An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans
The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids...
Ausführliche Beschreibung
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| Autor*in: |
Martínez, Paula [verfasserIn] Ljungdahl, Per O. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Science Ltd ; 2004 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2004 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Molecular microbiology - Oxford [u.a.] : Wiley-Blackwell, 1987, 51(2004), 2, Seite 0 |
| Übergeordnetes Werk: |
volume:51 ; year:2004 ; number:2 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1046/j.1365-2958.2003.03845.x |
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| 520 | |a The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. | ||
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10.1046/j.1365-2958.2003.03845.x doi (DE-627)NLEJ243548699 DE-627 ger DE-627 rakwb Martínez, Paula verfasserin aut An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans Oxford, UK Blackwell Science Ltd 2004 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. 2004 Blackwell Publishing Journal Backfiles 1879-2005 |2004|||||||||| Ljungdahl, Per O. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 51(2004), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:51 year:2004 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2003.03845.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 2004 2 0 |
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10.1046/j.1365-2958.2003.03845.x doi (DE-627)NLEJ243548699 DE-627 ger DE-627 rakwb Martínez, Paula verfasserin aut An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans Oxford, UK Blackwell Science Ltd 2004 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. 2004 Blackwell Publishing Journal Backfiles 1879-2005 |2004|||||||||| Ljungdahl, Per O. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 51(2004), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:51 year:2004 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2003.03845.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 2004 2 0 |
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10.1046/j.1365-2958.2003.03845.x doi (DE-627)NLEJ243548699 DE-627 ger DE-627 rakwb Martínez, Paula verfasserin aut An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans Oxford, UK Blackwell Science Ltd 2004 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. 2004 Blackwell Publishing Journal Backfiles 1879-2005 |2004|||||||||| Ljungdahl, Per O. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 51(2004), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:51 year:2004 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2003.03845.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 2004 2 0 |
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10.1046/j.1365-2958.2003.03845.x doi (DE-627)NLEJ243548699 DE-627 ger DE-627 rakwb Martínez, Paula verfasserin aut An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans Oxford, UK Blackwell Science Ltd 2004 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. 2004 Blackwell Publishing Journal Backfiles 1879-2005 |2004|||||||||| Ljungdahl, Per O. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 51(2004), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:51 year:2004 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2003.03845.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 2004 2 0 |
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10.1046/j.1365-2958.2003.03845.x doi (DE-627)NLEJ243548699 DE-627 ger DE-627 rakwb Martínez, Paula verfasserin aut An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans Oxford, UK Blackwell Science Ltd 2004 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. 2004 Blackwell Publishing Journal Backfiles 1879-2005 |2004|||||||||| Ljungdahl, Per O. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 51(2004), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:51 year:2004 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2003.03845.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 51 2004 2 0 |
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An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans |
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The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. |
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The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. |
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The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. These results strongly suggest that C. albicans cells use amino acids, presumably as nitrogen sources, during growth in mammalian hosts. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243548699</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506095619.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2004 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1365-2958.2003.03845.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243548699</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Martínez, Paula</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">An ER packaging chaperone determines the amino acid uptake capacity and virulence of Candida albicans</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Science Ltd</subfield><subfield code="c">2004</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The Candida albicans CSH3 gene encodes a functional and structural homologue of Shr3p, a yeast protein that is specifically required for proper uptake and sensing of extracellular amino acids in Saccharomyces cerevisiae. A Candida csh3Δ/csh3Δ null mutant has a reduced capacity to take up amino acids, and is unable to switch morphologies on solid and in liquid media in response to inducing amino acids. CSH3/csh3Δ heterozygous strains display normal amino acid induced morphological switching. However, although heterozygous cells apparently sense and properly react to amino acid induced signals they cannot take up amino acids at wild-type rates. Strikingly, both CSH3/csh3Δ heterozygous and csh3Δ/csh3Δ homozygous strains are unable to efficiently mount virulent infections in a mouse model. The haploinsufficiency phenotypes indicate that both CSH3 alleles contribute to maintain high-capacity amino acid uptake in wild-type strains. 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