Parasites, Hosts and Diseases

"immunoglobulin"

Original Articles

Alterations in immunized antigens of Anisakis pegreffii by ampicillin-induced gut microbiome changes in mice: Myungjun Kim, Jun Ho Choi, Myung-hee Yi, Singeun Oh, Tai-Soon Yong, Ju Yeong Kim; Parasites Hosts Dis 2024;62(3):351-364.
Published online August 26, 2024; DOI: https://doi.org/10.3347/PHD.23114

Abstract
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The gut microbiome plays an essential role in host immune responses, including allergic reactions. However, commensal gut microbiota is extremely sensitive to antibiotics and excessive usage can cause microbial dysbiosis. Herein, we investigated how changes in the gut microbiome induced by ampicillin affected the production of IgG1 and IgG2a antibodies in mice subsequently exposed to Anisakis pegreffii antigens. Ampicillin treatment caused a notable change in the gut microbiome as shown by changes in both alpha and beta diversity indexes. In a 1-dimensional immunoblot using Anisakis-specific anti-mouse IgG1, a 56-kDa band corresponding to an unnamed Anisakis protein was detected using mass spectrometry analysis only in ampicillin-treated mice. In the Anisakis-specific anti-mouse IgG2a-probed immunoblot, a 70-kDa band corresponding to heat shock protein 70 (HSP70) was only detected in ampicillin-treated and Anisakis-immunized mice. A 2-dimensional immunoblot against Anisakis extract with immunized mouse sera demonstrated altered spot patterns in both groups. Our results showed that ampicillin treatment altered the gut microbiome composition in mice, changing the immunization response to antigens from A. pegreffii. This research could serve as a basis for developing vaccines or allergy immunotherapies against parasitic infections.

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Effect of Diclazuril on the Bursa of Fabricius Morphology and SIgA Expression in Chickens Infected with Eimeria tenella: Bian-hua Zhou, Li-li Liu, Jeffrey Liu, Fu-wei Yuan, Er-jie Tian, Hong-wei Wang; Korean J Parasitol 2015;53(6):675-682.
Published online December 31, 2015; DOI: https://doi.org/10.3347/kjp.2015.53.6.675

Abstract
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The effects of diclazuril on the bursa of Fabricius (BF) structure and secretory IgA (SIgA) expression in chickens infected with Eimeria tenella were examined. The morphology of the BF was observed by hematoxylin and eosin staining, while ultrastructural changes were monitored by transmission electron microscopy. E. tenella infection caused the BF cell volumes to decrease, irregularly arranged, as well as, enlargement of the intercellular space. Diclazuril treatment alleviated the physical signs of damages associated with E. tenella infection. The SIgA expression in BF was analyzed by immunohistochemistry technique. The SIgA expression increased significantly by 350.4% (P<0.01) after E. tenella infection compared to the normal control group. With the treatment of diclazuril, the SIgA was relatively fewer in the cortex, and the expression level was significantly decreased by 46.7% (P<0.01) compared with the infected and untreated group. In conclusion, E. tenella infection in chickens induced obvious harmful changes in BF morphological structure and stimulated the expression of SIgA in the BF. Diclazuril treatment effectively alleviated the morphological changes. This result demonstrates a method to develop an immunological strategy in coccidiosis control.

Citations

Citations to this article as recorded by

Experimental Eimeria tenella infection of chickens followed by very virulent infectious bursal disease viral challenge: clinical and pathological effects
Nahed A. El-Shall, Mahmoud E. Sedeik, Heba M. Ismail, Ashraf M. Awad
Avian Pathology.2026; 55(1): 38. CrossRef
Identification of differentially expressed genes and metabolism signaling pathway in the spleen of broilers supplemented with probiotic Bacillus spp.
Anh Duc Truong, Ha Thi Thanh Tran, Huyen Thi Nguyen, Nhu Thi Chu, Lanh Phan, Hoai Thi Phan, Ngoc Thi Pham, Van Hai Nguyen, Lan Huong Nguyen, Dang Kim Pham, Phu- Ha Ho, Hoang Vu Dang
Veterinary Immunology and Immunopathology.2024; 272: 110755. CrossRef
Efficacy and safety of diclazuril nanoemulsion in control of Eimeria tenella in broilers
Azza A. El-Sawah, Shawky M. Aboelhadid, El-Shymaa N. El-Nahass, Hassan E. Helal
BMC Veterinary Research.2024;[Epub] CrossRef
Diclazuril-induced expression of CDK-related kinase 2 in the second-generation merozoites of Eimeria tenella
Bian-hua Zhou, Hai-yan Ding, Jing-yun Yang, Jun Chai, Hong-wei Guo, Er-jie Tian
Molecular and Biochemical Parasitology.2023; 255: 111575. CrossRef
Ameliorative effect of yeast cell walls on broiler chickens' performance and gut health under coccidiosis challenge
Shawkat Abdulrazaq M'Sadeq
Czech Journal of Animal Science.2023; 68(8): 346. CrossRef
In Vivo Recovery of Bacteriophages and Their Effects on Clostridium perfringens-Infected Broiler Chickens
Hyun-Gwan Lee, Yoo-Bhin Kim, Sang-Hyeok Lee, Jun-Ok Moon, Jong-Pyo Chae, Yu-Jin Kim, Kyung-Woo Lee
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EFFECTS OF ZN2+- AND CR3+-MODIFIED PALYGORSKITE ON THE TREATMENT OF EIMERIA TENELLA
D.W. Yao, F.M. Khand, Y Xu, Q.Q. Shen, Y Wang, D.J. Yang
The Journal of Animal and Plant Sciences.2022; 32(2): 397. CrossRef
Prolonging and enhancing the protective efficacy of the EtMIC3-C-MAR against eimeria tenella through delivered by attenuated salmonella typhimurium
Ningning Zhao, Junfeng Lv, Yaru Lu, Yingying Jiang, Hongmei Li, Yumin Liu, Xiao Zhang, Xiaomin Zhao
Veterinary Parasitology.2020; 279: 109061. CrossRef
Efficacy of probiotic Enterococcus faecium in combination with diclazuril against coccidiosis in experimentally infected broilers
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Combination of purine and pyrimidine nucleosides influences growth performance, gut morphology, digestive enzymes, serum biochemical indices and immune functions in broiler chickens
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Analysis of Differentially Expressed Genes in Necrotic Enteritis-infected Fayoumi Chickens using RNA Sequencing
Anh Duc Truong, Yeojin Hong, Jihye Ban, Boyeong Park, Thanh C. Hoang, Yeong H. Hong, Hyun S. Lillehoj
The Journal of Poultry Science.2017; 54(2): 121. CrossRef
Effect of purine nucleosides on growth performance, gut morphology, digestive enzymes, serum profile and immune response in broiler chickens
A. Daneshmand, Hassan Kermanshahi, M. Danesh Mesgaran, A. J. King, S. A. Ibrahim
British Poultry Science.2017; 58(5): 536. CrossRef
Effects of pyrimidine nucleosides on growth performance, gut morphology, digestive enzymes, serum biochemical indices and immune response in broiler chickens
A. Daneshmand, H. Kermanshahi, M. Danesh Mesgaran, A.J. King, S.A. Ibrahim
Livestock Science.2017; 204: 1. CrossRef

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Brief Communication

Antibody Responses in Sera of Different Mouse Strains Experimentally Infected with Neodiplostomum seoulense: Eun-Taek Han, Jun-Hu Chen, Jong-Yil Chai; Korean J Parasitol 2008;46(4):279-283.
Published online December 20, 2008; DOI: https://doi.org/10.3347/kjp.2008.46.4.279

Abstract
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To examine humoral immune responses in the host, we measured serum antibody levels in different strains of mice (ICR, BALB/c, and C3H) experimentally infected with Neodiplostomum seoulense. Specific IgG antibody levels were increased remarkably with little difference among 3 strains of mice infected with N. seoulense from day 7 to 35 post-infection. More target proteins of adult parasites reacted with IgG at the time when the worm recovery decreased compared with other times. More than 20 protein bands, from 14 kDa to 94 kDa in size, were separated from the crude antigen of N. seoulense adults by SDS-PAGE, and among them 26, 30, 35, 43, 54, 67, and 94 kDa proteins were the major antigenic proteins. The results suggest that significant IgG antibody responses occur against N. seoulense in mice and this may be related with expulsion of worms.

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Foodborne Intestinal Flukes in Southeast Asia
Jong-Yil Chai, Eun-Hee Shin, Soon-Hyung Lee, Han-Jong Rim
The Korean Journal of Parasitology.2009; 47(Suppl): S69. CrossRef

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Original Articles

Degradation of immunoglobulins, protease inhibitors, and interleukin-1 by a secretory proteinase of Acanthamoeba castellanii: Byoung-Kuk Na, Jong-Hwa Cho, Chul-Yong Song, Tong-Soo Kim; Korean J Parasitol 2002;40(2):93-99.
Published online June 30, 2002; DOI: https://doi.org/10.3347/kjp.2002.40.2.93

Abstract
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The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on host's defense-oriented or regulatory proteins such as immunoglobulins, interleukin-1, and protease inhibitors was investigated. The enzyme was found to degrade secretory immunoglobulin A (sIgA), IgG, and IgM. It also degraded interleukin-1α (IL-1α) and IL-1β. Its activity was not inhibited by endogenous protease inhibitors, such as α2-macroglobulin, α1-trypsin inhibitor, and α2-antiplasmin. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of host's defense-oriented or regulatory proteins by the Acanthamoeba proteinase suggested that the enzyme might be an important virulence factor in the pathogenesis of Acanthamoeba infection.

Citations

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A Synthetic View on Acanthamoeba Keratitis Host Immune Response: Potential Factors Influencing the Development of Chronic Inflammation
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Biological characteristics and pathogenicity of Acanthamoeba
Yuehua Wang, Linzhe Jiang, Yitong Zhao, Xiaohong Ju, Le Wang, Liang Jin, Ryan D. Fine, Mingguang Li
Frontiers in Microbiology.2023;[Epub] CrossRef
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Infection and Immunity.2022;[Epub] CrossRef
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Jian-Ming Huang, Yao-Tsung Chang, Min-Hsiu Shih, Wei-Chen Lin, Fu-Chin Huang
Parasitology Research.2019; 118(6): 1865. CrossRef
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Naveed Ahmed Khan, Ayaz Anwar, Ruqaiyyah Siddiqui
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Differential effects of α-helical and β-hairpin antimicrobial peptides against Acanthamoeba castellanii
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Degradations of human immunoglobulins and hemoglobin by a 60 kDa cysteine proteinase of Trichomonas vaginalis: Duk-Young Min, Keun-Hee Hyun, Jae-Sook Ryu, Myoung-Hee Ahn, Myung-Hwan Cho; Korean J Parasitol 1998;36(4):261-268.
Published online December 20, 1998; DOI: https://doi.org/10.3347/kjp.1998.36.4.261

Abstract
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The present study was undertaken to investigate the role of cysteine proteinase of Trichomonas vaginalis in escaping from host defense mechanism. A cysteine proteinase of T. vaginalis was purified by affinity chromatography and gel filtration. Optimum pH for the purified proteinase activity was 6.0. The proteinase was inhibited by cysteine and serine proteinase inhibitors such as E-64, NEM, IAA, leupeptin, TPCK and TLCK, and also by Hg²⁺, but not affected by serine-, metallo-, and aspartic proteinase inhibitors such as PMSF, EDTA and pepstatin A. However, it was activated by the cysteine proteinase activator, DTT. The molecular weight of a purified proteinase was 62 kDa on gel filtration and 60 kDa on SDS-PAGE. Interestingly, the purified proteinase was able to degrade serum IgA, secretory IgA, and serum IgG in time- and dose-dependent manners. In addition, the enzyme also degraded hemoglobin in a dose-dependent manner. These results suggest that the acidic cysteine proteinase of T. vaginalis may play a dual role for parasite survival in conferring escape from host humoral defense by degradation of immunoglobulins, and in supplying nutrients to parasites by degradation of hemoglobin.

Citations

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Hemoglobin uptake and utilization by human protozoan parasites: a review
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