Genetic Basis for Dimorphism and Pathogenicity in Candida Albicans

Fonzi, William A.; Saporito-Irwin, Susan M.; Chen, Jiangye; Sypherd, Paul S.

doi:10.1007/978-1-4615-2834-0_4

Cited by 52 publications

(79 citation statements)

References 34 publications

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“…To rule out the possible existence of other TER genes and to characterize further the function of TER1, we generated homozygous deletion strains by replacing both copies of TER1 with HisG using the URA-Blaster cassette (30). To facilitate comparison with other telomerase deletion mutants, we generated the ter1-⌬⌬ strains in the BWP17 strain background (13,21).…”

Section: Deletion Of the Ter1 Gene Results In Complete Loss Of Telomementioning

confidence: 99%

“…The C. albicans strains CA I4 (ura3⌬::imm434/ura3⌬::imm434) and BWP17 (ura3⌬::-imm434/ura3⌬:: imm434 his1::hisG/his1::hisG arg4::hisG/ arg4::hisG) were used as the parental strains (30,46). The derivations of mutant strains are described below.…”

Section: Methodsmentioning

confidence: 99%

“…The EcoRI site of the insert was derived from C. albicans sequences, and the SacI site was derived from polylinker bordering the phage insert. The C. albicans URA3 gene, isolated as a 1566 HpaII fragment from pMB7 (30), was introduced into pSR3 at the ClaI site to create plasmid pSR3-U. Two base substitutions were then made in the putative template region of pSR3-U to create a BglII site, resulting in plasmid pSR3-U-B4D (47).…”

Section: Construction Of Mutant Candidamentioning

confidence: 99%

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Telomerase core components protect Candida telomeres from aberrant overhang accumulation

Hsu

McEachern

Dandjinou

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Telomerase is a cellular reverse transcriptase that extends one strand (the G-strand) of the telomere terminal repeats. Aside from this role in telomere length maintenance, telomerase has been proposed to serve a protective function at chromosome ends, although this is not well understood mechanistically. Earlier analysis suggests that, in the pathogenic yeast Candida albicans, the catalytic reverse transcriptase subunit of telomerase (TERT/EST2) can protect telomeres against nucleolytic degradation. In this report we demonstrate that the RNA component (TER1) has a similar function; in addition to complete loss of telomerase activity and progressive telomere attrition, the ter1-⌬⌬ strains manifested a dramatic increase in the amount of G-strand overhangs, consistent with aberrant degradation of the complementary C-strand. We also demonstrate that a catalytically incompetent EST2 protein can suppress such overhang accumulation in the est2-⌬⌬ mutant to the same extent as the wild-type protein. Altogether, our data support the notion that the Candida telomerase core components mediate a protective function through a mechanism that is independent of its catalytic activity.G-strand ͉ telomerase RNA ͉ telomerase reverse transcriptase

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Section: Deletion Of the Ter1 Gene Results In Complete Loss Of Telomementioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Construction Of Mutant Candidamentioning

confidence: 99%

See 1 more Smart Citation

Telomerase core components protect Candida telomeres from aberrant overhang accumulation

Hsu

McEachern

Dandjinou

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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“…SYTOX Green was obtained from Molecular Probes (Eugene, OR). Yeast strains used in this study are S. cerevisiae strain BY4741 (Invitrogen), P. pastoris strain GS115 (Invitrogen) and the corresponding P. pastoris gcs-deletion strain (13), C. albicans strain SC5314 CAI4 (23) and the corresponding C. albicans gcs-deletion strain (13).…”

Section: Methodsmentioning

confidence: 99%

Defensins from Insects and Plants Interact with Fungal Glucosylceramides

Thevissen¹,

Warnecke

François³

et al. 2004

Journal of Biological Chemistry

326

310

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Growth of the yeast species Candida albicans andPichia pastoris is inhibited by RsAFP2, a plant defensin isolated from radish seed (Raphanus sativus), at micromolar concentrations. In contrast, gcs-deletion mutants of both yeast species are resistant toward RsAFP2. GCS genes encode UDP-glucose:ceramide glucosyltransferases, which catalyze the final step in the biosynthesis of the membrane lipid glucosylceramide. In an enzymelinked immunosorbent assay-based binding assay, RsAFP2 was found to interact with glucosylceramides isolated from P. pastoris but not with soybean nor human glucosylceramides. Furthermore, the P. pastoris parental strain is sensitive toward RsAFP2-induced membrane permeabilization, whereas the corresponding gcs-deletion mutant is highly resistant to RsAFP2-mediated membrane permeabilization. A model for the mode of action of RsAFP2 is presented in which all of these findings are linked. Similarly to RsAFP2, heliomicin, a defensin-like peptide from the insect Heliothis virescens, is active on C. albicans and P. pastoris parental strains but displays no activity on the gcs-deletion mutants of both yeast species. Furthermore, heliomicin interacts with glucosylceramides isolated from P. pastoris and soybean but not with human glucosylceramides. These data indicate that structurally homologous antifungal peptides present in species from different eukaryotic kingdoms interact with the same target in the fungal plasma membrane, namely glucosylceramides, and as such support the hypothesis that defensins from plants and insects have evolved from a single precursor.

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“…One of several identified strains, CAP1-31, of the genotype pmt1⌬::hisG/PMT1 was used for a second round of gene disruption using the original URA blaster fragment. Several transformants had the genotype pmt1⌬::hisG/pmt1⌬::hisG-URA3-hisG, and strain CAP1-312 was chosen to identify strains by 5-fluoroorotic acid resistance (21). Strain CAP1-3121 is a representative of mutant strains of the genotype pmt1⌬::hisG/pmt1⌬::hisG.…”

Section: Methodsmentioning

confidence: 99%

Multiple Functions of Pmt1p-mediated ProteinO-Mannosylation in the Fungal Pathogen Candida albicans

Timpel¹,

Strahl‐Bolsinger²,

Ziegelbauer³

et al. 1998

Journal of Biological Chemistry

149

186

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Protein mannosylation by Pmt proteins initiates Oglycosylation in fungi. We have identified the PMT1 gene and analyzed the function of Pmt1p in the fungal human pathogen Candida albicans. Mutants defective in PMT1 alleles lacked Pmt in vitro enzymatic activity, showed reduced growth rates, and tended to form cellular aggregates. In addition, multiple specific deficiencies not known in Saccharomyces cerevisiae (including defective hyphal morphogenesis; supersensitivity to the antifungal agents hygromycin B, G418, clotrimazole, and calcofluor white; and reduced adherence to Caco-2 epithelial cells) were observed in pmt1 mutants. PMT1 deficiency also led to faster electrophoretic mobility of the Als1p cell wall protein and to elevated extracellular activities of chitinase. Homozygous pmt1 mutants were avirulent in a mouse model of systemic infection, while heterozygous PMT1/pmt1 strains showed reduced virulence. The results indicate that protein O-mannosylation by Pmt proteins occurs in different fungal species, where PMT1 deficiency can lead to defects in multiple cellular functions.

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Genetic Basis for Dimorphism and Pathogenicity in Candida Albicans

Cited by 52 publications

References 34 publications

Telomerase core components protect Candida telomeres from aberrant overhang accumulation

Telomerase core components protect Candida telomeres from aberrant overhang accumulation

Defensins from Insects and Plants Interact with Fungal Glucosylceramides

Multiple Functions of Pmt1p-mediated ProteinO-Mannosylation in the Fungal Pathogen Candida albicans

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