TY  - JOUR
A1  - Palige, Katja
A1  - Linde, Jörg
A1  - Martin, Ronny
A1  - Böttcher, Bettina
A1  - Citiulo, Francesco
A1  - Sullivan, Derek J.
A1  - Weber, Johann
A1  - Staib, Claudia
A1  - Rupp, Steffen
A1  - Hube, Bernhard
A1  - Morschhäuser, Joachim
A1  - Staib, Peter
T1  - Global Transcriptome Sequencing Identifies Chlamydospore Specific Markers in Candida albicans and Candida dubliniensis
JF  - PLoS ONE
N2  - Candida albicans and Candida dubliniensis are pathogenic fungi that are highly related but differ in virulence and in some phenotypic traits. During in vitro growth on certain nutrient-poor media, C. albicans and C. dubliniensis are the only yeast species which are able to produce chlamydospores, large thick-walled cells of unknown function. Interestingly, only C. dubliniensis forms pseudohyphae with abundant chlamydospores when grown on Staib medium, while C. albicans grows exclusively as a budding yeast. In order to further our understanding of chlamydospore development and assembly, we compared the global transcriptional profile of both species during growth in liquid Staib medium by RNA sequencing. We also included a C. albicans mutant in our study which lacks the morphogenetic transcriptional repressor Nrg1. This strain, which is characterized by its constitutive pseudohyphal growth, specifically produces masses of chlamydospores in Staib medium, similar to C. dubliniensis. This comparative approach identified a set of putatively chlamydospore-related genes. Two of the homologous C. albicans and C. dubliniensis genes (CSP1 and CSP2) which were most strongly upregulated during chlamydospore development were analysed in more detail. By use of the green fluorescent protein as a reporter, the encoded putative cell wall related proteins were found to exclusively localize to C. albicans and C. dubliniensis chlamydospores. Our findings uncover the first chlamydospore specific markers in Candida species and provide novel insights in the complex morphogenetic development of these important fungal pathogens.
KW  - NRG1
KW  - staib agar
KW  - gene
KW  - morphogenesis
KW  - expression
KW  - regulator
KW  - virulence
KW  - growth
KW  - UME6
KW  - epidemiology
Y1  - 2013
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-131007
VL  - 8
IS  - 4
ER  - 
TY  - JOUR
A1  - Makgotlho, Phuti E.
A1  - Marincola, Gabriella
A1  - Schäfer, Daniel
A1  - Liu, Quian
A1  - Bae, Taeok
A1  - Geiger, Tobias
A1  - Wasserman, Elizabeth
A1  - Wolz, Christine
A1  - Ziebuhr, Wilma
A1  - Sinha, Bhanu
T1  - SDS Interferes with SaeS Signaling of Staphylococcus aureus Independently of SaePQ
JF  - PLOS ONE
N2  - The Staphylococcus aureus regulatory saePQRS system controls the expression of numerous virulence factors, including extracellular adherence protein (Eap), which amongst others facilitates invasion of host cells. The saePQRS operon codes for 4 proteins: the histidine kinase SaeS, the response regulator SaeR, the lipoprotein SaeP and the transmembrane protein SaeQ. S. aureus strain Newman has a single amino acid substitution in the transmembrane domain of SaeS (L18P) which results in constitutive kinase activity. SDS was shown to be one of the signals interfering with SaeS activity leading to inhibition of the sae target gene eap in strains with SaeS(L) but causing activation in strains containing SaeS(P). Here, we analyzed the possible involvement of the SaeP protein and saePQ region in SDS-mediated sae/eap expression. We found that SaePQ is not needed for SDS-mediated SaeS signaling. Furthermore, we could show that SaeS activity is closely linked to the expression of Eap and the capacity to invade host cells in a number of clinical isolates. This suggests that SaeS activity might be directly modulated by structurally non-complex environmental signals, as SDS, which possibly altering its kinase/phosphatase activity.
KW  - host-cell invasion
KW  - 2-component system
KW  - strain Newman
KW  - allelic replacement
KW  - genome sequence
KW  - locus
KW  - gene
KW  - activation
KW  - expression
KW  - infection
Y1  - 2013
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-128469
SN  - 1932-6203
VL  - 8
IS  - 8
ER  -