hosts: the susceptible BALB/c mice; the Wistar rats, which have a considerably lower susceptibility; and the resistant reed vole, Microtus fortis. Soluble proteins of the schistosomula collected from the above three hosts 10 days postinfection were subjected to two-dimensional difference gel electrophoresis. Comparative proteomic analyses revealed that 39, 21, and 25 protein spots were significantly differentially expressed between schistosomula from mice and rats, mice and reed voles, or rats and reed voles, respectively (ANCOVA, p < 0.05). Further, the protein spots were identified by liquid chromatographytandem MS. Bioinformatics analysis showed that the differentially expressed proteins were essentially those involved in the metabolism of proteins, ribonucleotides, or carbohydrates, or in stress response or cellular movement. This study represents the first attempt at profiling S.

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Immunocytochemistry of cytoskeletal proteins in adult Schistosoma mansoni

Cited by 29 publications

References 27 publications

Tropomyosin implicated in host protective responses to microfilariae in onchocerciasis

Tropomyosin implicated in host protective responses to microfilariae in onchocerciasis

The cytoskeleton and motor proteins of human schistosomes and their roles in surface maintenance and host–parasite interactions

Proteomic Analysis of Schistosoma japonicum Schistosomulum Proteins that are Differentially Expressed Among Hosts Differing in Their Susceptibility to the Infection

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