Cellular Localization of Carbonic Anhydrase Nce103p in Candida albicans and Candida parapsilosis
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00521503" target="_blank" >RIV/61388963:_____/20:00521503 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00216208:11310/20:10420135
Výsledek na webu
<a href="https://www.mdpi.com/1422-0067/21/3/850" target="_blank" >https://www.mdpi.com/1422-0067/21/3/850</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms21030850" target="_blank" >10.3390/ijms21030850</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Cellular Localization of Carbonic Anhydrase Nce103p in Candida albicans and Candida parapsilosis
Popis výsledku v původním jazyce
Pathogenic yeasts Candida albicans and Candida parapsilosis possess a ß-type carbonic anhydrase Nce103p, which is involved in CO2 hydration and signaling. C. albicans lacking Nce103p cannot survive in low CO2 concentrations, e.g., in atmospheric growth conditions. Candida carbonic anhydrases are orthologous to the Saccharomyces cerevisiae enzyme, which had originally been detected as a substrate of a non-classical export pathway. However, experimental evidence on localization of C. albicans and C. parapsilosis carbonic anhydrases has not been reported to date. Immunogold labeling and electron microscopy used in the present study showed that carbonic anhydrases are localized in the cell wall and plasmatic membrane of both Candida species. This localization was confirmed by Western blot and mass spectrometry analyses of isolated cell wall and plasma membrane fractions. Further analysis of C. albicans and C. parapsilosis subcellular fractions revealed presence of carbonic anhydrases also in the cytosolic and mitochondrial fractions of Candida cells cultivated in shaken liquid cultures, under the atmospheric conditions.
Název v anglickém jazyce
Cellular Localization of Carbonic Anhydrase Nce103p in Candida albicans and Candida parapsilosis
Popis výsledku anglicky
Pathogenic yeasts Candida albicans and Candida parapsilosis possess a ß-type carbonic anhydrase Nce103p, which is involved in CO2 hydration and signaling. C. albicans lacking Nce103p cannot survive in low CO2 concentrations, e.g., in atmospheric growth conditions. Candida carbonic anhydrases are orthologous to the Saccharomyces cerevisiae enzyme, which had originally been detected as a substrate of a non-classical export pathway. However, experimental evidence on localization of C. albicans and C. parapsilosis carbonic anhydrases has not been reported to date. Immunogold labeling and electron microscopy used in the present study showed that carbonic anhydrases are localized in the cell wall and plasmatic membrane of both Candida species. This localization was confirmed by Western blot and mass spectrometry analyses of isolated cell wall and plasma membrane fractions. Further analysis of C. albicans and C. parapsilosis subcellular fractions revealed presence of carbonic anhydrases also in the cytosolic and mitochondrial fractions of Candida cells cultivated in shaken liquid cultures, under the atmospheric conditions.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10606 - Microbiology
Návaznosti výsledku
Projekt
<a href="/cs/project/GA17-08343S" target="_blank" >GA17-08343S: Studium struktur karbonických anhydráz z pathogenních druhů Candid pro vývoj potenciálních antimykotik</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2020
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
International Journal of Molecular Sciences
ISSN
1422-0067
e-ISSN
—
Svazek periodika
21
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
8
Strana od-do
850
Kód UT WoS článku
000522551603004
EID výsledku v databázi Scopus
2-s2.0-85078852515