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-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-hypha