Paragonimus westermani: biochemical and immunological characterizations of paramyosin |
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Authors: | Zhao Qin-Ping Moon Sung-Ung Na Byoung-Kuk Kim Seon-Hee Cho Shin-Hyeong Lee Hyeong-Woo Kong Yoon Sohn Woon-Mok Jiang Ming-Sen Kim Tong-Soo |
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Affiliation: | Division of Malaria and Parasitic Diseases, National Institute of Health, Korea Centers for Disease Control and Prevention, Seoul 122-701, Republic of Korea. |
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Abstract: | Paramyosin of the helminth parasite is a muscle protein that plays multifunctional roles in host-parasite relationships. In this study, we have cloned a gene encoding Paragonimus westermani paramyosin (PwPmy) and characterized biochemical and immunological properties of the recombinant protein. The recombinant PwPmy (rPwPmy) was shown to bind both human immunoglobulin G (IgG) and collagen. The protein was constitutively expressed in various developmental stages of the parasite and its expression level increased progressively as the parasite matured. Immunohistological analysis revealed that PwPmy was mainly localized in subtegumental muscle, tegument and cells surrounding the oral sucker, intestine, and ovary of the parasite. Sera from patients with paragonimiasis showed antibody reactivity against rPwPmy, and IgG1 and IgG4 were predominant. Immunization of mice with rPwPmy also induced high IgG responses. Biochemical and immunological characterization of PwPmy may provide valuable information for the further study to develop a vaccine or a chemotherapeutic agent for paragonimiasis. |
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Keywords: | Paragonimus westermani Trematode Paramyosin Recombinant protein Localization Stage-specific expression Antibody response P. westermani, Paragonimus westermani PwPmy, P. westermani paramyosin IgG, Immunoglobulin G |
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