01963nas a2200229 4500008004100000022001400041245014700055210006900202260007300271300001200344490000800356520107500364653001201439653002501451653002201476100001901498700002001517700001901537700002501556700002201581856013001603 2007 eng d a0168-165600aCharacterization of the proteins of bacterial strain isolated from contaminated site involved in heavy metal resistance - a proteomic approach0 aCharacterization of the proteins of bacterial strain isolated fr aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB a444-4510 v1283 a

The present study describes response of a bacterial strain isolated from a polluted river to heavy metal toxicity. The bacterium was identified to be Klebsiella pneumoniae by biochemical tests using API 20E strips and 16S ribotyping. The isolate was studied for its tolerance to two heavy metals, i.e., cobalt (Co2+) and lead (Pb2+) by growing it in citrate mineral medium (CMM). Proteomic approach involving two-dimensional polyacrylamide gel electrophoresis (2D PAGE) and mass spectrometry (MS) was used to identify the differentially expressed proteins under heavy metal stress. Two of the differentially expressed proteins were identified to be L-isoaspartate protein carboxymethyltransferase type II and DNA gyrase A. To our knowledge, this is for the first time that K pneumoniae has been reported to be present in metal contaminated site and L-isoaspartate protein carboxymethyltransferase type II protein to be over expressed under heavy metal stress. The role of these proteins in metal tolerance is discussed. (c) 2006 Elsevier B.V. All rights reserved.

10a2D PAGE10aheavy metal toxicity10aMass spectrometry1 aBar, Chinmayee1 aPatil, Rajendra1 aDoshi, Jignesh1 aKulkarni, Mahesh, J.1 aGade, Wasudeo, N. uhttps://library.ncl.res.in/content/characterization-proteins-bacterial-strain-isolated-contaminated-site-involved-heavy-metal02315nas a2200277 4500008004100000022001400041245007900055210006900134260007300203300000900276490000800285520137500293653001201668653002001680653002601700653001801726653004001744100002001784700002401804700002001828700001701848700001801865700002501883700002201908856010701930 2012 eng d a0168-165600aEffects of arsenite stress on growth and proteome of Klebsiella pneumoniae0 aEffects of arsenite stress on growth and proteome of Klebsiella  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAR a8-160 v1583 a

In the present study an arsenite, As(III), tolerating bacterium, MR4, was isolated from Mulla River Pune, India, capable of reducing arsenate to arsenite and identified as Klebsiella pneumoniae (HQ857583). Comparative proteomic analysis using two-dimensional gel electrophoresis (2-DGE) and matrix assisted laser desorption ionization-time of flight-time of flight (MALDI-TOF/ TOF) was used to monitor the proteins undergoing changes in expression levels under 2.5 mM As(III) stress. The 2-DGE proteome map has shown that 60 proteins were differentially expressed under As(III) stress, of which 39 proteins were successfully identified with a MASCOT score greater than 70 (p < 0.05). Among the identified proteins, membrane transport/ binding proteins, porins, and amino acid metabolism enzymes were down-regulated while stress responsive proteins and antioxidant enzymes were up-regulated. Proteins involved in carbohydrate metabolism, particularly those in pentose phosphate pathway were also up-regulated while those involved in pyruvate metabolism were down-regulated. However, proteins involved in glycolysis and tricarboxylic acid cycle showed a mixed regulation response. These findings provide new insights into the probable mechanisms by which K. pneumoniae (HQ857583) could be adapting to As(III) stress. (C) 2012 Elsevier B.V. All rights reserved.

10a(2-DGE)10aArsenite stress10aKlebsiella pneumoniae10aMALDI-TOF-TOF10aTwo dimensional gel electrophoresis1 aDaware, Vandana1 aKesavan, Suresh, K.1 aPatil, Rajendra1 aNatu, Arvind1 aKumar, Ameeta1 aKulkarni, Mahesh, J.1 aGade, Wasudeo, N. uhttps://library.ncl.res.in/content/effects-arsenite-stress-growth-and-proteome-klebsiella-pneumoniae-002342nas a2200205 4500008004100000022001400041245005200055210005000107260011000157300001400267490000600281520163200287100002001919700002501939700002001964700002501984700002102009700002202030856008402052 2013 eng d a2046-206900aArsenomics of exiguobacterium sp PS (NCIM 5463)0 aArsenomics of exiguobacterium sp PS NCIM 5463 aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcAPR a9705-97130 v33 a

In the present study, arsenate [As(V)] tolerant organisms were isolated from a metal contaminated site, and identified by 16S rDNA sequencing as Exiguobacterium sp. Arsenomics (omics of arsenic response) in Exiguobacterium sp. PS via two-dimensional gel electrophoresis (2-DGE) coupled with identification of proteins using MALDI-TOF MS, MALDI-TOF MS/MS and LC/MSE are studied vide this paper. Out of 2460 Coomassie stained proteins, 270 were differentially expressed (p < 0.05). Considering the resolution and abundance level, 45 spots (proteins) were subjected to MALDI-TOF MS/MS, MALDI-TOF/TOF and LC/MSE. Out of these, 33 were identified and categorized into several functional categories (including both known and novel/putative stress responsive proteins) viz., carbohydrate and energy metabolism, stress response, motility, amino acid, and purine and protein synthesis. The identifications of unique proteins, phosphate ABC transporter ATPase subunit and pyridine nucleotide disulfide oxidoreductase, are the significant findings of the present study which may be used as markers of As(V) stress in Exiguobacterium sp. PS. The absence of As(V) reductase activity and non-amplification of the arsC gene of the ars operon suggests that the classical mechanism of As(V) resistance may not be operating in Exiguobacterium sp. PS. Lastly, considering the fact that proteomic studies under As(V) stress were performed only in Gram negative organisms, this study is the first comprehensive endeavour to explore the mechanism of As(V) response in Gram positive organisms, Exiguobacterium sp. PS at the proteomic level.

1 aSacheti, Poonam1 aBhonsle, Hemangi, S.1 aPatil, Rajendra1 aKulkarni, Mahesh, J.1 aSrikanth, Rapole1 aGade, Wasudeo, N. uhttps://library.ncl.res.in/content/arsenomics-exiguobacterium-sp-ps-ncim-5463-002477nas a2200325 4500008004100000022001400041245009500055210006900150260005700219300001400276490000700290520142400297653001201721653002001733653001501753653001101768653002001779100002001799700002001819700001701839700002501856700002101881700002001902700002201922700001901944700002501963700002101988700002202009856012002031 2014 eng d a0175-759800aProteomics of arsenic stress in the gram-positive organism Exiguobacterium sp PS NCIM 54630 aProteomics of arsenic stress in the grampositive organism Exiguo a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcAUG a6761-67730 v983 a

The general responses of microorganisms to environmental onslaughts are modulated by altering the gene expression pattern to reduce damage in the cell and produce compensating stress responses. The present study attempts to unravel the response of the Gram-positive Exiguobacterium sp. PS NCIM 5463 in the presence of [As(III)] and arsenate [As(V)] using comparative proteomics via two-dimension gel electrophoresis (2-DE) coupled with identification of proteins using matrix-assisted laser desorption/ionisation (MALDI-TOF/MALDI-TOF/TOF). Out of 926 Coomassie-stained proteins, 45 were differentially expressed (p < 0.05). Considering the resolution and abundance level, 24 spots (peptides) were subjected to MALDI analysis, identified and categorised into several functional categories, viz., nitrogen metabolism, energy and stress regulators, carbohydrate metabolism, protein synthesis components and others. A functional role of each protein is discussed in Exiguobacterium sp. PS 5463 under arsenic stress and validated at their transcript level using a quantitative real-time polymerase chain reaction. Unlike previous reports that unravel the responses toward arsenic stress in Gram-negative organisms, the present study identified new proteins under arsenic stress in a Gram-positive organism, Exiguobacterium sp. PS NCIM 5463, which could elucidate the physiology of organisms under arsenic stress.

10aArsenic10aExiguobacterium10aproteomics10aStress10aTranscriptomics1 aSacheti, Poonam1 aPatil, Rajendra1 aDube, Ankita1 aBhonsle, Hemangi, S.1 aThombre, Dipalee1 aMarathe, Sayali1 aVidhate, Ravindra1 aWagh, Priyanka1 aKulkarni, Mahesh, J.1 aRapole, Srikanth1 aGade, Wasudeo, N. uhttps://library.ncl.res.in/content/proteomics-arsenic-stress-gram-positive-organism-exiguobacterium-sp-ps-ncim-546302639nas a2200265 4500008004100000022001400041245006800055210006800123260000800191300001300199490000700212520181400219100002002033700001802053700002102071700001702092700002102109700002002130700001902150700002902169700002502198700001802223700003202241856010002273 2018 eng d a1369-378600aLimonene inhibits Candida albicans growth by inducing apoptosis0 aLimonene inhibits Candida albicans growth by inducing apoptosis cJUL a 565-5780 v563 a

Anti-Candida potential of limonene was evaluated against planktonic growth, biofilm (adhesion, development and maturation) and morphogenesis of Candida albicans in this study. Limonene is a major constituent of citrus oil and most frequently used terpene in food and beverage industry due to its pleasant fragrance, nontoxic, and is generally recognized as safe (GRAS) flavoring agent as well as treatment option in many gastrointestinal diseases. Limonene exhibited excellent anti-Candida activity and was equally effective against planktonic growth of C. albicans isolates differentially susceptible to FLC (N = 35). Limonene inhibited morphogenesis significantly at low concentration. However, it showed stage dependent activity against biofilm formation, that is, it was more effective against adhesion followed by development and maturation. Limonene also exhibited excellent synergy with FLC against planktonic and biofilm growth. SWATH-MS analysis led to identification of limonene responsive proteins that provided molecular insight of its anti-Candida activity. Proteomic analysis revealed upregulation of proteins involved in cell wall glucan synthesis (Kre6); oxidative stress (Rhr2, Adh7 and Ebp1); DNA damage stress (Mbf1 and Npl3); nucleolar stress (Rpl11, Rpl7, Rpl29, Rpl15) and down regulation of cytoskeleton organization (Crn1, Pin3, Cct8, Rbl2), and so forth, in response to limonene. Limonene mediated down regulation of Tps3 indicates activation of caspase (CaMca1) and induction of apoptosis in C. albicans. These results suggest that limonene inhibits C. albicans growth by cell wall/membrane damage induced oxidative stress that leads to DNA damage resulting into modulation of cell cycle and induction of apoptosis through nucleolar stress and metacaspase dependent pathway.

1 aThakre, Archana1 aZore, Gajanan1 aKodgire, Santosh1 aKazi, Rubina1 aMulange, Shradha1 aPatil, Rajendra1 aShelar, Amruta1 aSanthakumari, Bayitigeri1 aKulkarni, Mahesh, J.1 aKharat, Kiran1 aKaruppayil, Sankunny, Mohan uhttps://library.ncl.res.in/content/limonene-inhibits-candida-albicans-growth-inducing-apoptosis02763nas a2200289 4500008004100000022001400041245013200055210006900187260000800256300001000264490000800274520177900282653001302061653002102074653002202095653004402117653001802161653003002179653001802209100001802227700002102245700002102266700002002287700002502307700001802332856012302350 2018 eng d a1874-391900aSerum responsive proteome reveals correlation between oxidative phosphorylation and morphogenesis in Candida albicans ATCC102310 aSerum responsive proteome reveals correlation between oxidative  cAUG a25-380 v1853 a

To understand the impact of fetal bovine serum (FBS) on metabolism and cellular architecture in addition to morphogenesis, we have identified FBS responsive proteome of Candida albicans. FBS induced 34% hyphae and 60% pseudohyphae in C. albicans at 30 C while 98% hyphae at 37 C. LC-MS/MS analysis revealed that 285 proteins modulated significantly in response to FBS at 30 degrees C and 37 degrees C. Out of which 152 were upregulated and 62 were downregulated at 30 degrees C while 18 were up and 53 were downregulated at 37 degrees C. Functional annotation suggests that FBS may inhibit glycolysis and fermentative pathway and enhance oxidative phosphorylation (OxPhos), TCA cycle, amino acid and fatty acid metabolism indicating a use of alternative energy source by C. albicans. OxPhos inhibition assay using sodium azide corroborated the correlation between inhibition of glycolysis and enhanced OxPhos with pseudohyphae formation. C. albicans induced hyphae in response to FBS irrespective of down regulation of Rasl,Asrl/Asr2, indicates the possible involvement of MAPK and cAMP-PKA independent pathway. The Cell wall of cells grown in presence of FBS at 30 degrees C was rich in mannan, Beta 1,3glucan and chitin while membranes were rich in ergosterol compared to those grown at 37 degrees C. Significance of the study: This is the first study suggesting a correlation between OxPhos and morphogenesis especially pseudohyphae formation in C. albicans. Our data also indicate that fetal bovine serum (FBS) induced morphogenesis is multifactorial and may involve MAPK and cAMP-PKA independent pathway. In addition to morphogenesis, our study provides an insight in to the modulation of metabolism and cellular architecture of C. albicans in response to FBS.

10aanalysis10aCandida albicans10aFetal bovin serum10aLiquid chromatography mass spectrometry10amorphogenesis10aOxidative phosphorylation10apathogenicity1 aAhmed, Radfan1 aKodgire, Santosh1 aSanthakumari, B.1 aPatil, Rajendra1 aKulkarni, Mahesh, J.1 aZore, Gajanan uhttps://library.ncl.res.in/content/serum-responsive-proteome-reveals-correlation-between-oxidative-phosphorylation-and03094nas a2200301 4500008004100000022001400041245008000055210006900135260000800204300001200212490000700224520220800231653001402439653001602453653002002469653001302489653001502502653001202517100002002529700002302549700001702572700001902589700002002608700001802628700001802646700002202664856010602686 2021 eng d a1369-378600aOxidative stress induced by piperine leads to apoptosis in Candida albicans0 aOxidative stress induced by piperine leads to apoptosis in Candi cAPR a366-3780 v593 a

Candida albicans is a member of pathogens with potential drug resistance threat that needs novel chemotherapeutic strategies. Considering the multifarious biological activities including bioenhancer activity, anti-Candida potential of piperine was evaluated against planktonic/biofilm and hyphal growth of C. albicans alone or in combination as a synergistic agent with fluconazole. Piperine inhibits planktonic growth at or less than 15 mu g/ml, hyphae induction at 5 mu g/ml concentration, and exhibits stage-dependent activity against biofilm growth of a fluconazole-resistant strain of C. albicans (ATCC10231). Though piperine couldn't kill inoculum completely at minimum inhibitory concentration (MIC), it is fungicidal at higher concentrations, as shown in apoptosis assay. FIC index values indicate that piperine exhibits excellent synergistic activity with fluconazole against planktonic (0.123) and biofilm (0.215) growth of an FLC resistant strain. Mode of anti-Candida activity was studied by identifying piperine responsive proteins wherein the abundance of 25 proteins involved in stress response, signal transduction and cell cycle were modulated (22 up and 3 downregulated) significantly in response to piperine (MIC50). Modulation of the proteins involved suggests that piperine affectsmembrane integrity leading to oxidative stress followed by cell cycle arrest and apoptosis in C. albicans. Flow cytometry-basedmitochondrialmembrane potential (MMP), cell cycle and apoptosis assay, as well as real-time quantitative polymerase chain reaction analysis of selected genes, confirms piperine induced oxidative stress (TRR1), cell cycle arrest and apoptosis (CaMCA1). Based on our results, we conclude that piperine inhibits planktonic and difficult-to treat-biofilm growth of C. albicans by affecting membrane integrity thereby inducing oxidative stress and apoptosis. Lay Abstract Piperine inhibit Candida albicans growth (planktonic and biofilm) significantly in our study. Piperine exhibits excellent synergistic potential with fluconazole The proteome analysis suggests that piperine induced membrane damage leads to oxidative stress followed by cell cycle arrest and apoptosis.

10aApoptosis10aC. albicans10adrug resistance10apiperine10aproteomics10asynergy1 aThakre, Archana1 aJadhav, Vyankatesh1 aKazi, Rubina1 aShelar, Amruta1 aPatil, Rajendra1 aKharat, Kiran1 aZore, Gajanan1 aKaruppayil, Mohan uhttps://library.ncl.res.in/content/oxidative-stress-induced-piperine-leads-apoptosis-candida-albicans02906nas a2200313 4500008004100000022001400041245005000055210005000105260000900155300001100164490000800175520208100183653001202264653002102276653001402297653001002311653001502321653000702336653001502343100002202358700001802380700002102398700001802419700001702437700002002454700001802474700001802492856008202510 2022 eng d a1874-391900aProteomic profile of candida albicans biofilm0 aProteomic profile of candida albicans biofilm cAUG  a1046610 v2653 a

Candida albicans biofilms are characterized by structural and cellular heterogeneity that confers antifungal resistance and immune evasion. Despite this, biofilm formation remains poorly understood. In this study, we used proteomic analysis to understand biofilm formation in C. albicans related to morphophysiological and architectural features. LC-MS/MS analysis revealed that 64 proteins were significantly modulated, of which 31 were upregulated and 33 were downregulated. The results indicate that metabolism (25 proteins), gene expression (13 proteins), stress response (7 proteins), and cell wall (5 proteins) composition are modulated. The rate of oxidative phosphorylation (OxPhos) and biosynthesis of UDP-N-acetylglucosamine, vitamin B6, and thiamine increased, while the rate of methionine biosynthesis decreased. There was a significant modification of the cell wall architecture due to higher levels of Sun41, Pir1 and Csh1 and increased glycosylation of proteins. It was observed that C. albicans induces hyphal growth by upregulating the expression of genes involved in cAMP-PKA and MAPK pathways. This study is significant in that it suggests an increase in OxPhos and alteration of cell wall architecture that could be contributing to the recalcitrance of C. albicans cells growing in biofilms. Nevertheless, a deeper investigation is needed to explore it further.Significance: Candida sps is included in the list of pathogens with potential drug resistance threat due to the increased frequency especially colonization of medical devices, and tissues among the patients, in recent years. Significance of our study is that we are reporting traits like modulation in cell wall composition, amino acid and vitamin biosynthesis and importantly energy generation (OxPhos) etc. These traits could be conferring antifungal resistance, host immune evasion etc. and thus survival, in addition to facilitating biofilm formation. These findings are expected to prime the further studies on devising potent strategy against biofilm growth among the patients.

10aBiofilm10aCandida albicans10aCell wall10aLC-MS10aMetabolism10aMS10aproteomics1 aAbdulghani, Mazen1 aIram, Rasiqua1 aChidrawar, Priti1 aBhosle, Kajal1 aKazi, Rubina1 aPatil, Rajendra1 aKharat, Kiran1 aZore, Gajanan uhttps://library.ncl.res.in/content/proteomic-profile-candida-albicans-biofilm03041nas a2200337 4500008004100000022001400041245006500055210006400120260000800184300001200192490000700204520212500211653001302336653000602349653001002355653000702365653001102372653002102383653001102404653001202415100002202427700002202449700001902471700001902490700001702509700001902526700002002545700002302565700001802588856009702606 2023 eng d a1369-378600aOpaque cell-specific proteome of Candida albicans ATCC 102310 aOpaque cellspecific proteome of Candida albicans ATCC 10231 cJUL amyad0620 v613 a

Candida albicans, a polymorphic opportunistic pathogen of humans, can exist in different morphological forms like yeast, hyphae, pseudohyphae, chlamydospores, and white and opaque cells. Proteomic analysis of opaque form of C. albicans ATCC 10231 is carried out in the present study using microflow liquid chromatography-tandem mass spectrometry and validated using expression analysis of selected genes using reverse transcription quantitative real-time PCR and mitochondrial membrane potential assay. This is the first report identifying opaque cell-specific proteins of C. albicans. A total of 188 proteins were significantly modulated under opaque form compared to white cells, of which 110 were upregulated, and 78 were downregulated. It was observed that oxidative phosphorylation (OxPhos) and oxidative stress are enhanced in C. albicans cells growing under opaque form as proteins involved in OxPhos (Atp1, Atp3, Atp16, Atp7, Cox6, Nuc2, Qcr7, and Sdh12) and oxidative stress response (Gcs1, Gtt11, Gpx2, Sod1, Ccp1, and Lys7) were significantly upregulated. The maximum upregulation of 23.16- and 13.93-fold is observed in the cases of Ccp1 and Nuc2, respectively. The downregulation of proteins, namely Als1, Csh1, Sap9, and Rho1, determining cell surface chemistry indicates modulation in cell wall integrity and reduced adhesion of opaque cells compared to white cells. This study is significant as it is the first draft of the proteomic profile of opaque cells that suggests enhanced OxPhos, oxidative stress, and modulation in cell surface chemistry indicating reduced adhesion and cell wall integrity, which could be associated with reduced virulence in opaque form. However, a deeper investigation is needed to explore it further. Lay Summary Opaque form is one of the least studied morphological forms of Candida albicans. To the best of our knowledge, this is the first report providing opaque cell-specific proteome. It suggests enhanced oxidative phosphorylation, oxidative stress, and modulation in cell surface chemistry, which could be associated with reduced virulence in opaque form.

10aalbicans10aC10aLC-MS10aMS10aopaque10aOxidative stress10aOxPhos10aprotein1 aAbdulghani, Mazen1 aTelang, Saraswati1 aDesai, Manisha1 aKadam, Shivdas1 aKazi, Rubina1 aShelar, Amruta1 aPatil, Rajendra1 aMaurya, Radheshyam1 aZore, Gajanan uhttps://library.ncl.res.in/content/opaque-cell-specific-proteome-candida-albicans-atcc-1023102975nas a2200181 4500008004100000245006500041210006300106260000800169490000700177520239700184100001802581700002202599700002102621700001702642700001902659700002002678856009502698 2024 eng d00aProteome dataset of Candida albicans (ATCC10231) opaque cell0 aProteome dataset of Candida albicans ATCC10231 opaque cell cJAN0 v173 a

Objectives

Candida albicans, a polymorphic yeast, is one of the most common, opportunistic fungal pathogens of humans. Among the different morphological forms, opaque form is one of the least-studied ones. This opaque phenotype is essential for mating and is also reported to be involved in colonizing the gastrointestinal tract. Considering the significance of the clinical and sexual reproduction of C. albicans, we have investigated the morphophysiological modulations in opaque form using a proteomic approach.

Data description

In the current investigation, we have used Micro-Liquid Chromatography-Mass Spectrometry (LC-MS/MS) analysis to create a protein profile for opaque-specific proteins. Whole-cell proteins from C. albicans (ATCC10231) cells that had been cultured for seven days on synthetic complete dextrose (SCD) medium in both as an opaque (test) and as a white (control) form cells were extracted, digested, and identified using LC-MS/MS. This information is meant to serve the scientific community and represents the proteome profile (SWATH Spectral Libraries) of C. albicans opaque form.

1 aZore, Gajanan1 aAbdulghani, Mazen1 aKodgire, Santosh1 aKazi, Rubina1 aShelar, Amruta1 aPatil, Rajendra uhttps://library.ncl.res.in/content/proteome-dataset-candida-albicans-atcc10231-opaque-cell