(XLS 10 KB) Additional file 7: Table S4 – Oligonucleotides for Ga

(XLS 10 KB) Additional file 7: Table S4 – Oligonucleotides for Gateway(r) recombination. (XLS 8 KB) Additional file 8: Table S5 – Oligonucleotides for real-time RT-PCR and probe amplification (Southern blot). (XLS 7 KB) References 1. Tetaud E, Lecuix I, Sheldrake T, Baltz T, Fairlamb AH: A new expression vector for Crithidia fasciculata and Leishmania. Mol Biochem Parasitol 2002,120(2):195–204.PubMedCrossRef 2. Schimanski B, Nguyen TN, Gunzl A: Highly efficient tandem affinity purification of trypanosome protein complexes based on a novel epitope combination. Eukaryot Cell 2005,4(11):1942–1950.PubMedCrossRef

3. Martinez-Calvillo S, Lopez I, Hernandez R: pRIBOTEX expression Fosbretabulin vector: a pTEX derivative for a rapid selection of Trypanosoma cruzi transfectants. Gene 1997,199(1–2):71–76.PubMedCrossRef 4. Xu D, Brandan CP, Basombrio MA, Tarleton RL: Evaluation of high efficiency gene knockout strategies for Trypanosoma cruzi. BMC Microbiol GDC 0032 order 2009, 9:90.PubMedCrossRef 5. Wirtz E, Leal S, Ochatt C, Cross GA: A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative

genetics in Trypanosoma brucei. Mol Biochem Parasitol 1999,99(1):89–101.PubMedCrossRef 6. Machado CA, Ayala FJ: Nucleotide sequences provide evidence of genetic exchange among distantly related lineages of Trypanosoma cruzi. Proc Natl Acad Sci USA 2001,98(13):7396–7401.PubMedCrossRef 7. Gaunt MW, Yeo M, Frame IA, Stothard JR, Carrasco HJ, Taylor MC, Mena SS, Veazey P, Miles GA, Acosta N, et al.: Mechanism of genetic exchange in American trypanosomes. Nature 2003,421(6926):936–939.PubMedCrossRef 8. Vanhamme L, Pays E: Pevonedistat molecular weight Control of gene Y-27632 2HCl expression

in trypanosomes. Microbiol Rev 1995,59(2):223–240.PubMed 9. Van der Ploeg LH, Liu AY, Michels PA, De Lange T, Borst P, Majumder HK, Weber H, Veeneman GH, Van Boom J: RNA splicing is required to make the messenger RNA for a variant surface antigen in trypanosomes. Nucleic Acids Res 1982,10(12):3591–3604.PubMedCrossRef 10. LeBowitz JH, Smith HQ, Rusche L, Beverley SM: Coupling of poly(A) site selection and trans-splicing in Leishmania. Genes Dev 1993,7(6):996–1007.PubMedCrossRef 11. Kelly JM, Ward HM, Miles MA, Kendall G: A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania. Nucleic Acids Res 1992,20(15):3963–3969.PubMedCrossRef 12. Taylor MC, Kelly JM: pTcINDEX: a stable tetracycline-regulated expression vector for Trypanosoma cruzi. BMC Biotechnol 2006, 6:32.PubMedCrossRef 13. Wirtz E, Hartmann C, Clayton C: Gene expression mediated by bacteriophage T3 and T7 RNA polymerases in transgenic trypanosomes. Nucleic Acids Res 1994,22(19):3887–3894.PubMedCrossRef 14. Wirtz E, Clayton C: Inducible gene expression in trypanosomes mediated by a prokaryotic repressor. Science 1995,268(5214):1179–1183.PubMedCrossRef 15. Bellofatto V, Cross GA: Expression of a bacterial gene in a trypanosomatid protozoan. Science 1989,244(4909):1167–1169.

coli β-galactosidase The identities of all strain constructs wer

coli β-galactosidase. The identities of all strain constructs were confirmed by DNA sequencing. Construction of the ΔompC::kan E. coli To construct an E. coli strain defective in OmpC production, we chose JW2203 from the Keio collection (CGSC#9781), which carries the desired ΔompC768::kan mutation [45], as our donor strain for P1 transduction. However, for some unknown reasons, we were unable to successfully P1-transduce the chromosomal region containing the ΔompC768::kan mutation into our XL1 Blue strain. To further our goal of determining the effect of phage morphology on plaque size, we constructed the strain IN731 by P1-transducing the mutation into

the recipient RXDX-101 solubility dmso strain SYP124, which is essentially the strain MG1655 but carrying the necessary ω-fragment expressed from lcaZΔM15 (unpublished data). Plaque size was determined by Selleck RG7420 plating

on SYP124 and its ΔompC counterpart, IN731. Standard PCR and DNA sequencing Standard PCR reactions were performed using the following conditions: one cycle of 95°C for 1 min, followed by 30 cycles of 95°C for 30 s, 50°C for 30 s, and 72°C for several minutes, depending on the template size (using an extension of 1 min/Kb). PfuUltra (Stratagene, La Jolla, CA), a high-fidelity thermostable DNA polymerase, was used for amplification. The BigDye Terminator Cycle Sequencing kit (v3.1; ABI) was used for DNA sequencing according to the manufacturer’s recommendation. Phage plating To minimize variation, all plating conditions were

standardized. A total of ~100 A-1210477 in vivo phages were mixed with fresh 100 μL of E. coli cells, prepared by two-fold dilution Florfenicol of overnight culture and grown at 37°C for 90 min in TB medium (5 g NaCl and 10 g Tryptone in 1 L H2O), and then incubated at room temperature for 20 min for pre-adsorption. In our experience, >90% of phages would be adsorbed onto the cells during the pre-adsorption period. The mixture was then mixed with 3 mL of molten H-top agar with IPTG and X-gal and overlaid on plates containing 40 mL LB-agar. Both the LB plates and the H-top agar were freshly prepared a few hours before use. The plates were then incubated for 18-22 h at 37°C before plaque size determination [17]. In our experience, the plaques would have reached their maximum size within this incubation period. Determination of phage adsorption rate The protocol for adsorption rate determination, which is essentially the same as that used by Schlesinger [51], has been described previously [17]. Briefly, ~4.5 × 104 phages were mixed with 10 mL of E. coli XL1 Blue stationary phase cells (grown at 37°C for overnight in TB medium of 1% tryptone and 0.5% NaCl) in a flask with constant shaking (250 rpm/min) at 37°C.

These protein profiles were designated FN, SN, FJ and SJ, indicat


JS32 in fructose, and JS32 in sorbitol fermentation medium, respectively. On the SN and FN proteome profiles, 901 and 903 spots were identified, respectively, but only 39 spots had changed in abundance, in them 27 were more abundant in N16961 cultured in sorbitol fermentation medium (SN), 12 were more abundant in check details sample of FN (Fig. 3) [also see Additional file1]. Such similarity also existed in the SJ and FJ profiles, with 34 differential spots found, 17 were more abundant in samples of SJ and FJ respectively (Fig. 3) [also see Additional file1]. All of the 73 differential protein spots were analyzed by MALDI-MS, and 71 spots significantly matched known proteins (one spot of FJ and one spot of SN were not identified)

[see Additional file1]. Sixty-two percent of the spots were identified as proteins involved in energy metabolism and central intermediary metabolism, and six spots were identified as transport/see more binding proteins. Figure 3 2-DE gels of whole cell proteins of V. cholerae strains JS32 and N16961 cultured in sorbitol and fructose fermentation media. The comparative proteins (comparison between SN/FN NVP-BSK805 ic50 and SJ/FJ) were marked and numbered on their more abundant maps. Out of 73 total differential spots identified in the SN/FN and SJ/FJ comparisons, 10 common signified potential proteins of these two comparison groups may be involved in the difference between the sorbitol and fructose metabolism


As cutoff value for gene essentiality a >99% decrease in the biom

As cutoff value for gene essentiality a >99% decrease in the biomass production after the gene deletion was used, as described by Thomas et al. [24]. For the Bge strain network, a set of essential genes was determined ranging between 76.1 % (minimal medium) and 72.3 % (with added glycerol) of the total genes comprised in the model. With the Pam network we found a genetic essentiality between 79.6 % (minimal medium) and 73.5 % (with added fumarate, L-malate or glycerol). Discussion Uncultivable bacteria can be studied by in silico simulations In this paper we

describe the genome-scale metabolic networks corresponding to two strains of B. cuenoti, Bge and Pam, the endosymbiotic selleck inhibitor bacteria of the cockroaches B. germanica and P. americana, respectively.

Despite the approximately 140-Myr of parallel evolution, both metabolic networks showed striking conservation Proteasome inhibitor and we decided to compare their functionality by means of a stoichiometric approach such as FBA. This computational methodology has already been successfully used in a study of the metabolic network robustness of B. aphidicola, the primary endosymbiont of aphids, in comparison to E. coli [24] and for the simulation of reductive evolution in endosymbionts [25, 26]. Thus, FBA represents a valid strategy for the functional study of those bacterial species that pose see more important obstacles to their empirical study, as it is the case of the uncultivable endosymbionts. In this work we used the E. coli model as a reference since to the best of our knowledge there are no empirical data on the biomass function of any members within the phylum Bacteroidetes. In the absence of information related to real biomass composition of the modeled Demeclocycline organism, the use of the equations

of E. coli is considered a reliable approach and an acceptable starting point [19, 27–29]. The simulations allowed us to identify the minimal environmental components for a functional metabolic network (Fig. 2). For instance, both Blattabacterium networks show a strict dependence on L-Gln supply from the host due to the absence of glutamine synthase in both endosymbionts. This dependence of the functionality on the availability of some chemical species may also suggest a possible regulatory role of the external medium in the metabolic behavior of the bacterium. In other biological systems, like the nitrogen-fixing nodules of Leguminosae, oxygen availability modulation by the host has been suggested as a mechanism of punishment to cheaters in the symbiotic relationship [30]. Our in silico simulations (Fig. 5) suggest that access to L-Gln and/or oxygen is a good candidate for a control mechanism of cockroaches over their endosymbiotic population.

Since extracellular ATP level was found to decrease during the st

Since extracellular ATP level was found to decrease during the stationary phase of growth (Figure 3), we determined if the extracellular ATP is beneficial to bacteria at stationary

phase and if ATP Selleck Combretastatin A4 supplement could enhance the JNJ-26481585 chemical structure bacterial survival. Salmonella and E. coli were cultured for 7 days and exogenous ATP was added to the cultures. We chose to use 10 μM or 100 μM to supplement bacterial culture since the ATP depletion assays showed that Salmonella and E. coli depletes ATP at approximately 5 μM/hr (Figure 5A and B) and high concentrations of ATP would allow ATP level in the bacterial cultures to stay elevated for an extended period of time. Survival of bacteria was determined by the ratio of bacterial CFU/mL after 7 days

of incubation to that after 1 day of incubation (Figure 6). Our results showed that an ATP supplement increased the survival of the bacterial strains tested. The dosage response varied in different strains. Salmonella responded best to 10 μM ATP, while E. coli responded equally well to 10 μM and 100 μM ATP. The results suggest that extracellular ATP can affect bacterial survival (Figure 6). Figure 6 ATP supplementation increases the stationary survival of bacteria. E. coli K12, Salmonella enterica Serovar Enteritidis (SE) or Salmonella enterica Serovar Typhimurium (ST) was cultured in M9 minimal medium or M9 minimal medium supplemented with 10 μM or 100 μM of ATP. The rate of survival was determined by comparing bacterial CFU/mL after 7 days of incubation to that after 1 day of incubation. The experiment Alanine-glyoxylate transaminase was performed three times and results are from a representative experiment performed

in triplicate. LY2603618 Error bars represent standard deviation. * p < 0.05, Student’s t-test. Extracellular ATP was detected in several Gram-negative and Gram-positive bacterial species In addition to Gram-negative bacterial species E. coli and Salmonella, other bacterial species were tested for the presence of ATP in the culture medium to determine if the phenomenon is limited to Enterobacteriaceae or is present in more bacterial families such as Acinetobacter, Klebsiella, Pseudomonas and Staphylococcus. Clinical isolates of various human pathogenic bacterial species were tested for the presence of ATP in culture medium during their growth in vitro and the ATP levels in the culture supernatant were determined. The peak values of the ATP concentration in the culture medium and the incubation time when the ATP levels peaked are listed in Table 5. ATP was detected in the culture supernatant of all bacterial strains tested. Although the levels and peak time points varied from strain to strain, all bacterial strains displayed the presence of growth phase dependent ATP in the culture supernatant (Table 5). This result suggests that the presence of extracellular ATP is not restricted to Enterobacteriaceae and instead can be detected in many bacterial families.

Electronic supplementary material Additional file 1: Cloning, exp

Electronic supplementary material Additional file 1: Cloning, expression, Natural Product Library concentration purification and immunodetection of PknG. (A) Cloning of pknG in pTriEx4 vector; M, 500 bp DNA ladder; 1, pTriEx4-pknG digested with BamHI, right oriented recombinants will produce 0.7 kb fragment; selleck 2, pTriEx4-pknG digested with HindIII, recombinants will produce 2.2 kb fragment; 3, pTriEx4 vector digested with HindIII; 4, pTriEx4-pknG undigested, (B) overexpression and

purification of PknG; 1, cells transformed with vector; 2, cells transformed with recombinant; 3, cells transformed with vector and induced with IPTG; 4, cells transformed with recombinant and induced with IPTG; 5 and 6, purified PknG. (C) Immunodetection of PknG in mycobacteria; equal amounts of total cell lysates (20 μg) were resolved by SDS-PAGE and immunoblotted with polyclonal antiserum against PknG (1) MS (2) BCG (3) Ra (4) Rv (D) Cloning of pknG in pMV361 vector; M, 500 bp DNA ladder; 1, pMV361 vector uncut; 2, pMV361-pknG uncut; 3, pMV361 digested with EcoRI and HindIII; 4, pMV361-pknG digested with EcoRI and HindIII; (E) PCR of pknG from genomic DNA; M, 1 kb DNA ladder; Selleckchem FRAX597 1, MS; 2, MS-pMV361-pknG; (F) expression of PknG in MS; equal amounts of total cell lysates (20 μg) were resolved by SDS-PAGE and immunoblotted with polyclonal antiserum against PknG, (1) MS-pMV361 (2) MS-pMV361-pknG (3) MS and (4) Rv. (TIFF 859

KB) References 1. Koul A, Herget T, Klebl B, Ullrich A: Interplay between mycobacteria and host signalling pathways. Nat Rev Microbiol 2004, 2:189–202.CrossRefPubMed 2. Malik ZA, Denning GM, Kusner DJ: Inhibition of ca 2+ signaling by Mycobacterium tuberculosis is associated with reduced phagosome-lysosome fusion

an d increased survival within human macrophages. J Exp Med 2000, 191:287–302.CrossRefPubMed 3. Malik ZA, Iyer SS, Kusner DJ:Mycobacterium tuberculosis phagosomes exhibit altered calmodulin-dependent signal transduction: contribution to inhibition of phagosome-lysosome fusion and intracellular survival in human macrophages. J Immunol 2001, 166:3392–3401.PubMed Tyrosine-protein kinase BLK 4. Rao KMK: MAP kinase activation in macrophages. J Leukoc Biol 2001, 69:3–10.PubMed 5. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor T, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393:537–544.CrossRefPubMed 6. Av-Gay Y, Everett M: The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol 2000, 8:238–244.CrossRefPubMed 7.

TZ and YL wrote the paper All authors read and approved the fina

TZ and YL wrote the paper. All authors read and approved the final manuscript.”

[1]. The most economically important of these is the cosmopolitan sweetpotato whitefly Bemisia tabaci (Gennadius), which is a species complex of more than 20 biotypes. The B and Q biotypes, among the most predominant and damaging worldwide, differ in many biological parameters, including resistance to insecticides, ability to damage ARN-509 supplier plants [2] and tolerance to LGK-974 cell line environmental conditions [3]. Another important whitefly insect pest is the greenhouse whitefly Trialeurodes vaporariorum

(Westwood) which is less important as a virus vector, but causes serious damage by direct feeding on plants. Whereas T. vaporariorum can be identified based on external morphology (Figure 1), B. tabaci biotypes are only well defined by DNA markers [4]. Figure 1 Whiteflies in Croatia. Demonstration of heavy whitefly infestations on cucumbers grown in the coastal part of Croatia (A), and external phenotypical differences between B. tabaci and T. vaporariorum (B). Symbiosis is quite common among known whitefly species. Both B. tabaci and T. vaporariorum harbor the primary obligatory bacterium Portiera aleyrodidarum, which supplements their unbalanced diet [5]. B. tabaci can also harbor a diverse array of facultative PXD101 in vitro secondary symbionts, including the Gammaproteobacteria Racecadotril Arsenophonus (Enterobacteriales), Hamiltonella (Enterobacteriales) [5, 6], Fritschea (Chlamydiales) [7] and Cardinium (Bacteroidetes)


Similar observations were made for non-toxigenic strains [10] sho

Similar observations were made for non-toxigenic strains [10] showing that also pharyngeal

Detroit 562 cells can be invaded by C. diphtheriae and that viable intracellular bacteria can be detected up to 48 h after infection. While host cell receptors and invasion-associated proteins of the pathogen are still unknown, bacterial adhesion factors have been recently at least partially characterized on the molecular level. BVD-523 manufacturer C. diphtheriae strain NCTC13129 is able to assemble three distinct types of pili on its surface [11, 12]. Mutant analyses showed that the SpaA-type pilus is sufficient for adhesion of this strain to pharynx cells, shaft proteins are not crucial for pathogen-host interaction, and adherence to pharyngeal cells is greatly diminished when minor pili proteins SpaB and SpaC are lacking [13]. The results obtained in other studies indicated the existence of additional proteins besides pili subunits selleck products involved in adhesion buy GSK2879552 to larynx, pharynx, and lung epithelial cells, since a total loss of attachment to pharyngeal cells due to mutagenesis of pili- and sortase-encoding genes could not be observed and attachment to lung or larynx cells was less affected by the mutations. This is in line with a number of studies suggesting the multifactorial mechanism of adhesion (reviewed in [14]). Furthermore, Hirata and co-workers [7, 15] described three distinct patterns of adherence to HEp-2 cells, an aggregative, a

localized, and a diffuse form, an observation that hints also to the existence of several adhesion factors and different receptors on the host cell surface. The involvement of different C. diphtheriae proteins to adherence to

distinct cell types is further supported by work on adhesion to human erythrocytes, showing that non-fimbrial surface proteins 67p and 72p, which were up to now only characterized by their apparent mass, are involved in this process [16]. Interestingly, besides strain-specific differences in adherences (see references cited above), Beta adrenergic receptor kinase also growth-dependent effects were observed. In a study using two toxigenic C. diphtheriae strains and erythrocytes as well as HEp-2 cells, de Oliveira Moreira and co-workers [17] showed an effect of iron supply on hemagglutination and lectin binding properties of the microorganisms. In this study, we present a characterization of different non-toxigenic C. diphtheriae and a toxin-producing strain with respect to adhesion to and internalization into epithelial cells. Analyses reveal significant strain-specific differences in host colonization and macromolecular surface structures of the studied strains, while neither of the strains evoked rapid cell damage under the conditions tested. Results Adhesion of C. diphtheriae to epithelial cells, invasion of host cells and intracellular survival In this study, adhesion of six non-toxigenic strains and one toxin-producing C. diphtheriae to Detroit562 cells was analyzed (Fig. 1).

The A mode especially is subject to change for high Se concentrat

The A mode especially is subject to change for high Se concentrations. This fact makes this mode a sensitive NVP-HSP990 mw indicator of variations

in the concentration x. The high-frequency E mode is broadened as in the original data of Richter and Becker [cf. their Figure five(a)]. The position of the A and the higher E mode was weighted stronger than the position of the relatively constant A mode and the lower E mode. The value of x was determined to be 0.7, corresponding to BST. Figure 3 Raman spectrum of a single nanowire and representation of the Raman data for Bi 2 (Te 1−x Se x ) 3 . (a) Raman spectrum of a nanowire grown at 480°C. Four peaks at 66, 112, 129, and 164 cm −1 are obtained from fitting Lorentzians. The peaks can be assigned to the Raman modes of Bi2Se2Te. (b) Representation of the Raman data for Bi2(Te 1−x Se x )3 for 0

maximum). The diameter (measured height) of the nanowires is 22.0 nm, corresponding to 23 quintuple layers (QLs) with 1 QL = 0.96 nm. We can conclude that these nanowires were grown along the [110] direction. Figure 4 AFM micrographs of Bi 2 Se 2 Te nanowires on Si. Two nanowires are visible which stick together side by side, having a diameter (height) of 22.0 nm or 23 quintuple Thiazovivin purchase layers (QLs). The VLS ARRY-438162 in vivo growth mechanism requires the formation of a catalyst-precursor alloy and the subsequent BCKDHB crystallisation out of the supersaturated solution [22]. A metal alloy particle is typically either found at the tip or the root of the nanowire [23]. The samples show root-catalysed growth as can be seen in Figure

1c. A catalyst particle is found at the base of all of the nanowires investigated at this temperature. Tip-based Bi2Se3 nanowire growth was observed by Kong et al. using 20-nm-diameter Au particles in an identical experiment [24]. In contrast, Alegria et al. reported root-based growth of Bi2Se3 nanostructures from an annealed, 5-nm-thick Au layer using metal-organic chemical vapour deposition [18]. The differing growth mechanism was explained by the use of a gas source instead of a solid precursor. Our study suggests that it is not the growth technique that determines the VLS growth mechanism, but rather the size of the catalytic particle. Above a critical size, the catalytic particle is lifted up by the growing nanowire as observed by Kong et al. This effect can be explained by a catalyst-substrate interaction that depends on the size of the catalyst particle. If the Au catalyst alloys with the SiO2/Si substrate, e.g.

J Clin Microbiol 1998, 36:1271–1276 PubMed 142 Rhead JL, Letley

J Clin Microbiol 1998, 36:1271–1276.PubMed 142. Rhead JL, Selleckchem ABT 263 Letley DP, Mohammadi M, Hussein N, Mohagheghi MA, Eshagh Hosseini M, Atherton JC: A new Helicobacter pylori vacuolating cytotoxin determinant, JPH203 mw the intermediate region, is associated with gastric cancer. Gastroenterology 2007, 133:926–936.PubMedCrossRef 143. McClain MS, Shaffer CL, Israel DA, Peek RM Jr, Cover TL: Genome sequence analysis of Helicobacter pylori strains associated with gastric ulceration and gastric cancer. BMC Genomics 2009, 10:3.PubMedCrossRef 144. Xie W, Zhou C, Huang RH: Structure of tRNA dimethylallyltransferase: RNA modification through a channel. J Mol

Biol 2007, 367:872–881.PubMedCrossRef 145. Blokesch M, Albracht SP, Matzanke BF, Drapal NM, Jacobi A, Bock A: The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J Mol Biol 2004, 344:155–167.PubMedCrossRef 146. Blokesch M, Bock A: Properties

selleck kinase inhibitor of the [NiFe]-hydrogenase maturation protein HypD. FEBS Lett 2006, 580:4065–4068.PubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions MK and YF contributed to informatics analysis and wrote the manuscript. YF carried out experimental verification of sequences of molybdenum-related genes and acetate unless pathway related genes. KY, TT, and IU contributed to informatics analysis. NH and NT

contributed to genome DNA preparation. KO and MH contributed to sequencing and assembly. MY and TA provided the strains. I.K. contributed to design, analysis and writing. All the authors discussed the results and commented on the manuscript. All the authors read and approved the final manuscript.”
“Background Candida albicans is both a commensal and a pathogenic yeast, which is responsible for severe infections in humans, particularly in immunocompromised persons, such as AIDS and cancer patients, diabetics, newborns and the elderly [1, 2]. Although several anti-Candida agents are currently available, such as amphotericin B, azoles and echinocandins, there is clearly a need for new specific anti-fungal agents and drug-targets [3]. The cell wall of C. albicans is an essential organelle that helps to withstand osmotic pressure and determines the shape of the cell. The cell wall is a plastic and dynamic structure, whose macromolecular composition, molecular organization and thickness can greatly vary depending on environmental conditions. The cell wall construction is also tightly controlled in space and time by many genes [4]. Within a host-parasite relationship, the cell wall of C. albicans lies at the crossroads of pathogenicity and therapeutics.