Xiang M

References (8)

Title : NDRG1 facilitates lytic replication of Kaposi's sarcoma-associated herpesvirus by maintaining the stability of the KSHV helicase - Dong_2021_PLoS.Pathog_17_e1009645
Author(s) : Dong L , Dong J , Xiang M , Lei P , Li Z , Zhang F , Sun X , Niu D , Bai L , Lan K
Ref : PLoS Pathog , 17 :e1009645 , 2021
Abstract : The presumed DNA helicase encoded by ORF44 of Kaposi's sarcoma-associated herpesvirus (KSHV) plays a crucial role in unwinding viral double-stranded DNA and initiating DNA replication during lytic reactivation. However, the regulatory mechanism of KSHV ORF44 has not been fully elucidated. In a previous study, we identified that N-Myc downstream regulated gene 1 (NDRG1), a host scaffold protein, facilitates viral genome replication by interacting with proliferating cell nuclear antigen (PCNA) and the latent viral protein latency-associated nuclear antigen (LANA) during viral latency. In the present study, we further demonstrated that NDRG1 can interact with KSHV ORF44 during viral lytic replication. We also found that the mRNA and protein levels of NDRG1 were significantly increased by KSHV ORF50-encoded replication and transcription activator (RTA). Remarkably, knockdown of NDRG1 greatly decreased the protein level of ORF44 and impaired viral lytic replication. Interestingly, NDRG1 enhanced the stability of ORF44 and inhibited its ubiquitin-proteasome-mediated degradation by reducing the polyubiquitination of the lysine residues at positions 79 and 368 in ORF44. In summary, NDRG1 is a novel binding partner of ORF44 and facilitates viral lytic replication by maintaining the stability of ORF44. This study provides new insight into the mechanisms underlying KSHV lytic replication.
ESTHER : Dong_2021_PLoS.Pathog_17_e1009645
PubMedSearch : Dong_2021_PLoS.Pathog_17_e1009645
PubMedID: 34077484
Gene_locus related to this paper: human-NDRG1

Title : High-level expression of codon-optimized Thielavia terrestris cutinase suitable for ester biosynthesis and biodegradation - Duan_2019_Int.J.Biol.Macromol_135_768
Author(s) : Duan X , Jiang Z , Liu Y , Yan Q , Xiang M , Yang S
Ref : Int J Biol Macromol , 135 :768 , 2019
Abstract : A codon-optimized cutinase gene (TtCutopt) from Thielavia terrestris was over-expressed in Pichia pastoris. An extracellular activity reached 10,200U/mL using high cell density fermentation. The optimal pH and temperature of TtCutopt were 7.0 and 50 degrees C, respectively. It displayed high stability over a wide range of pH from 3.0 to 11.0 and up to 85 degrees C. Among tested p-nitrophenyl esters and triglycerides, TtCutopt showed the highest activity towards p-nitrophenyl butyrate and tributyrin, with specificity activity of 2322.4U/mg and 1152.5U/mg, respectively. It was extremely stable in organic solvents and surfactants. TtCutopt efficiently catalyzed the synthesis of butyl butyrate, hexyl butyrate, butyl hexanoate and hexyl hexanoate with esterification efficiency of >95%. Furthermore, it catalyzed the degradation of >90% of dimethyl phthalate, diethyl phthalate, dipropyl phthalate and dibutyl phthalate to release their corresponding monoalkyl phthalates within 24h. Thus, high yield, high stability, and esterification efficiency of TtCutopt make it an attractive candidate for ester biosynthesis and biodegradation.
ESTHER : Duan_2019_Int.J.Biol.Macromol_135_768
PubMedSearch : Duan_2019_Int.J.Biol.Macromol_135_768
PubMedID: 31129216
Gene_locus related to this paper: thite-g2rae6

Title : Biochemical characterization of a novel lipase from Malbranchea cinnamomea suitable for production of lipolyzed milkfat flavor and biodegradation of phthalate esters - Duan_2019_Food.Chem_297_124925
Author(s) : Duan X , Xiang M , Wang L , Yan Q , Yang S , Jiang Z
Ref : Food Chem , 297 :124925 , 2019
Abstract : A novel lipase gene (McLipB) was cloned from a thermophilic fungus Malbranchea cinnamomea and expressed in Pichia pastoris. The deduced amino acid sequence of the lipase (McLipB) shared the highest identity of 46% with the Candida rugosa lipase LIP4. The extracellular lipase activity of 4304 U/mL with protein concentration of 7.7 mg/mL was achieved in a 5-L fermentor. The optimal pH and temperature of McLipB were 7.5 and 40 degreesC, respectively. The lipase showed high specificity towards triglycerides with short and medium chain fatty acids, and had non-position specificity. McLipB hydrolyzed butter to produce mainly butyric acid, hexanoic acid and a small amount of octanoic acid and decanoic acid. Furthermore, it degraded more than 90% dipropyl phthalate, dibutyl phthalate and dihexyl phthalate to their corresponding monoalkyl phthalates. The properties of McLipB indicate that it has great application potential for production of lipolyzed milkfat flavor and biodegradation of phthalate esters.
ESTHER : Duan_2019_Food.Chem_297_124925
PubMedSearch : Duan_2019_Food.Chem_297_124925
PubMedID: 31253266
Gene_locus related to this paper: malci-McLipB

Title : Galanthamine, Plicamine, and Secoplicamine Alkaloids from Zephyranthes candida and Their Anti-acetylcholinesterase and Anti-inflammatory Activities - Zhan_2016_J.Nat.Prod_79_760
Author(s) : Zhan G , Zhou J , Liu R , Liu T , Guo G , Wang J , Xiang M , Xue Y , Luo Z , Zhang Y , Yao G
Ref : Journal of Natural Products , 79 :760 , 2016
Abstract : Sixteen new alkaloids belonging to the galanthamine (1-6), plicamine (7-14), and secoplicamine (15 and 16) classes, together with eight known analogues (17-24), were isolated from Zephyranthes candida. The structures of 1-16 were determined by extensive spectroscopic analyses, and the absolute configurations of 1, 2, 7, 8, and 17 were confirmed by single-crystal X-ray diffraction analysis. The orientation of 3-OCH3 in N-methyl-5,6-dihydroplicane (22) was revised. Alkaloids 3, 12-14, and 18-21 exhibited anti-acetylcholinesterase activities with IC50 values ranging from 0.48 to 168.7 muM. Compounds 10-12, 14, and 16 showed in vitro anti-inflammatory activities with IC50 values ranging from 7.50 to 23.55 muM.
ESTHER : Zhan_2016_J.Nat.Prod_79_760
PubMedSearch : Zhan_2016_J.Nat.Prod_79_760
PubMedID: 26913788

Title : Engineering of Glarea lozoyensis for exclusive production of the pneumocandin B0 precursor of the antifungal drug caspofungin acetate - Chen_2015_Appl.Environ.Microbiol_81_1550
Author(s) : Chen L , Yue Q , Li Y , Niu X , Xiang M , Wang W , Bills GF , Liu X , An Z
Ref : Applied Environmental Microbiology , 81 :1550 , 2015
Abstract : Pneumocandins produced by the fungus Glarea lozoyensis are acylated cyclic hexapeptides of the echinocandin family. Pneumocandin B0 is the starting molecule for the first semisynthetic echinocandin antifungal drug, caspofungin acetate. In the wild-type strain, pneumocandin B0 is a minor fermentation product, and its industrial production was achieved by a combination of extensive mutation and medium optimization. The pneumocandin biosynthetic gene cluster was previously elucidated by a whole-genome sequencing approach. Knowledge of the biosynthetic cluster suggested an alternative way to produce exclusively pneumocandin B0. Disruption of GLOXY4, encoding a nonheme, alpha-ketoglutarate-dependent oxygenase, confirmed its involvement in l-leucine cyclization to form 4S-methyl-l-proline. The absence of 4S-methyl-l-proline abolishes pneumocandin A0 production, and 3S-hydroxyl-l-proline occupies the hexapeptide core's position 6, resulting in exclusive production of pneumocandin B0. Retrospective analysis of the GLOXY4 gene in a previously isolated pneumocandin B0-exclusive mutant (ATCC 74030) indicated that chemical mutagenesis disrupted the GLOXY4 gene function by introducing two amino acid mutations in GLOXY4. This one-step genetic manipulation can rationally engineer a high-yield production strain.
ESTHER : Chen_2015_Appl.Environ.Microbiol_81_1550
PubMedSearch : Chen_2015_Appl.Environ.Microbiol_81_1550
PubMedID: 25527531
Gene_locus related to this paper: glal2-glon

Title : Genomic and transcriptomic analysis of the endophytic fungus Pestalotiopsis fici reveals its lifestyle and high potential for synthesis of natural products - Wang_2015_BMC.Genomics_16_28
Author(s) : Wang X , Zhang X , Liu L , Xiang M , Wang W , Sun X , Che Y , Guo L , Liu G , Wang C , Yin WB , Stadler M , Liu X
Ref : BMC Genomics , 16 :28 , 2015
Abstract : BACKGROUND: In recent years, the genus Pestalotiopsis is receiving increasing attention, not only because of its economic impact as a plant pathogen but also as a commonly isolated endophyte which is an important source of bioactive natural products. Pestalotiopsis fici Steyaert W106-1/CGMCC3.15140 as an endophyte of tea produces numerous novel secondary metabolites, including chloropupukeananin, a derivative of chlorinated pupukeanane that is first discovered in fungi. Some of them might be important as the drug leads for future pharmaceutics.
RESULTS: Here, we report the genome sequence of the endophytic fungus of tea Pestalotiopsis fici W106-1/CGMCC3.15140. The abundant carbohydrate-active enzymes especially significantly expanding pectinases allow the fungus to utilize the limited intercellular nutrients within the host plants, suggesting adaptation of the fungus to endophytic lifestyle. The P. fici genome encodes a rich set of secondary metabolite synthesis genes, including 27 polyketide synthases (PKSs), 12 non-ribosomal peptide synthases (NRPSs), five dimethylallyl tryptophan synthases, four putative PKS-like enzymes, 15 putative NRPS-like enzymes, 15 terpenoid synthases, seven terpenoid cyclases, seven fatty-acid synthases, and five hybrids of PKS-NRPS. The majority of these core enzymes distributed into 74 secondary metabolite clusters. The putative Diels-Alderase genes have undergone expansion. CONCLUSION: The significant expansion of pectinase encoding genes provides essential insight in the life strategy of endophytes, and richness of gene clusters for secondary metabolites reveals high potential of natural products of endophytic fungi.
ESTHER : Wang_2015_BMC.Genomics_16_28
PubMedSearch : Wang_2015_BMC.Genomics_16_28
PubMedID: 25623211
Gene_locus related to this paper: 9pezi-w3wud0 , 9pezi-w3xja3 , pesfw-w3wz53 , pesfw-w3x341 , pesfw-w3whp0 , pesfw-w3xc39 , pesfw-w3wrn9 , pesfw-pfmab , pesfw-pfmae

Title : Comparative genomics and transcriptomics analyses reveal divergent lifestyle features of nematode endoparasitic fungus Hirsutella minnesotensis - Lai_2014_Genome.Biol.Evol_6_3077
Author(s) : Lai Y , Liu K , Zhang X , Li K , Wang N , Shu C , Wu Y , Wang C , Bushley KE , Xiang M , Liu X
Ref : Genome Biol Evol , 6 :3077 , 2014
Abstract : Hirsutella minnesotensis [Ophiocordycipitaceae (Hypocreales, Ascomycota)] is a dominant endoparasitic fungus by using conidia that adhere to and penetrate the secondary stage juveniles of soybean cyst nematode. Its genome was de novo sequenced and compared with five entomopathogenic fungi in the Hypocreales and three nematode-trapping fungi in the Orbiliales (Ascomycota). The genome of H. minnesotensis is 51.4 Mb and encodes 12,702 genes enriched with transposable elements up to 32%. Phylogenomic analysis revealed that H. minnesotensis was diverged from entomopathogenic fungi in Hypocreales. Genome of H. minnesotensis is similar to those of entomopathogenic fungi to have fewer genes encoding lectins for adhesion and glycoside hydrolases for cellulose degradation, but is different from those of nematode-trapping fungi to possess more genes for protein degradation, signal transduction, and secondary metabolism. Those results indicate that H. minnesotensis has evolved different mechanism for nematode endoparasitism compared with nematode-trapping fungi. Transcriptomics analyses for the time-scale parasitism revealed the upregulations of lectins, secreted proteases and the genes for biosynthesis of secondary metabolites that could be putatively involved in host surface adhesion, cuticle degradation, and host manipulation. Genome and transcriptome analyses provided comprehensive understanding of the evolution and lifestyle of nematode endoparasitism.
ESTHER : Lai_2014_Genome.Biol.Evol_6_3077
PubMedSearch : Lai_2014_Genome.Biol.Evol_6_3077
PubMedID: 25359922
Gene_locus related to this paper: 9hypo-a0a0f7zjg7 , 9hypo-a0a0f7zm48 , 9hypo-a0a0f7zrk5 , 9hypo-a0a0f7ztt4 , 9hypo-a0a0f7ztz3 , 9hypo-a0a0f7zun4 , 9hypo-a0a0f7zus6 , 9hypo-a0a0f7zx75 , 9hypo-a0a0f7zy63 , 9hypo-a0a0f8a122 , 9hypo-a0a0f8a341 , 9hypo-a0a0f8a483 , 9hypo-a0a0f8a644 , 9hypo-a0a0f8a655 , 9hypo-a0a0f8a6k2 , 9hypo-a0a0f7zgk0 , 9hypo-a0a0f7zy10 , 9hypo-a0a0f7zmp5

Title : Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in the fungus Glarea lozoyensis - Chen_2013_BMC.Genomics_14_339
Author(s) : Chen L , Yue Q , Zhang X , Xiang M , Wang C , Li S , Che Y , Ortiz-Lopez FJ , Bills GF , Liu X , An Z
Ref : BMC Genomics , 14 :339 , 2013
Abstract : BACKGROUND: The antifungal therapy caspofungin is a semi-synthetic derivative of pneumocandin B0, a lipohexapeptide produced by the fungus Glarea lozoyensis, and was the first member of the echinocandin class approved for human therapy. The nonribosomal peptide synthetase (NRPS)-polyketide synthases (PKS) gene cluster responsible for pneumocandin biosynthesis from G. lozoyensis has not been elucidated to date. In this study, we report the elucidation of the pneumocandin biosynthetic gene cluster by whole genome sequencing of the G. lozoyensis wild-type strain ATCC 20868.
RESULTS: The pneumocandin biosynthetic gene cluster contains a NRPS (GLNRPS4) and a PKS (GLPKS4) arranged in tandem, two cytochrome P450 monooxygenases, seven other modifying enzymes, and genes for L-homotyrosine biosynthesis, a component of the peptide core. Thus, the pneumocandin biosynthetic gene cluster is significantly more autonomous and organized than that of the recently characterized echinocandin B gene cluster. Disruption mutants of GLNRPS4 and GLPKS4 no longer produced the pneumocandins (A0 and B0), and the Deltaglnrps4 and Deltaglpks4 mutants lost antifungal activity against the human pathogenic fungus Candida albicans. In addition to pneumocandins, the G. lozoyensis genome encodes a rich repertoire of natural product-encoding genes including 24 PKSs, six NRPSs, five PKS-NRPS hybrids, two dimethylallyl tryptophan synthases, and 14 terpene synthases.
CONCLUSIONS: Characterization of the gene cluster provides a blueprint for engineering new pneumocandin derivatives with improved pharmacological properties. Whole genome estimation of the secondary metabolite-encoding genes from G. lozoyensis provides yet another example of the huge potential for drug discovery from natural products from the fungal kingdom.
ESTHER : Chen_2013_BMC.Genomics_14_339
PubMedSearch : Chen_2013_BMC.Genomics_14_339
PubMedID: 23688303
Gene_locus related to this paper: glal2-s3cg73 , glal2-s3d2r4 , glal2-s3dmm6 , glal2-s3e306 , glal2-s3dl45 , glal2-s3d1r9 , glal2-s3e4a7 , glal2-s3ddr1 , glal2-s3ctz6 , glal2-s3dy35 , glal2-s3dws5 , glal2-s3df31 , glal2-s3d7q5 , glal2-s3cwz5 , glal2-s3dcn7 , glal2-s3dhj7 , glal2-s3dm96 , glal2-s3d6q1 , glal2-s3cv25 , glal2-s3e8v9 , glal2-s3crh2 , glal2-s3dde8 , glal2-s3cxt6 , glal2-s3da89 , glal2-s3ckn8 , glal2-s3d4y3 , glal2-s3ddw6 , glal2-s3dk02 , glal2-s3d048 , glal2-s3de12