Lactate Dehydrogenase Gene Family in Spirometra mansoni (Cestoda: Diphyllobothriidea)-Phylogenetic Patterns and Molecular Characteristics

by Selleckchem | Jan 16 2024

The plerocercoid of Spirometra mansoni 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 S. mansoni is still inadequate. This work identified 19 new LDH members in S. mansoni. Clustering analysis demonstrated that all SmLDHs 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. SmLDHs contained both conserved family members and members in the process of further diversification. rSmLDH 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 rSmLDH 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 S. mansoni and other LDH-containing taxa.

Comments:

It seems like you're summarizing a scientific study or research findings about lactate dehydrogenase (LDH) in Spirometra mansoni, a parasitic organism known to cause sparganosis in humans and animals. The study appears to have identified and characterized 19 new LDH members in S. mansoni and explored their expression patterns, structural features, localization, enzymatic properties, and inhibition.

The key findings from this work seem to be:

1. Identification of 19 new LDH members in S. mansoni, categorized into two main groups based on clustering analysis and conserved motif organization.
2. Varied expression patterns of LDHs across different developmental stages, with two LDHs highly expressed in the plerocercoid stage and 17 LDHs highly expressed in the adult stage.
3. Evolutionary analysis indicating diversity among cestode and trematode LDHs, with some LDHs showing conservation while others undergoing further diversification.
4. Localization of LDH protein (rSmLDH) in specific anatomical structures: in the epidermis of the plerocercoid and in the tegument, uterus, and egg shell of adult worms.
5. Determination of optimal conditions for LDH activity: pH 4.5 and 37 °C for the pyruvate reduction reaction, and pH 9.0 and 30 °C for the oxidation reaction.
6. Identification of gossypol as a potent inhibitor for both reduction and oxidation reactions of LDH.

Overall, this research provides foundational information for understanding the roles of LDHs in S. mansoni and other LDH-containing organisms, potentially offering insights for further studies on the biological functions of LDH in these parasites.