Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen
Abstract The binding and activation of host plasminogen (PLG) by worm surface enolases has been verified to participate in parasite invasion, but the role of this processes during Trichinella spiralis infection has not been clarified. Therefore, the expression and immunolocalization of a T. spiralis...
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| Format: | Article |
| Language: | English |
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BMC
2019-12-01
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| Series: | Veterinary Research |
| Online Access: | https://doi.org/10.1186/s13567-019-0727-y |
| _version_ | 1818384743791591424 |
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| author | Peng Jiang You Jiao Zao Shu Wei Yan Yan Yan Song Dong Min Yang Li Yuan Dai Ruo Dan Liu Xi Zhang Zhong Quan Wang Jing Cui |
| author_facet | Peng Jiang You Jiao Zao Shu Wei Yan Yan Yan Song Dong Min Yang Li Yuan Dai Ruo Dan Liu Xi Zhang Zhong Quan Wang Jing Cui |
| author_sort | Peng Jiang |
| collection | DOAJ |
| description | Abstract The binding and activation of host plasminogen (PLG) by worm surface enolases has been verified to participate in parasite invasion, but the role of this processes during Trichinella spiralis infection has not been clarified. Therefore, the expression and immunolocalization of a T. spiralis enolase (TsENO) and its binding activity with PLG were evaluated in this study. Based on the three-dimensional (3D) molecular model of TsENO, the protein interaction between TsENO and human PLG was analysed by the ZDOCK server. The interacting residues were identified after analysis of the protein–protein interface by bioinformatics techniques. The key interacting residues were confirmed by a series of experiments. The qPCR analysis results demonstrated that Ts-eno was transcribed throughout the whole life cycle of T. spiralis. The immunofluorescence assay (IFA) results confirmed that TsENO was distributed on the T. spiralis surface. The binding assays showed that recombinant TsENO (rTsENO) and native TsENO were able to bind PLG. Four lysine residues (90, 289, 291 and 300) of TsENO were considered to be active residues for PLG interaction. The quadruple mutant (Lys90Ala + Lys289Ala + Lys291Ala + Lys300Ala) TsENO, in which the key lysine residues were substituted with alanine (Ala) residues, exhibited a reduction in PLG binding of nearly 50% (45.37%). These results revealed that TsENO has strong binding activity with human PLG. The four lysine residues (90, 289, 291 and 300) of TsENO play an important role in PLG binding and could accelerate PLG activation and invasion of the host’s intestinal wall by T. spiralis. |
| first_indexed | 2024-12-14T03:27:07Z |
| format | Article |
| id | doaj.art-8c2fe75973254c6b93ded7a744d101c1 |
| institution | Directory Open Access Journal |
| issn | 1297-9716 |
| language | English |
| last_indexed | 2024-12-14T03:27:07Z |
| publishDate | 2019-12-01 |
| publisher | BMC |
| record_format | Article |
| series | Veterinary Research |
| spelling | doaj.art-8c2fe75973254c6b93ded7a744d101c12022-12-21T23:18:51ZengBMCVeterinary Research1297-97162019-12-0150111210.1186/s13567-019-0727-yMolecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogenPeng Jiang0You Jiao Zao1Shu Wei Yan2Yan Yan Song3Dong Min Yang4Li Yuan Dai5Ruo Dan Liu6Xi Zhang7Zhong Quan Wang8Jing Cui9Department of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityDepartment of Parasitology, Medical College, Zhengzhou UniversityAbstract The binding and activation of host plasminogen (PLG) by worm surface enolases has been verified to participate in parasite invasion, but the role of this processes during Trichinella spiralis infection has not been clarified. Therefore, the expression and immunolocalization of a T. spiralis enolase (TsENO) and its binding activity with PLG were evaluated in this study. Based on the three-dimensional (3D) molecular model of TsENO, the protein interaction between TsENO and human PLG was analysed by the ZDOCK server. The interacting residues were identified after analysis of the protein–protein interface by bioinformatics techniques. The key interacting residues were confirmed by a series of experiments. The qPCR analysis results demonstrated that Ts-eno was transcribed throughout the whole life cycle of T. spiralis. The immunofluorescence assay (IFA) results confirmed that TsENO was distributed on the T. spiralis surface. The binding assays showed that recombinant TsENO (rTsENO) and native TsENO were able to bind PLG. Four lysine residues (90, 289, 291 and 300) of TsENO were considered to be active residues for PLG interaction. The quadruple mutant (Lys90Ala + Lys289Ala + Lys291Ala + Lys300Ala) TsENO, in which the key lysine residues were substituted with alanine (Ala) residues, exhibited a reduction in PLG binding of nearly 50% (45.37%). These results revealed that TsENO has strong binding activity with human PLG. The four lysine residues (90, 289, 291 and 300) of TsENO play an important role in PLG binding and could accelerate PLG activation and invasion of the host’s intestinal wall by T. spiralis.https://doi.org/10.1186/s13567-019-0727-y |
| spellingShingle | Peng Jiang You Jiao Zao Shu Wei Yan Yan Yan Song Dong Min Yang Li Yuan Dai Ruo Dan Liu Xi Zhang Zhong Quan Wang Jing Cui Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen Veterinary Research |
| title | Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen |
| title_full | Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen |
| title_fullStr | Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen |
| title_full_unstemmed | Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen |
| title_short | Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen |
| title_sort | molecular characterization of a trichinella spiralis enolase and its interaction with the host s plasminogen |
| url | https://doi.org/10.1186/s13567-019-0727-y |
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