02016nas a2200277 4500008004100000022001400041245011600055210006900171260009900240300001400339490000800353520100300361653002801364653001501392653001701407653003201424100001801456700002201474700001401496700001701510700001601527700002101543700002101564700002601585856012701611 2010 eng d a0960-852400aFlocculation of dimorphic yeast benjaminiella poitrasii is altered by modulation of NAD-glutamate dehydrogenase0 aFlocculation of dimorphic yeast benjaminiella poitrasii is alter aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcFEB a1393-13950 v1013 a

A strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibited faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Atomic force microscopy revealed higher surface roughness of Y (439.34 rms) than Y-5 (52 rms). Also, the former had a zeta potential of -65.97 +/- 3.45 as against -50.21 +/- 2.49 for the latter. Flocculation of both Y and Y-5 could be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation was promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing. (C) 2009 Elsevier Ltd. All rights reserved.

10aBenjaminiella poitrasii10adimorphism10aflocculation10aNAD-glutamate dehydrogenase1 aJoshi, C., V.1 aGhormade, Vandana1 aKunde, P.1 aKulkarni, P.1 aMamgain, H.1 aBhat, Suresh, K.1 aPaknikar, K., M.1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/flocculation-dimorphic-yeast-benjaminiella-poitrasii-altered-modulation-nad-glutamate-001296nas a2200217 4500008004100000022001400041245013100055210006900186260011200255300001200367490000700379520042600386653002200812653001500834653002200849653002700871100001800898700002000916700001700936856012500953 2011 eng d a0019-452200aSynthesis and structural characterization of a solvated dimorph of a hydrazonato-oxovanadium(v) complex with [OV(mu-O)VO] core0 aSynthesis and structural characterization of a solvated dimorph  a5-A, NEW PALI RD, PO BOX 91, NEAR HOTEL TAJ HARI MAHAL, JODHPUR, 342 003, INDIAbSCIENTIFIC PUBL-INDIAcJUL a937-9410 v883 a

In this paper we report the synthesis and structural characterization of a different monoclinic variety of the title complex [V2O3(L)(2)], incorporating the doubly deprotonated benzoyl hydrazone of 5-chloro-2-hydroxyacetophenone (H2L) with P2(1)/c space group that showed some differences in bonding patterns in the solid state with respect to its another monoclinic variety with C2/c space group reported earlier.

10acrystal structure10adimorphism10ahydrazone complex10aOxovanadium(v) complex1 aMondal, Bipul1 aBanerjee, Rahul1 aGhosh, Tapas uhttps://library.ncl.res.in/content/synthesis-and-structural-characterization-solvated-dimorph-hydrazonato-oxovanadiumv-002489nas a2200277 4500008004100000022001400041245016500055210006900220260006700289300001000356490000800366520147900374653001401853653002101867653001501888653001501903653001901918653002801937100001701965700002101982700001602003700001702019700002102036700002602057856012802083 2015 eng d a1364-507200aPossible mechanism of antifungal phenazine-1-carboxamide from pseudomonas sp against dimorphic fungi Benjaminiella poitrasii and human pathogen Candida albicans0 aPossible mechanism of antifungal phenazine1carboxamide from pseu a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcJAN a39-480 v1183 a

AimInvestigation of antifungal mechanism of phenazine 1-carboxamide (PC) produced by a Pseudomonas strain MCC2142. Methods and ResultsAn antifungal metabolite produced by a Pseudomonas was purified and identified as PC. Human pathogenic fungi such as Candida albicans, Candidaglabrata, Cryptococcus neoformans, Fusarium oxysporum, Aspergillus fumigatus and Aspergillus niger were found to be inhibited by PC (MIC90 32-64gml(-1)). Addition of PC (20gml(-1)) during yeast (Y)-hypha (H) transitions inhibited germ tube formation by >90% and >99% in C.albicans National Collection of Industrial Microorganisms (NCIM) 3471 and nonpathogenic model Benjaminiella poitrasii, respectively. After exposure to PC (20gml(-1)), 75-80% yeast cells of B.poitrasii and C.albicans NCIM 3471 showed rhodamine 123 fluorescence indicating high intracellular reactive oxygen species (ROS) production. ROS further led to hyperpolarization of mitochondrial membrane, subsequently induction of apoptosis as evident by externalization of phosphatidylserine, DNA fragmentation, chromatin condensation and finally death in B.poitrasii. In C.albicans NCIM 3471, PC (20gml(-1)) induced apoptosis. ConclusionsThe antifungal effect of PC in B.poitrasii and C.albicans may be due to ROS-mediated apoptotic death. Significance and Impact of the StudyInhibition of Y-H transition of B.poitrasii and C.albicans by PC indicates that it may prove useful in the control of dimorphic human pathogens.

10aApoptosis10aCandida albicans10adimorphism10aphenazines10aPseudomonas sp10areactive oxygen species1 aTupe, S., G.1 aKulkarni, R., R.1 aShirazi, F.1 aSant, D., G.1 aJoshi, Swati, P.1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/possible-mechanism-antifungal-phenazine-1-carboxamide-pseudomonas-sp-against-dimorphic-002431nas a2200277 4500008004100000022001400041245015100055210006900206260000800275300001100283490000700294520142900301653002801730653002101758653003301779653001501812653002301827653003701850653002701887100002101914700002201935700002301957700002101980700002602001856012602027 2019 eng d a1567-135600aMolecular studies of NAD- and NADP-glutamate dehydrogenases decipher the conundrum of yeast-hypha dimorphism in zygomycete Benjaminiella poitrasii0 aMolecular studies of NAD and NADPglutamate dehydrogenases deciph cDEC afoz0740 v193 a

Benjaminiella poitrasii, a zygomycete, shows glucose- and temperature-dependent yeast (Y)-hypha (H) dimorphic transition. Earlier, we reported the biochemical correlation of relative proportion of NAD- and NADP-glutamate dehydrogenases (GDHs) with Y-H transition. Further, we observed the presence of one NAD-GDH and two form-specific NADP-GDH isoenzymes in B. poitrasii. However, molecular studies are necessary to elucidate the explicit role of GDHs in regulating Y-H reversible transition. Here, we report the isolation and characterization of one NAD (BpNADGDH, 2.643 kb) and two separate genes, BpNADPGDH I (Y-form specific, 1.365 kb) and BpNADPGDH II (H-form specific, 1.368 kb) coding for NADP-GDH isoenzymes in B. poitrasii. The transcriptional profiling during Y-H transition showed higher BpNADPGDH I expression in Y cells while expression of BpNADPGDH II was higher in H cells. Moreover, the yeast-form monomorphic mutant (Y-5) did not show BpNADPGDH II expression under normal dimorphism triggering conditions. Transformation with H-form specific BpNADPGDH II induced the germ tube formation in Y-5, which confirmed the cause-effect relationship between BpNADPGDH genes and morphological outcome in B. poitrasii. Interestingly, expression of H-form specific BpNADPGDH II also induced germ tube formation in human pathogenic, non-dimorphic yeast Candida glabrata, which further corroborated our findings.

10aBenjaminiella poitrasii10aCandida glabrata10adifferential gene expression10adimorphism10amonomorphic mutant10aNAD/NADP-glutamate dehydrogenase10ayeast-hypha transition1 aPathan, Ejaj, K.1 aGhormade, Vandana1 aPanwar, Sneh, Lata1 aPrasad, Rajendra1 aDeshpande, Mukund, V. uhttps://library.ncl.res.in/content/molecular-studies-nad-and-nadp-glutamate-dehydrogenases-decipher-conundrum-yeast-hypha02706nas a2200277 4500008004100000022001400041245017600055210006900231260000800300300001100308490000900319520169400328653002402022653002802046653002102074653005102095653001502146653002202161653003402183100002102217700002402238700003202262700000502294700000502299856012402304 2020 eng d a0304-416500aNADP-dependent glutamate dehydrogenases in a dimorphic zygomycete Benjaminiella poitrasii: purification, characterization and their evaluation as an antifungal drug target0 aNADPdependent glutamate dehydrogenases in a dimorphic zygomycete cNOV a1296960 v18643 a

Background: It has been reported that the genes coding for NADP-dependent glutamate dehydrogenases (NADP-GDHs) showed a cause-effect relationship with Yeast-Hypha (Y-H) reversible transition in a zygomycete Benjaminiella poitrasii. As Y-H transition is significant in human pathogenic fungi for their survival and proliferation in the host, the NADP-GDHs can be explored as antifungal drug targets. Methods: The yeast-form specific BpNADPGDH I and hyphal-form specific BpNADPGDH II of B. poitrasii were purified by heterologous expression in E. coll. BL-21 cells and characterized. The structural analogs of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives were designed, synthesized and screened for inhibition of NADP-GDH activity as well as Y-H transition in B. poitrasii, and also in human pathogenic Candida albicans strains. Results: The BpNADPGDH I and BpNADPGDH II were found to be homo-hexameric proteins with native molecular mass of 282 kDa and 298 kDa, respectively and subunit molecular weights of 47 kDa and 49 kDa, respectively. Besides the distinct kinetic properties, BpNADPGDH I and BpNADPGDH II were found to be regulated by cAMP-dependent- and Calmodulin (CaM) dependent- protein kinases, respectively. The DMIP compounds showed a more pronounced effect on H-form specific BpNADPGDH II and inhibited Y-H transition as well as growth in B. poitrasii and C. albicans strains. Conclusion: The present study will be useful to design and develop antifungal drugs against dimorphic human pathogens using glutamate dehydrogenase as a target. Significance: Glutamate dehydrogenases can be explored as a target against human pathogenic fungi.

10aAntifungal compound10aBenjaminiella poitrasii10aCandida albicans10aDimethyl esters and amides of isophthalic acid10adimorphism10aEnzyme inhibition10aNADP-glutamate dehydrogenases1 aPathan, Ejaj, K.1 aKulkarni, Anand, M.1 aPrasanna, Nallaballe, V. L.1 a1 a uhttps://library.ncl.res.in/content/nadp-dependent-glutamate-dehydrogenases-dimorphic-zygomycete-benjaminiella-poitrasii04119nas a2200337 4500008004100000022001400041245014800055210006900203260000900272300001100281490000800292520302600300653001503326653001003341653001003351653000903361653001403370653001403384100002403398700003203422700002203454700002103476700002103497700002003518700002803538700001803566700002503584700002503609700002203634856012503656 2024 eng d a1874-391900aComparative proteomics of sugarcane smut fungus- Sporisorium scitamineum unravels dynamic proteomic alterations during the dimorphic transition0 aComparative proteomics of sugarcane smut fungus Sporisorium scit cJUL  a1052300 v3043 a

Life cycle of the dimorphic sugarcane smut fungi, Sporisorium scitamineum , involves recognition and mating of compatible saprophytic yeast -like haploid sporidia (MAT -1 and MAT -2) that upon fusion, develop into infective dikaryotic mycelia. Although the dimorphic transition is intrinsically linked with the pathogenicity and virulence of S. scitamineum , it has never been studied using a proteomic approach. In the present study, an iTRAQ-based comparative proteomic analysis of three distinct stages was carried out. The stages were: the dimorphic transition period - haploid sporidial stage (MAT -1 and MAT -2); the transition phase (24 h post co -culturing (hpc)) and the dikaryotic mycelial stage (48 hpc). Functional categorization of differentially abundant proteins showed that the most altered biological processes were energy production, primary metabolism, especially, carbohydrate, amino acid, fatty acid, followed by translation, post -translation and protein turnover. Several differentially abundant proteins (DAPs), especially in the dikaryotic mycelial stage were predicted as effectors. Taken together, key molecular mechanisms underpinning the dimorphic transition in S. scitamineum at the proteome level were highlighted. The catalogue of stage -specific and dimorphic transition -associated -proteins and potential effectors identified herein represents a list of potential candidates for defective mutant screening to elucidate their functional role in the dimorphic transition and pathogenicity in S. scitamineum . Biological significance: Being the first comparative proteomics analysis of S. scitamineum , this study comprehensively examined three pivotal life cycle stages of the pathogen: the non-pathogenic haploid phase, the transition phase, and the pathogenic dikaryotic mycelial stage. While previous studies have reported the sugarcane and S. scitamineum interactions, this study endeavored to specifically identify the proteins responsible for pathogenicity. By analyzing the proteomic alterations between the haploid and dikaryotic mycelial phases, the study revealed significant changes in metabolic pathway -associated proteins linked to energy production, notably oxidative phosphorylation, and the citrate cycle. Furthermore, this study successfully identified key metabolic pathways that undergo reprogramming during the transition from the non-pathogenic to the pathogenic stage. The study also deciphered the underlying mechanisms driving the morphological and physiological alterations crucial for the S. scitamineum virulence. By studying its life cycle stages, identifying the key metabolic pathways and stage -specific proteins, it provides unprecedented insights into the pathogenicity and potential avenues for intervention. As proteomics continues to advance, such studies pave the way for a deeper understanding of plantpathogen interactions and the development of innovative strategies to mitigate the impact of devastating pathogens like S. scitamineum.

10adimorphism10afungi10aiTRAQ10aSmut10aSugarcane10aVirulence1 aKumaravel, Nalayeni1 aEbinezer, Leonard, Barnabas1 aAshwin, N., M. R.1 aFranchin, Cinzia1 aBattisti, Ilaria1 aCarletti, Paolo1 aSundar, Amalraj, Ramesh1 aMasi, Antonio1 aMalathi, Palaniyandi1 aViswanathan, Rasappa1 aArrigoni, Giorgio uhttps://library.ncl.res.in/content/comparative-proteomics-sugarcane-smut-fungus-sporisorium-scitamineum-unravels-dynamic