Molecular Cloning and Characterization of a Paramyosin from Clonorchis sinensis

Park, Tae Joo; Kang, Jung‐Mi; Na, Byoung-Kuk; Sohn, Woon-Mok

doi:10.3347/kjp.2009.47.4.359

Cited by 24 publications

(23 citation statements)

References 41 publications

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“…Tropomyosin found among invertebrates like house dust mites causes allergic reactions and is identified to have homology with the tropomyosins found in parasitic helminthes such as A. suum, Anisakis, Onchocerca and T. spiralis [50]. Paramyosin is found also in numerous invertebrates and in other parasites such as Clonorchis, Schistosoma, Fasciola, Paragonimus, Onchocerca and Anisakis and has been associated with the cross reactions observed between A. lumbricoides and house dust mites [46,51,52]. Another cross-reacting allergen found between Ascaris and dust mites (D. pteronyssinus and B. tropicalis) is glutathione-s-transferase at 23 kD level [41].…”

Section: Discussionmentioning

confidence: 97%

Comparative Immunomodulatory Activity of Ascaris Suum Eggs and Dermatophagoides pteronyssinus Extract in BALB/C Mice: Cytokine and Immunoglobulin Regulations

Ruth¹

2012

J Aller Ther

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Allergy is highly prevalent in well-developed countries; hygiene hypothesis suggests that this is due to exposure to previous bacterial infection eliciting Th1-response that suppresses Th2-mediated responses. Aside from Th2 suppressing Th1-responses, Th2-mediated infections such as parasitism, appear to lower the risk of developing allergy. This study investigates the effects of Ascaris suum infection in Dermatophagoides pteronyssinus-induced allergic BALB/c mice. Ninety BALB/c mice divided into three trials were randomly grouped into: normal control (1), A. suum infected mice (2), D. pteronyssinus exposed mice (3), A. suum infected mice and then exposed to D. pteronyssinus (4), D. pteronyssinus exposed mice and then infected with A. suum (5), and mice exposed and infected with D. pteronyssinus and A. suum, simultaneously (6). Blood and fecal samples were collected at days 0, 36, and 72 for the measurement of cytokines and immunoglobulins through ELISA, and for fecal analysis. Results showed that A. suum infection suppressed D. pteronyssinus-induced allergy morphologically and histologically and downregulated the production of D. pteronyssinus-specific IgE. A. suum and D. pteronyssinus upregulated the production of IL-4 and IL-5, and only A. suum eggs enhanced the production of IL-10. D. pteronyssinus enhanced production of both D. pteronyssinus-specific and A. suum-specific IgE and IgG and may be accounted to crossreacting antigens present in D. pteronyssinus and A. suum. IL-10 is upregulated in mice with A. suum infection and appears to protect mice against D. pteronyssinus-induced allergy. The possible role of IL-10 production in response to A. suum infection and against D. pteronyssinus-induced allergy needs further investigation.

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Section: Discussionmentioning

confidence: 97%

Comparative Immunomodulatory Activity of Ascaris Suum Eggs and Dermatophagoides pteronyssinus Extract in BALB/C Mice: Cytokine and Immunoglobulin Regulations

Ruth¹

2012

J Aller Ther

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“…8a ). Paramyosin, present in numerous invertebrates including helminths, is a muscle protein that plays multifunctional roles in host-parasite relationships [ 25 , 53 ]. The less expressed histopathological changes in B.s -CotC-CsPmy-immunized mice might be due not only to the lower quantity of C. sinensis eggs or adult worms but also to function inhibition of CsPmy by local or humoral anti-CsPmy antibodies including IgG and IgA.…”

Section: Discussionmentioning

confidence: 99%

Bacillus subtilis spore with surface display of paramyosin from Clonorchis sinensis potentializes a promising oral vaccine candidate

et al. 2018

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BackgroundClonorchiasis caused by Clonorchis sinensis has become increasingly prevalent in recent years. Effective prevention strategies are urgently needed to control this food-borne infectious disease. Previous studies indicated that paramyosin of C. sinensis (CsPmy) is a potential vaccine candidate.MethodsWe constructed a recombinant plasmid of PEB03-CotC-CsPmy, transformed it into Bacillus subtilis WB600 strain (B.s-CotC-CsPmy), and confirmed CsPmy expression on the spore surface by SDS-PAGE, Western blotting and immunofluorescence assay. The immune response and protective efficacy of the recombinant spore were investigated in BALB/c mice after intragastrical or intraperitoneal immunization. Additionally, biochemical enzyme activities in sera, the intestinal histopathology and gut microflora of spore-treated mice were investigated.ResultsCsPmy was successfully expressed on the spore surface and the fusion protein on the spore surface with thermostability. Specific IgG in sera and intestinal mucus were increased after intraperitoneal and intragastrical immunization. The sIgA level in intestinal mucus, feces and bile of B.s-CotC-CsPmy orally treated mice were also significantly raised. Furthermore, numerous IgA-secreting cells were detected in intestinal mucosa of intragastrically immunized mice. No inflammatory injury was observed in the intestinal tissues and there was no significant difference in levels of enzyme-indicated liver function among the groups. Additionally, the diversity and abundance of gut microbiota were not changed after oral immunization. Intragastric and intraperitoneal immunization of B.s-CotC-CsPmy spores in mice resulted in egg reduction rates of 48.3 and 51.2% after challenge infection, respectively. Liver fibrosis degree in B.s-CotC-CsPmy spores treated groups was also significantly reduced.ConclusionsCsPmy expressed on the spore surface maintained its immunogenicity. Both intragastrical and intraperitoneal immunization with B.s-CotC-CsPmy spores induced systemic and local mucosal immune response in mice. Although both intragastric and intraperitoneal immunization elicited a similar protective effect, intragastric immunization induced stronger mucosal immune response without side effects to the liver, intestine and gut microbiota, compared with intraperitoneal immunization. Oral immunization with B. subtilis spore expressing CsPmy on the surface was a promising, safe and needle-free vaccination strategy against clonorchiasis.

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“…shellfish species showed greater diversity compared to the other groups of species. Fluke [25] paramyosins showed high sequence similarities within the group, with percentages of 93% or greater. Tapeworm [26] [27] paramyosins also showed high sequence similarities with percentages of 98% or greater.…”

Section: Phylogenetic Analysismentioning

confidence: 99%

cDNA Cloning of Paramyosin from Several Kinds of Squid Mantle Muscle

Kajita¹,

Takeda²,

Yoshida³

et al. 2018

ABB

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Paramyosin is a rod-shaped muscle protein found exclusively in invertebrates, with α-helices coiled around each other to form a coiled-coil structure. Marine organisms in which the primary structure of paramyosin has been determined are mollusks, including abalone (Haliotis discus), mussels (Mytilus galloprovincialis), octopus (Octopus bimaculoides), and oyster (Crassostrea gigas). In contrast, the primary structure of squid paramyosin, which is of particular interest, has yet to be reported. In the present study, cDNA cloning of paramyosins from four squid species, the neon flying squid (Ommastrephes bartramii), the Humboldt squid (Dosidicus gigas), the golden cuttlefish (Sepia esculenta), and the clawed armhook squid (Gonatus onyx), was performed to determine the following: the 2605-bp O. bartramii paramyosin gene containing a 2574-bp open reading frame (ORF), the 2691-bp D. gigas paramyosin gene containing a 2640-bp ORF, the 2631-bp S. esculenta paramyosin gene containing a 2574 ORF, and the 2609-bp G. onyx paramyosin gene containing a 2574-bp ORF. The primary structure of the four squid paramyosins was found to contain heptad repeats and an ACD (assembly competence domain), which are characteristic of a coiled coil. A phylogenetic analysis was performed with paramyosin sequences from species including the four squid species examined in this study, the results of which indicated that the four squid paramyosins form a group independent from the paramyosins of other species, to which octopus paramyosins are closest.

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Molecular Cloning and Characterization of a Paramyosin from Clonorchis sinensis

Cited by 24 publications

References 41 publications

Comparative Immunomodulatory Activity of Ascaris Suum Eggs and Dermatophagoides pteronyssinus Extract in BALB/C Mice: Cytokine and Immunoglobulin Regulations

Comparative Immunomodulatory Activity of Ascaris Suum Eggs and Dermatophagoides pteronyssinus Extract in BALB/C Mice: Cytokine and Immunoglobulin Regulations

Bacillus subtilis spore with surface display of paramyosin from Clonorchis sinensis potentializes a promising oral vaccine candidate

cDNA Cloning of Paramyosin from Several Kinds of Squid Mantle Muscle

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