Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics
The plerocercoid of <i>Spirometra mansoni</i> can parasitize both human and animals, resulting in sparganosis. Lactate dehydrogenase (LDH) is an important enzyme in parasites. However, our knowledge of the LDH family in <i>S. mansoni</i> is still inadequate. This work identif...
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MDPI AG
2023-11-01
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| author | Shasha Liu Ke Zhou Fei Gao Wen Li Zhongquan Wang Xi Zhang |
| author_facet | Shasha Liu Ke Zhou Fei Gao Wen Li Zhongquan Wang Xi Zhang |
| author_sort | Shasha Liu |
| collection | DOAJ |
| description | The plerocercoid of <i>Spirometra mansoni</i> can parasitize both human and animals, resulting in sparganosis. Lactate dehydrogenase (LDH) is an important enzyme in parasites. However, our knowledge of the LDH family in <i>S. mansoni</i> is still inadequate. This work identified 19 new LDH members in <i>S. mansoni</i>. Clustering analysis demonstrated that all <i>Sm</i>LDHs were divided into two main groups, which is consistent with the patterns of conserved motif organization. According to RT-qPCR, 2 LDHs were highly expressed in the plerocercoid stage and 17 LDHs were highly expressed in the adult stage. The evolutionary tree showed a high level of diversity of both cestode and trematode LDHs. <i>Sm</i>LDHs contained both conserved family members and members in the process of further diversification. r<i>Sm</i>LDH has a NAD-binding domain and a substrate-binding domain. The protein was immunolocalized in the epidermis of the pleroceroid and in the tegument, uterus and egg shell of adult worms. The optimum activity for r<i>Sm</i>LDH in the pyruvate reduction reaction was found to be pH 4.5 and 37 °C. In the oxidation reaction, optimal values for pH and temperature were 9.0 and 30 °C, respectively. Gossypol was found to be the most powerful inhibitor in both reduction and oxidation reactions. The results provide a basis for the further study of the biological roles of LDHs in <i>S. mansoni</i> and other LDH-containing taxa. |
| first_indexed | 2024-03-09T01:55:53Z |
| format | Article |
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| issn | 2076-2615 |
| language | English |
| last_indexed | 2024-03-09T01:55:53Z |
| publishDate | 2023-11-01 |
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| series | Animals |
| spelling | doaj.art-95d3b4e07edb476482f335504d59693e2023-12-08T15:10:32ZengMDPI AGAnimals2076-26152023-11-011323364210.3390/ani13233642Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular CharacteristicsShasha Liu0Ke Zhou1Fei Gao2Wen Li3Zhongquan Wang4Xi Zhang5Department of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, ChinaDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, ChinaDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, ChinaDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, ChinaDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, ChinaDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, ChinaThe plerocercoid of <i>Spirometra mansoni</i> can parasitize both human and animals, resulting in sparganosis. Lactate dehydrogenase (LDH) is an important enzyme in parasites. However, our knowledge of the LDH family in <i>S. mansoni</i> is still inadequate. This work identified 19 new LDH members in <i>S. mansoni</i>. Clustering analysis demonstrated that all <i>Sm</i>LDHs were divided into two main groups, which is consistent with the patterns of conserved motif organization. According to RT-qPCR, 2 LDHs were highly expressed in the plerocercoid stage and 17 LDHs were highly expressed in the adult stage. The evolutionary tree showed a high level of diversity of both cestode and trematode LDHs. <i>Sm</i>LDHs contained both conserved family members and members in the process of further diversification. r<i>Sm</i>LDH has a NAD-binding domain and a substrate-binding domain. The protein was immunolocalized in the epidermis of the pleroceroid and in the tegument, uterus and egg shell of adult worms. The optimum activity for r<i>Sm</i>LDH in the pyruvate reduction reaction was found to be pH 4.5 and 37 °C. In the oxidation reaction, optimal values for pH and temperature were 9.0 and 30 °C, respectively. Gossypol was found to be the most powerful inhibitor in both reduction and oxidation reactions. The results provide a basis for the further study of the biological roles of LDHs in <i>S. mansoni</i> and other LDH-containing taxa.https://www.mdpi.com/2076-2615/13/23/3642cestodelactate dehydrogenaseidentificationphylogenyenzymatic traits |
| spellingShingle | Shasha Liu Ke Zhou Fei Gao Wen Li Zhongquan Wang Xi Zhang Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics Animals cestode lactate dehydrogenase identification phylogeny enzymatic traits |
| title | Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics |
| title_full | Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics |
| title_fullStr | Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics |
| title_full_unstemmed | Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics |
| title_short | Lactate Dehydrogenase Gene Family in <i>Spirometra mansoni</i> (Cestoda: Diphyllobothriidea)—Phylogenetic Patterns and Molecular Characteristics |
| title_sort | lactate dehydrogenase gene family in i spirometra mansoni i cestoda diphyllobothriidea phylogenetic patterns and molecular characteristics |
| topic | cestode lactate dehydrogenase identification phylogeny enzymatic traits |
| url | https://www.mdpi.com/2076-2615/13/23/3642 |
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