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Journal articles on the topic 'Candida Candida albicans Decarboxylases'

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Published: 4 June 2021

Last updated: 5 February 2022

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1

Herrero, Ana B., M. Carmen López, Susana García, Axel Schmidt, Frank Spaltmann, José Ruiz-Herrera, and Angel Dominguez. "Control of Filament Formation in Candida albicans by Polyamine Levels." Infection and Immunity 67, no. 9 (September 1, 1999): 4870–78. http://dx.doi.org/10.1128/iai.67.9.4870-4878.1999.

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ABSTRACT Candida albicans, the most common fungal pathogen, regulates its cellular morphology in response to environmental conditions. The ODC gene, which encodes ornithine decarboxylase, a key enzyme in polyamine biosynthesis, was isolated and disrupted. Homozygous null Candida mutants behaved as polyamine auxotrophs and grew exclusively in the yeast form at low polyamine levels (0.01 mM putrescine) under all conditions tested. An increase in the polyamine concentration (10 mM putrescine) restored the capacity to switch from the yeast to the filamentous form. The strain with a deletion mutation also showed increased sensitivity to salts and calcofluor white. This Candida odc/odc mutant was virulent in a mouse model. The results suggest a model in which polyamine levels exert a pleiotrophic effect on transcriptional activity.

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2

Tylicki, Adam, Grazyna Ziolkowska, Aleksandra Bolkun, Magdalena Siemieniuk, Jan Czerniecki, and Agnieszka Nowakiewicz. "Comparative study of the activity and kinetic properties of malate dehydrogenase and pyruvate decarboxylase from Candida albicans, Malassezia pachydermatis, and Saccharomyces cerevisiae." Canadian Journal of Microbiology 54, no. 9 (September 2008): 734–41. http://dx.doi.org/10.1139/w08-062.

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Candida albicans and Malassezia pachydermatis cause human and animal infections of the skin and internal organs. We compare the properties of two enzymes, pyruvate decarboxylase (PDC) and malate dehydrogenase (MDH), from these species and from Saccharomyces cerevisiae cultivated under aerobic and anaerobic conditions to find differences between the enzymes that adapt pathogens for virulence and help us in searching for new antifungal agents. Malassezia pachydermatis did not show any growth under anaerobic conditions, as opposed to C. albicans and S. cerevisiae. Under aerobic conditions, C. albicans showed the highest growth rate. Malassezia pachydermatis, contrary to the others, did not show any PDC activity, simultaneously showing the highest MDH activity under aerobic conditions and a Km value for oxaloacetate lower than S. cerevisiae. Candida albicans and S. cerevisiae showed a strong decrease in MDH activity under anaerobic conditions. Candida albicans shows four different isoforms of MDH, while M. pachydermatis and S. cerevisiae are characterized by two and three isoforms. Candida albicans shows about a twofold lower activity of PDC but, simultaneously, almost a threefold lower Km value for pyruvate in comparison with S. cerevisiae. The PDC apoform share under aerobic conditions in C. albicans was 47%, while in S. cerevisiae was only 26%; under anaerobic conditions, the PDC apoform decreased to 12% and 8%, respectively. The properties of enzymes from C. albicans show its high metabolic flexibility (contrary to M. pachydermatis) and cause easy switching between fermentative and oxidative metabolism. This feature allows C. albicans to cause both surface and deep infections. We take into consideration the use of thiamin antimetabolites as antifungal factors that can affect both oxidative and fermentative metabolism.

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3

Ghosh, Suman, Bessie W. Kebaara, Audrey L. Atkin, and Kenneth W. Nickerson. "Regulation of Aromatic Alcohol Production in Candida albicans." Applied and Environmental Microbiology 74, no. 23 (October 3, 2008): 7211–18. http://dx.doi.org/10.1128/aem.01614-08.

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ABSTRACT Colonization by the fungal pathogen Candida albicans varies significantly, depending upon the pH and availability of oxygen. Because of our interest in extracellular molecules as potential quorum-sensing molecules, we examined the physiological conditions which regulate the production of the aromatic alcohols, i.e., phenethyl alcohol, tyrosol, and tryptophol. The production of these fusel oils has been well studied for Saccharomyces cerevisiae. Our data show that aromatic alcohol yields for C. albicans are determined by growth conditions. These conditions include the availability of aromatic amino acids, the pH, oxygen levels, and the presence of ammonium salts. For example, for wild-type C. albicans, tyrosol production varied 16-fold merely with the inclusion of tyrosine or ammonium salts in the growth medium. Aromatic alcohol production also depends on the transcription regulator Aro80p. Our results are consistent with aromatic alcohol production—aromatic transaminases (gene products for ARO8 and ARO9), aromatic decarboxylase (ARO10), and alcohol dehydrogenase (ADH)—via the fusel oil pathway. The expression of ARO8, ARO9, and ARO10 is also pH dependent. ARO8 and ARO9 were alkaline upregulated, while ARO10 was alkaline downregulated. The alkaline-dependent change in expression of ARO8 was Rim101 independent, while the expression of ARO9 was Rim101 dependent.

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4

Cheng, Shaoji, M. Hong Nguyen, Zongde Zhang, Hongyan Jia, Martin Handfield, and Cornelius J. Clancy. "Evaluation of the Roles of Four Candida albicans Genes in Virulence by Using Gene Disruption Strains That Express URA3 from the Native Locus." Infection and Immunity 71, no. 10 (October 2003): 6101–3. http://dx.doi.org/10.1128/iai.71.10.6101-6103.2003.

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ABSTRACT Reintroducing URA3 to its native locus in Candida albicans not5, not3, bur2, and kel1 disruption mutants enabled us to directly compare strains with control strain CAI-12. We showed that URA3 position affected orotidine 5′-monophosphate decarboxylase activity, hyphal morphogenesis, adherence, and mortality in murine disseminated candidiasis. After URA3 was reintroduced to its native locus, only NOT5 could be conclusively ascribed a role in virulence.

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5

Lay, Jennifer, L. Keith Henry, Julie Clifford, Yigal Koltin, Christine E. Bulawa, and Jeffrey M. Becker. "Altered Expression of Selectable Marker URA3 in Gene-Disrupted Candida albicans Strains Complicates Interpretation of Virulence Studies." Infection and Immunity 66, no. 11 (November 1, 1998): 5301–6. http://dx.doi.org/10.1128/iai.66.11.5301-5306.1998.

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ABSTRACT The ura-blaster technique for the disruption of Candida albicans genes has been employed in a number of studies to identify possible genes encoding virulence factors of this fungal pathogen. In this study, the URA3-encoded orotidine 5′-monophosphate (OMP) decarboxylase enzyme activities of C. albicans strains with ura-blaster-mediated genetic disruptions were measured. All strains harboring genetic lesions via the ura-blaster construct showed reduced OMP decarboxylase activities compared to that of the wild type when assayed. The activity levels in different gene disruptions varied, suggesting a positional effect on the level of gene expression. Because the URA3 gene ofC. albicans has previously been identified as a virulence factor for this microorganism, our results suggest that decreased virulence observed in strains constructed with the ura-blaster cassette cannot accurately be attributed, in all cases, to the targeted genetic disruption. Although revised methods for validating aURA3-disrupted gene as a target for antifungal drug development could be devised, it is clearly desirable to replaceURA3 with a different selectable marker that does not influence virulence.

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6

Kelly, R., S. M. Miller, M. B. Kurtz, and D. R. Kirsch. "Directed mutagenesis in Candida albicans: one-step gene disruption to isolate ura3 mutants." Molecular and Cellular Biology 7, no. 1 (January 1987): 199–208. http://dx.doi.org/10.1128/mcb.7.1.199.

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A method for introducing specific mutations into the diploid Candida albicans by one-step gene disruption and subsequent UV-induced recombination was developed. The cloned C. albicans URA3 gene was disrupted with the C. albicans ADE2 gene, and the linearized DNA was used for transformation of two ade2 mutants, SGY-129 and A81-Pu. Both an insertional inactivation of the URA3 gene and a disruption which results in a 4.0-kilobase deletion were made. Southern hybridization analyses demonstrated that the URA3 gene was disrupted on one of the chromosomal homologs in 15 of the 18 transformants analyzed. These analyses also revealed restriction site dimorphism of EcoRI at the URA3 locus which provides a unique marker to distinguish between chromosomal homologs. This enabled us to show that either homolog could be disrupted and that disrupted transformants of SGY-129 contained more than two copies of the URA3 locus. The A81-Pu transformants heterozygous for the ura3 mutations were rendered homozygous and Ura- by UV-induced recombination. The homozygosity of a deletion mutant and an insertion mutant was confirmed by Southern hybridization. Both mutants were transformed to Ura+ with plasmids containing the URA3 gene and in addition, were resistant to 5-fluoro-orotic acid, a characteristic of Saccharomyces cerevisiae ura3 mutants as well as of orotidine-5'-phosphate decarboxylase mutants of other organisms.

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7

Kelly, R., S. M. Miller, M. B. Kurtz, and D. R. Kirsch. "Directed mutagenesis in Candida albicans: one-step gene disruption to isolate ura3 mutants." Molecular and Cellular Biology 7, no. 1 (January 1987): 199–208. http://dx.doi.org/10.1128/mcb.7.1.199-208.1987.

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A method for introducing specific mutations into the diploid Candida albicans by one-step gene disruption and subsequent UV-induced recombination was developed. The cloned C. albicans URA3 gene was disrupted with the C. albicans ADE2 gene, and the linearized DNA was used for transformation of two ade2 mutants, SGY-129 and A81-Pu. Both an insertional inactivation of the URA3 gene and a disruption which results in a 4.0-kilobase deletion were made. Southern hybridization analyses demonstrated that the URA3 gene was disrupted on one of the chromosomal homologs in 15 of the 18 transformants analyzed. These analyses also revealed restriction site dimorphism of EcoRI at the URA3 locus which provides a unique marker to distinguish between chromosomal homologs. This enabled us to show that either homolog could be disrupted and that disrupted transformants of SGY-129 contained more than two copies of the URA3 locus. The A81-Pu transformants heterozygous for the ura3 mutations were rendered homozygous and Ura- by UV-induced recombination. The homozygosity of a deletion mutant and an insertion mutant was confirmed by Southern hybridization. Both mutants were transformed to Ura+ with plasmids containing the URA3 gene and in addition, were resistant to 5-fluoro-orotic acid, a characteristic of Saccharomyces cerevisiae ura3 mutants as well as of orotidine-5'-phosphate decarboxylase mutants of other organisms.

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8

López, M. Carmen, Susana García, José Ruiz-Herrera, and A. Domínguez. "The ornithine decarboxylase gene from Candida albicans. Sequence analysis and expression during dimorphism." Current Genetics 32, no. 2 (September 15, 1997): 108–14. http://dx.doi.org/10.1007/s002940050254.

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9

Khandelwal, Nitesh Kumar, Parijat Sarkar, Naseem A. Gaur, Amitabha Chattopadhyay, and Rajendra Prasad. "Phosphatidylserine decarboxylase governs plasma membrane fluidity and impacts drug susceptibilities of Candida albicans cells." Biochimica et Biophysica Acta (BBA) - Biomembranes 1860, no. 11 (November 2018): 2308–19. http://dx.doi.org/10.1016/j.bbamem.2018.05.016.

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10

Wolf, Julie M., Javier Espadas, Jose Luque-Garcia, Todd Reynolds, and Arturo Casadevall. "Lipid Biosynthetic Genes Affect Candida albicans Extracellular Vesicle Morphology, Cargo, and Immunostimulatory Properties." Eukaryotic Cell 14, no. 8 (May 29, 2015): 745–54. http://dx.doi.org/10.1128/ec.00054-15.

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ABSTRACT Microbial secretion is integral for regulating cell homeostasis as well as releasing virulence factors during infection. The genes encoding phosphatidylserine synthase ( CHO1 ) and phosphatidylserine decarboxylase ( PSD1 and PSD2 ) are Candida albicans genes involved in phospholipid biosynthesis, and mutations in these genes affect mitochondrial function, cell wall thickness, and virulence in mice. We tested the roles of these genes in several agar-based secretion assays and observed that the cho1 Δ/Δ and psd1 Δ/Δ psd2 Δ/Δ strains manifested less protease and phospholipase activity. Since extracellular vesicles (EVs) are surrounded by a lipid membrane, we investigated the effects of these mutations on EV structure, composition, and biological activity. The cho1 Δ/Δ mutant releases EVs comparable in size to wild-type EVs, but EVs from the psd1 Δ/Δ psd2 Δ/Δ strain are much larger than those from the wild type, including a population of >100-nm EVs not observed in the EVs from the wild type. Proteomic analysis revealed that EVs from both mutants had a significantly different protein cargo than that of EVs from the wild type. EVs were tested for their ability to activate NF-κB in bone marrow-derived macrophage cells. While wild-type and psd1 Δ/Δ psd2 Δ/Δ mutant-derived EVs activated NF-κB, the cho1 Δ/Δ mutant-derived EV did not. These studies indicate that the presence and absence of these C. albicans genes have qualitative and quantitative effects on EV size, composition, and immunostimulatory phenotypes that highlight a complex interplay between lipid metabolism and vesicle production.

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11

Fitzgerald-Hughes, Deirdre H., David C. Coleman, and Brian C. O’ Connell. "Differentially Expressed Proteins in Derivatives of Candida albicans Displaying a Stable Histatin 3-Resistant Phenotype." Antimicrobial Agents and Chemotherapy 51, no. 8 (May 7, 2007): 2793–800. http://dx.doi.org/10.1128/aac.00094-07.

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ABSTRACT Histatin-resistant derivatives of Candida albicans strain 132A, generated by successive exposure to increasing concentrations of histatin 3, were previously reported to be similar to the parent strain in their histatin binding, internalization, oxygen consumption, ATP efflux, and histatin degradation. Proteomic analysis of further histatin-resistant secondary derivatives of this series revealed that 59 proteins were differentially expressed compared to the parental strain. Of these 59 proteins, 3 were absent in histatin-resistant secondary derivatives and 11 were absent in the parent strain. Of the proteins absent in the histatin-resistant derivatives, the most notable was elongation factor 2, a target for the natural antifungal sordarin. Of the proteins absent in the parent strain but present in histatin-resistant derivatives, those identified included isocitrate lyase (Icl1p), fructose biphosphate aldolase (Fba1p), pyruvate decarboxylase (Pdc2p), and ketol-acid reductoisomerase (Ilv5p). The present secondary derivatives showed significantly decreased rates of oxygen consumption and histatin 3-mediated ATP release compared to the parent strain and also showed stability of the histatin-resistant phenotype. A significant (twofold) decrease in transcript levels of the potassium transporter encoded by TRK1, a critical mediator of histatin killing, was found in only one of the secondary histatin-resistant derivatives compared to the parent strain. The sequential exposure of C. albicans to histatin 3 described here resulted in the induction or selection of a phenotype with impaired metabolic function. The results support an important role for metabolic pathways in the histatin resistance mechanism and suggest that there may be several intracellular targets for histatin 3 in C. albicans.

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12

Dassanayake, R., L. Cao, L. Samaranayake, and T. Berges. "Characterization, heterologous expression and functional analysis of mevalonate diphosphate decarboxylase gene (MVD) of Candida albicans." Molecular Genetics and Genomics 267, no. 3 (May 2002): 281–90. http://dx.doi.org/10.1007/s00438-002-0648-7.

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13

Stratford, Malcolm, Andrew Plumridge, and David B. Archer. "Decarboxylation of Sorbic Acid by Spoilage Yeasts Is Associated with the PAD1 Gene." Applied and Environmental Microbiology 73, no. 20 (August 31, 2007): 6534–42. http://dx.doi.org/10.1128/aem.01246-07.

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ABSTRACT The spoilage yeast Saccharomyces cerevisiae degraded the food preservative sorbic acid (2,4-hexadienoic acid) to a volatile hydrocarbon, identified by gas chromatography mass spectrometry as 1,3-pentadiene. The gene responsible was identified as PAD1, previously associated with the decarboxylation of the aromatic carboxylic acids cinnamic acid, ferulic acid, and coumaric acid to styrene, 4-vinylguaiacol, and 4-vinylphenol, respectively. The loss of PAD1 resulted in the simultaneous loss of decarboxylation activity against both sorbic and cinnamic acids. Pad1p is therefore an unusual decarboxylase capable of accepting both aromatic and aliphatic carboxylic acids as substrates. All members of the Saccharomyces genus (sensu stricto) were found to decarboxylate both sorbic and cinnamic acids. PAD1 homologues and decarboxylation activity were found also in Candida albicans, Candida dubliniensis, Debaryomyces hansenii, and Pichia anomala. The decarboxylation of sorbic acid was assessed as a possible mechanism of resistance in spoilage yeasts. The decarboxylation of either sorbic or cinnamic acid was not detected for Zygosaccharomyces, Kazachstania (Saccharomyces sensu lato), Zygotorulaspora, or Torulaspora, the genera containing the most notorious spoilage yeasts. Scatter plots showed no correlation between the extent of sorbic acid decarboxylation and resistance to sorbic acid in spoilage yeasts. Inhibitory concentrations of sorbic acid were almost identical for S. cerevisiae wild-type and Δpad1 strains. We concluded that Pad1p-mediated sorbic acid decarboxylation did not constitute a significant mechanism of resistance to weak-acid preservatives by spoilage yeasts, even if the decarboxylation contributed to spoilage through the generation of unpleasant odors.

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14

Choi, Jae-Yeon, Raymond Black, HeeJung Lee, James Di Giovanni, Robert C. Murphy, Choukri Ben Mamoun, and Dennis R. Voelker. "An improved and highly selective fluorescence assay for measuring phosphatidylserine decarboxylase activity." Journal of Biological Chemistry 295, no. 27 (May 19, 2020): 9211–22. http://dx.doi.org/10.1074/jbc.ra120.013421.

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Phosphatidylserine decarboxylases (PSDs) catalyze the conversion of phosphatidylserine (PS) to phosphatidylethanolamine (PE), a critical step in membrane biogenesis and a potential target for development of antimicrobial and anti-cancer drugs. PSD activity has typically been quantified using radioactive substrates and products. Recently, we described a fluorescence-based assay that measures the PSD reaction using distyrylbenzene-bis-aldehyde (DSB-3), whose reaction with PE produces a fluorescence signal. However, DSB-3 is not widely available and also reacts with PSD's substrate, PS, producing an adduct with lower fluorescence yield than that of PE. Here, we report a new fluorescence-based assay that is specific for PSD and in which the presence of PS causes only negligible background. This new assay uses 1,2-diacetyl benzene/β-mercaptoethanol, which forms a fluorescent iso-indole-mercaptide conjugate with PE. PE detection with this method is very sensitive and comparable with detection by radiochemical methods. Model reactions examining adduct formation with ethanolamine produced stable products of exact masses (m/z) of 342.119 and 264.105. The assay is robust, with a signal/background ratio of 24, and can readily detect formation of 100 pmol of PE produced from Escherichia coli membranes, Candida albicans mitochondria, or HeLa cell mitochondria. PSD activity can easily be quantified by sequential reagent additions in 96- or 384-well plates, making it readily adaptable to high-throughput screening for PSD inhibitors. This new assay now enables straightforward large-scale screening for PSD inhibitors against pathogenic fungi, antibiotic-resistant bacteria, and neoplastic mammalian cells.

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15

Petrényi, Katalin, Cristina Molero, Zoltán Kónya, Ferenc Erdődi, Joaquin Ariño, and Viktor Dombrádi. "Analysis of Two Putative Candida albicans Phosphopantothenoylcysteine Decarboxylase / Protein Phosphatase Z Regulatory Subunits Reveals an Unexpected Distribution of Functional Roles." PLOS ONE 11, no. 8 (August 9, 2016): e0160965. http://dx.doi.org/10.1371/journal.pone.0160965.

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16

Brand, Alexandra, Donna M. MacCallum, Alistair J. P. Brown, Neil A. R. Gow, and Frank C. Odds. "Ectopic Expression of URA3 Can Influence the Virulence Phenotypes and Proteome of Candida albicans but Can Be Overcome by Targeted Reintegration of URA3 at the RPS10 Locus." Eukaryotic Cell 3, no. 4 (August 2004): 900–909. http://dx.doi.org/10.1128/ec.3.4.900-909.2004.

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ABSTRACT Uridine auxotrophy, based on disruption of both URA3 alleles in diploid Candida albicans strain SC5314, has been widely used to select gene deletion mutants created in this fungus by “Ura-blasting” and PCR-mediated disruption. We compared wild-type URA3 expression with levels in mutant strains where URA3 was positioned either within deleted genes or at the highly expressed RPS10 locus. URA3 expression levels differed significantly and correlated with the specific activity of Ura3p, orotidine 5′-monophosphate decarboxylase. Reduced URA3 expression following integration at the GCN4 locus was associated with an attenuation of virulence. Furthermore, a comparison of the SC5314 (URA3) and CAI-4 (ura3) proteomes revealed that inactivation of URA3 caused significant changes in the levels of 14 other proteins. The protein levels of all except one were partially or fully restored by the reintegration of a single copy of URA3 at the RPS10 locus. Transcript levels of genes expressed ectopically at this locus in reconstituted heterozygous mutants also matched the levels found when the genes were expressed at their native loci. Therefore, phenotypic changes in C. albicans can be associated with the selectable marker rather than the target gene. Reintegration of URA3 at an appropriate expression locus such as RPS10 can offset most problems related to the phenotypic changes associated with gene knockout methodologies.

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17

Martinez, J. P., J. L. Lopez-Ribot, M. L. Gil, R. Sentandreu, and J. Ruiz-Herrera. "Inhibition of the dimorphic transition of Candida albicans by the ornithine decarboxylase inhibitor 1,4-diaminobutanone: alterations in the glycoprotein composition of the cell wall." Journal of General Microbiology 136, no. 10 (October 1, 1990): 1937–43. http://dx.doi.org/10.1099/00221287-136-10-1937.

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18

Ells, Ruan, Johan L. F. Kock, and Carolina H. Pohl. "Candida albicans or Candida dubliniensis?" Mycoses 54, no. 1 (December 2, 2010): 1–16. http://dx.doi.org/10.1111/j.1439-0507.2009.01759.x.

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19

Wilson, Duncan. "Candida albicans." Trends in Microbiology 27, no. 2 (February 2019): 188–89. http://dx.doi.org/10.1016/j.tim.2018.10.010.

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20

Klotz, Stephen A., Mubashir Zahid, William R. Bartholomew, Pedro M. Revera, and Salim Butrus. "Candida albicans." Cornea 15, no. 1 (January 1996): 102???104. http://dx.doi.org/10.1097/00003226-199601000-00020.

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21

Thompson, June. "Candida albicans." Primary Health Care 7, no. 9 (October 1, 1989): 8. http://dx.doi.org/10.7748/phc.7.9.8.s11.

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22

Eagle, Kim, and David M. Phillips. "Candida albicans." New England Journal of Medicine 328, no. 18 (May 6, 1993): 1322. http://dx.doi.org/10.1056/nejm199305063281807.

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23

Witek-Janusek, Linda, Cynthia Cusack, and Herbert L. Mathews. "Candida albicans." Dimensions of Critical Care Nursing 17, no. 5 (September 1998): 243–55. http://dx.doi.org/10.1097/00003465-199809000-00002.

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24

Berman, Judith. "Candida albicans." Current Biology 22, no. 16 (August 2012): R620—R622. http://dx.doi.org/10.1016/j.cub.2012.05.043.

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&NA;. "Candida albicans antigen." Reactions Weekly &NA;, no. 1077 (November 2005): 9. http://dx.doi.org/10.2165/00128415-200510770-00025.

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26

Zellweger, C., and S. Zimmerli. "Candida-albicans-Endokarditis." DMW - Deutsche Medizinische Wochenschrift 128, no. 19 (May 2003): 1048–50. http://dx.doi.org/10.1055/s-2003-39101.

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27

Woei Lee, James Burnie, and Ruth Matthews. "Fingerprinting Candida albicans." Journal of Immunological Methods 93, no. 2 (November 1986): 177–82. http://dx.doi.org/10.1016/0022-1759(86)90186-9.

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Müller, Johannes. "Candida albicans im elektronenoptischen Bild: Candida albicans in electronmicroscopical presentation." Mycoses 42, S1 (April 1999): 5–11. http://dx.doi.org/10.1111/j.1439-0507.1999.tb04520.x.

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29

Pichová, Iva, Libuše Pavlíčková, Jiří Dostál, Elena Dolejší, Olga Hrušková-Heidingsfeldová, Jan Weber, Tomáš Ruml, and Milan Souček. "Secreted aspartic proteases of Candida albicans , Candida tropicalis , Candida parapsilosis and Candida lusitaniae." European Journal of Biochemistry 268, no. 9 (May 1, 2001): 2669–77. http://dx.doi.org/10.1046/j.1432-1327.2001.02152.x.

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30

Naglik, Julian R. "Candida Immunity." New Journal of Science 2014 (August 25, 2014): 1–27. http://dx.doi.org/10.1155/2014/390241.

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The human pathogenic fungus Candida albicans is the predominant cause of both superficial and invasive forms of candidiasis. C. albicans primarily infects immunocompromised individuals as a result of either immunodeficiency or intervention therapy, which highlights the importance of host immune defences in preventing fungal infections. The host defence system utilises a vast communication network of cells, proteins, and chemical signals distributed in blood and tissues, which constitute innate and adaptive immunity. Over the last decade the identity of many key molecules mediating host defence against C. albicans has been identified. This review will discuss how the host recognises this fungus, the events induced by fungal cells, and the host innate and adaptive immune defences that ultimately resolve C. albicans infections during health.

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31

Pathak, Apurva K., Sanjay Sharma, and Pallavi Shrivastva. "Multi-species biofilm of Candida albicans and non-Candida albicans Candida species on acrylic substrate." Journal of Applied Oral Science 20, no. 1 (February 2012): 70–75. http://dx.doi.org/10.1590/s1678-77572012000100013.

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Sang, H., B. Wu, and X. Zhang. "Cervical lymphadenitis caused by Candida albicans. Zervikale Lymphadenitis durch Candida albicans." Mycoses 46, no. 9-10 (October 2003): 422–24. http://dx.doi.org/10.1046/j.0933-7407.2003.00915.x.

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Whibley, Natasha, and Sarah L. Gaffen. "Beyond Candida albicans: Mechanisms of immunity to non-albicans Candida species." Cytokine 76, no. 1 (November 2015): 42–52. http://dx.doi.org/10.1016/j.cyto.2015.07.025.

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34

KERRIDGE, DAVID, MARCO FASOLI, and FRANCES J. WAYMAN. "Drug Resistance in Candida albicans and Candida glabrata." Annals of the New York Academy of Sciences 544, no. 1 Antifungal Dr (December 1988): 245–59. http://dx.doi.org/10.1111/j.1749-6632.1988.tb40410.x.

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35

Cutler, J. E., P. M. Glee, and H. L. Horn. "Candida albicans- and Candida stellatoidea-specific DNA fragment." Journal of Clinical Microbiology 26, no. 9 (1988): 1720–24. http://dx.doi.org/10.1128/jcm.26.9.1720-1724.1988.

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36

Fotedar, R., and S. S. A. Al-Hedaithy. "Identification of chlamydospore-negative Candida albicans using CHROMagar Candida medium. Identifizierung von Chlamydosporen-negativer Candida albicans auf CHROMagar Candida-Medium." Mycoses 46, no. 3-4 (March 4, 2003): 96–103. http://dx.doi.org/10.1046/j.1439-0507.2003.00867.x.

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Barchiesi, Francesco, Elisabetta Spreghini, Serena Tomassetti, Agnese Della Vittoria, Daniela Arzeni, Esther Manso, and Giorgio Scalise. "Effects of Caspofungin against Candida guilliermondii and Candida parapsilosis." Antimicrobial Agents and Chemotherapy 50, no. 8 (August 2006): 2719–27. http://dx.doi.org/10.1128/aac.00111-06.

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ABSTRACT The in vitro activity of caspofungin (CAS) was investigated against 28 yeast isolates belonging to Candida albicans (n = 5), Candida guilliermondii (n = 10), and Candida parapsilosis (n = 13). CAS MICs obtained by broth dilution and Etest methods clearly showed a rank order of susceptibility to the echinocandin compound with C. albicans > C. parapsilosis > C. guilliermondii. Similarly, time-kill assays performed on selected isolates showed that CAS was fungistatic against C. albicans and C. parapsilosis, while it did not exert any activity against C. guilliermondii. In a murine model of systemic candidiasis, CAS given at doses as low as 1 mg/kg of body weight/day was effective at reducing the kidney burden of mice infected with either C. albicans or C. guilliermondii isolates. Depending on the isolate tested, mice infected with C. parapsilosis responded to CAS given at 1 and/or 5 mg/kg/day. However, the overall CFU reduction for C. guilliermondii and C. parapsilosis was approximately 100-fold less than that for C. albicans. Our study shows that CAS was active in experimental systemic candidiasis due to C. guilliermondii and C. parapsilosis, but this activity required relatively high drug dosages.

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Odds, Frank C., and David Kerridge. "Morphogenesis in Candida Albicans." CRC Critical Reviews in Microbiology 12, no. 1 (January 1985): 45–93. http://dx.doi.org/10.3109/10408418509104425.

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Serracarbassa, Pedro Duraes, and Patrícia Dotto. "Endoftalmite por Candida albicans." Arquivos Brasileiros de Oftalmologia 66, no. 5 (October 2003): 701–7. http://dx.doi.org/10.1590/s0004-27492003000500027.

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Tsukahara, Tohru, and Yoshinori Nozawa. "Dimorphism of Candida albicans." Japanese Journal of Medical Mycology 30, no. 2 (1989): 92. http://dx.doi.org/10.3314/jjmm1960.30.92.

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Tuon, Felipe Francisco, and Antonio Carlos Nicodemo. "Candida albicans skin abscess." Revista do Instituto de Medicina Tropical de São Paulo 48, no. 5 (October 2006): 301–2. http://dx.doi.org/10.1590/s0036-46652006000500012.

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Subcutaneous candidal abscess is a very rare infection even in immunocompromised patients. Some cases are reported when breakdown in the skin occurs, as bacterial cellulites or abscess, iatrogenic procedures, trauma and parenteral substance abuse. We describe a case of Candida albicans subcutaneous abscess without fungemia, which can be associated with central venous catheter.

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&NA;. "Multiresistant Candida albicans isolates." Inpharma Weekly &NA;, no. 1066 (December 1996): 18. http://dx.doi.org/10.2165/00128413-199610660-00039.

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Reid, Gladys M. "Candida albicans and selenium." Medical Hypotheses 60, no. 2 (February 2003): 188–89. http://dx.doi.org/10.1016/s0306-9877(02)00355-9.

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Nguyen, T. B., N. Galezowski, J. Crouzet, F. Laroche, and P. Blanche. "Spondylodiscites à Candida albicans." La Revue de Médecine Interne 17 (January 1996): 419s—420s. http://dx.doi.org/10.1016/s0248-8663(97)80991-5.

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Guillerm, C., G. Kerdraon, B. Lejeune, A. M. Simitzis-Le Flohic, D. Parent, and D. Alix. "Candida albicans et prématurés." Médecine et Maladies Infectieuses 15, no. 12 (December 1985): 755–56. http://dx.doi.org/10.1016/s0399-077x(85)80331-0.

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Gow, Neil A. R. "Candida albicans Switches Mates." Molecular Cell 10, no. 2 (August 2002): 217–18. http://dx.doi.org/10.1016/s1097-2765(02)00608-1.

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Gower, D. J., K. Crone, E. Alexander, and D. L. Kelly. "Candida albicans shunt infection." Neurosurgery 19, no. 1 (July 1986): 111???3. http://dx.doi.org/10.1097/00006123-198607000-00018.

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Vialas, Vital, Zhi Sun, Carla Verónica Loureiro y Penha, Montserrat Carrascal, Joaquín Abián, Lucía Monteoliva, Eric W. Deutsch, Ruedi Aebersold, Robert L. Moritz, and Concha Gil. "A Candida albicans PeptideAtlas." Journal of Proteomics 97 (January 2014): 62–68. http://dx.doi.org/10.1016/j.jprot.2013.06.020.

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Sundstrom, Paula. "Adhesins in Candida albicans." Current Opinion in Microbiology 2, no. 4 (August 1999): 353–57. http://dx.doi.org/10.1016/s1369-5274(99)80062-9.

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Arocker-Mettinger, E., V. Huber-Spitzy, R. Haddad, and G. Grabner. "Keratomykose durch Candida albicans." Klinische Monatsblätter für Augenheilkunde 193, no. 08 (August 1988): 192–94. http://dx.doi.org/10.1055/s-2008-1050245.

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