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Articles by Li Du
Total Records ( 3 ) for Li Du
  Yongchang Hao , Xiaoru Zhang , Donglin Zhang , Ying Cheng , Li Du , Wenhua Kuang , Ming Lei , Hanwei Jiao , Chao Qi and Fengyang Wang
  Brucella sp. are pathogenic bacteria that are internalized by host cells upon activation of cell division cycle 42 (Cdc42) to cause Brucellosis. Buffalo are among the many species that are affected by Brucellosis. The objective of this study was to analyze the expression and distribution of Cdc42 small GTPases in buffalo which may help elucidating the molecular events leading to Brucella internalization. Full-length buffalo Cdc42 mRNA were obtained and real-time quantitative polymerase chain reaction was performed to assess the transcription level of Cdc42 in heart, liver, spleen, lung, kidney and intestine. Western blot was used to determine the level of Cdc42 in heart, liver, spleen, lung, kidney and intestine tissue; immunohistochemistry techniques were applied for evaluating the distribution of Cdc42 in tissue. Cdc42 were found to be expressed in heart, liver, spleen, lung, kidney and intestine tissue and the subcellular localization of Cdc42 was predominantly in the cytoplasma. These data provide important anatomical information on the role of Cdc42 in Brucella internalization in the different buffalo tissue.
  Yongchang Hao , Hanwei Jiao , Li Du , Donglin Zhang , Ying Cheng , Ming Lei , Hui Rong , Jianing Zhang , Xiaoxiao Jia and Fengyang Wang
  Brucellosis is an extremely important disease affecting the health of human and a number of animal species (including buffalo) around the world and Brucellae sp. is the causative agent of brucellosis. The innate immune system is the first line of defense mechanisms that protect hosts from invading Brucella. As an important innate immunity molecule, MyD88 is critical for TLR-mediated activation of the transcription factor NF-κB and the induction of proinflammatory cytokines. To analyze the expression of MyD88 protein and provide new alternatives for elucidating the molecular mechanism of Brucella infection in buffalo, Western blot were performed to assess the expression of MyD88 protein in heart, liver, spleen, lung, kidney and small intestine, immunohistochemistry techniques were applied for evaluating the distribution of MyD88 protein. The results indicated that MyD88 protein are ubiquitously present in all buffalo tissues examined with relatively high levels in lung and relatively low levels in heart and small intestine and the subcellular localization of MyD88 is predominantly cytoplasm and the tissue specificity were observed. These data provide important anatomical information for studying the role of MyD88 played in Brucella infection in the different tissue of buffalo.
  Liang Zhang , Weizhi Liu , Tiancen Hu , Li Du , Cheng Luo , Kaixian Chen , Xu Shen and Hualiang Jiang
  β-Hydroxyacyl-acyl carrier protein dehydratase (FabZ) is an important enzyme for the elongation cycles of both saturated and unsaturated fatty acids biosyntheses in the type II fatty acid biosynthesis system (FAS II) pathway. FabZ has been an essential target for the discovery of compounds effective against pathogenic microbes. In this work, to characterize the catalytic and inhibitory mechanisms of FabZ, the crystal structures of the FabZ of Helicobacter pylori (HpFabZ) and its complexes with two newly discovered inhibitors have been solved. Different from the structures of other bacterial FabZs, HpFabZ contains an extra short two-turn α-helix (α4) between α3 and β3, which plays an important role in shaping the substrate-binding tunnel. Residue Tyr-100 at the entrance of the tunnel adopts either an open or closed conformation in the crystal structure. The crystal structural characterization, the binding affinity determination, and the enzymatic activity assay of the HpFabZ mutant (Y100A) confirm the importance of Tyr-100 in catalytic activity and substrate binding. Residue Phe-83 at the exit tunnel was also refined in two alternative conformations, leading the tunnel to form an L-shape and U-shape. All these data thus contributed much to understanding the catalytic mechanism of HpFabZ. In addition, the co-crystal structures of HpFabZ with its inhibitors have suggested that the enzymatic activity of HpFabZ could be inhibited either by occupying the entrance of the tunnel or plugging the tunnel to prevent the substrate from accessing the active site. Our study has provided some insights into the catalytic and inhibitory mechanisms of FabZ, thus facilitating antibacterial agent development.
 
 
 
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