Group X hybrid histidine kinase Chk1 is dispensable for stress adaptation, host–pathogen interactions and virulence in the opportunistic yeast Candida guilliermondii

Navarro-Arias, María J.; Dementhon, Karine; Defosse, Tatiana A.; Foureau, Emilien; Courdavault, Vincent; Clastre, Marc; Gal, Solène Le; Nevez, Gilles; Govic, Yohann Le; Bouchara, Jean‐Philippe; Giglioli-Guivarc’h, Nathalie; Noël, Thierry; Mora-Montes, Héctor M.; Papon, Nicolas

doi:10.1016/j.resmic.2017.04.009

Cited by 8 publications

(10 citation statements)

References 53 publications

(77 reference statements)

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“…In both cases, the reintegrant control strains restored the content of these wall components to levels similar to those found in the WT control strain (Table 3). The phosphomannan content and the porosity to DEAE-dextran are wall parameters that have been correlated with defects in the protein glycosylation pathways (Mora-Montes et al, 2007, 2010; Cheng et al, 2011; Navarro-Arias et al, 2016, 2017; Perez-Garcia et al, 2016; Lozoya-Perez et al, 2019). The phosphomannan content was reduced in both null mutants, and this was accompanied by an increment in the cell wall porosity (Table 3).…”

Section: Resultsmentioning

confidence: 99%

“…The reintegrant control strains showed a similar ability to bind Con A-FITC than the WT cells (Figure 3 and Supplementary Figure S1). Since heat inactivation of cells artificially exposes β1,3-glucan and chitin at the cell wall surface (Gow et al, 2007; Mora-Montes et al, 2011; Estrada-Mata et al, 2015; Navarro-Arias et al, 2016, 2017, 2019; Perez-Garcia et al, 2016; Hernandez-Chavez et al, 2018); we next repeated the experiment but using heat-killed (HK) cells for fluorescent labeling. This cell treatment did not have an impact on the ability of Con A-FITC to bind the cell wall (Figure 3 and Supplementary Figure S1).…”

Section: Resultsmentioning

confidence: 99%

“…Next, we analyzed the organization of the structural polysaccharides chitin and β1,3-glucan within the cell wall, using fluorescence labeling with fluorescein isothiocyanate-wheat germ agglutinin conjugate (WGA-FITC) and an IgG Fc-Dectin-1 chimera, respectively (Graham et al, 2006; Mora-Montes et al, 2011; Marakalala et al, 2013; Estrada-Mata et al, 2015; Navarro-Arias et al, 2016, 2017, 2019; Hernandez-Chavez et al, 2018). Both lectins barely bound to chitin and β1,3-glucan localized in the cell wall of the WT and the re-integrant control strains (Figure 3 and Supplementary Figures S2, S3).…”

Section: Resultsmentioning

confidence: 99%

“…Besides the importance of the immune cell- Candida interaction, mannans are key players in maintaining the cell wall integrity, cellular and colonial morphology, as well as in determining biofilm formation and virulence (Bates et al, 2005, 2006, 2013; Munro et al, 2005; Prill et al, 2005; Mora-Montes et al, 2007, 2010; Hall et al, 2013; West et al, 2013; Estrada-Mata et al, 2015; Navarro-Arias et al, 2016, 2017; Perez-Garcia et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

“…Besides the genetic approach to assess the relevance of mannans in the fungal biology, the chemical removal of O -linked mannans by β-elimination or the enzymatic trimming of N -linked mannans with endoglycosidase H (endo H) have positively impacted in our current knowledge about the versatile functions of mannans in the biology of Candida spp. and other fungal species (Hamada et al, 1981; Hazen and Glee, 1994; Mormeneo et al, 1994; Goins and Cutler, 2000; Spreghini et al, 2003; Navarro-Arias et al, 2016, 2017, 2019; Perez-Garcia et al, 2016; Martinez-Alvarez et al, 2017; Lozoya-Perez et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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Role of Protein Mannosylation in the Candida tropicalis-Host Interaction

et al. 2019

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Mannans are components of the fungal wall attached to proteins via N- or O-linkages. In Candida albicans, Och1 is an α1,6-mannosyltransferase that adds the first mannose unit to the N-linked mannan outer chain; whereas Pmr1 is an ion pump that imports Mn2+ into the Golgi lumen. This cation is the cofactor of Golgi-resident mannosyltransferases, and thus Pmr1 is involved in the synthesis of both N- and O-linked mannans. Since we currently have limited information about the genetic network behind the Candida tropicalis protein mannosylation machinery, we disrupted OCH1 and PMR1 in this organism. The C. tropicalis pmr1Δ and och1Δ mutants showed increased doubling times, aberrant colony and cellular morphology, reduction in the wall mannan content, and increased susceptibility to wall perturbing agents. These changes were accompanied by increased exposure of both β1,3-glucan and chitin at the wall surface of both mutant strains. Our results showed that O-linked mannans are dispensable for cytokine production by human mononuclear cells, but N-linked mannans and β1,3-glucan are key ligands to trigger cytokine production in a co-stimulatory pathway involving dectin-1 and mannose receptor. Moreover, we found that the N-linked mannan core found on the surface of C. tropicalis och1Δ null mutant was capable of inducing cytokine production; and that a mannan-independent pathway for IL-10 production is present in the C. tropicalis-mononuclear cell interaction. Both mutant strains showed virulence attenuation in the Galleria mellonella and the mouse model of systemic candidiasis. Therefore, mannans are relevant for cell wall composition and organization, and for the C. tropicalis-host interaction.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Role of Protein Mannosylation in the Candida tropicalis-Host Interaction

et al. 2019

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CmpX Affects Virulence in Pseudomonas aeruginosa Through the Gac/Rsm Signaling Pathway and by Modulating c-di-GMP Levels

Bhagirath

Somayajula

et al. 2017

J Membrane Biol

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Pseudomonas aeruginosa is an ubiquitous organism which is able to infect and colonize many types of hosts including humans. Colonization of P. aeruginosa in chronic infections leads to the formation of biofilms, which are difficult to eradicate. P. aeruginosa is capable of regulating its virulence factors in response to external environment triggers and its signaling mechanism involves two-component regulatory systems and small molecules such as bis-(3'-5')-cyclic dimeric guanosine monophosphate. PA1611-RetS-GacS/A-RsmA/Y/Z is a key regulatory pathway in P. aeruginosa that controls several virulence factors and biofilm formation. We have previously identified a conserved cytoplasmic membrane protein cmpX (PA1775), as a regulator for PA1611 expression. In this study, we demonstrate that cmpX regulates virulence, and controls biofilm formation in P. aeruginosa as well as provide evidence showing that cmpX affects Gac/Rsm pathway, possibly by modulating intra-cellular c-di-GMP levels. A cmpX knockout showed significantly decreased promoter activity of exoS (PA1362) and increased activity of small RNA, RsmY. As compared to the wild-type PAO1, cmpX mutant had elevated intracellular c-di-GMP level as measured indirectly by cdrA (PA4625) activity, as well as increased expression of wspR (PA3702), a c-di-GMP synthase. The transcription of the major outer membrane porin gene oprF (PA1777), and sigma factor sigX (PA1776) was also significantly decreased in the cmpX mutant. Biolog phenotype microarray experiments further indicated that the cmpX knockout mutant had increased sensitivity to membrane detergents and antibiotics such as lauryl sulfobetaine, tobramycin, and vancomycin. These results point to a significant role of cmpX in P. aeruginosa virulence and colonization.

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