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The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans
Invasive growth of the fungal pathogen Candida albicans into tissues promotes disseminated infections in humans. The plasma membrane is essential for pathogenesis because this important barrier mediates morphogenesis and invasive growth, as well as secretion of virulence factors, cell wall synthesis...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society of Microbiology
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3870249/ https://www.ncbi.nlm.nih.gov/pubmed/24281718 http://dx.doi.org/10.1128/mBio.00723-13 |
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author | Douglas, Lois M. Wang, Hong X. Konopka, James B. |
author_facet | Douglas, Lois M. Wang, Hong X. Konopka, James B. |
author_sort | Douglas, Lois M. |
collection | PubMed |
description | Invasive growth of the fungal pathogen Candida albicans into tissues promotes disseminated infections in humans. The plasma membrane is essential for pathogenesis because this important barrier mediates morphogenesis and invasive growth, as well as secretion of virulence factors, cell wall synthesis, nutrient import, and other processes. Previous studies showed that the Sur7 tetraspan protein that localizes to MCC (membrane compartment occupied by Can1)/eisosome subdomains of the plasma membrane regulates a broad range of key functions, including cell wall synthesis, morphogenesis, and resistance to copper. Therefore, a distinct tetraspan protein found in MCC/eisosomes, Nce102, was investigated. Nce102 belongs to the MARVEL domain protein family, which is implicated in regulating membrane structure and function. Deletion of NCE102 did not cause the broad defects seen in sur7Δ cells. Instead, the nce102Δ mutant displayed a unique phenotype in that it was defective in forming hyphae and invading low concentrations of agar but could invade well in higher agar concentrations. This phenotype was likely due to a defect in actin organization that was observed by phalloidin staining. In support of this, the invasive growth defect of a bni1Δ mutant that mislocalizes actin due to lack of the Bni1 formin was also reversed at high agar concentrations. This suggests that a denser matrix provides a signal that compensates for the actin defects. The nce102Δ mutant displayed decreased virulence and formed abnormal hyphae in mice. These studies identify novel ways that Nce102 and the physical environment surrounding C. albicans regulate morphogenesis and pathogenesis. |
format | Online Article Text |
id | pubmed-3870249 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | American Society of Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-38702492013-12-26 The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans Douglas, Lois M. Wang, Hong X. Konopka, James B. mBio Research Article Invasive growth of the fungal pathogen Candida albicans into tissues promotes disseminated infections in humans. The plasma membrane is essential for pathogenesis because this important barrier mediates morphogenesis and invasive growth, as well as secretion of virulence factors, cell wall synthesis, nutrient import, and other processes. Previous studies showed that the Sur7 tetraspan protein that localizes to MCC (membrane compartment occupied by Can1)/eisosome subdomains of the plasma membrane regulates a broad range of key functions, including cell wall synthesis, morphogenesis, and resistance to copper. Therefore, a distinct tetraspan protein found in MCC/eisosomes, Nce102, was investigated. Nce102 belongs to the MARVEL domain protein family, which is implicated in regulating membrane structure and function. Deletion of NCE102 did not cause the broad defects seen in sur7Δ cells. Instead, the nce102Δ mutant displayed a unique phenotype in that it was defective in forming hyphae and invading low concentrations of agar but could invade well in higher agar concentrations. This phenotype was likely due to a defect in actin organization that was observed by phalloidin staining. In support of this, the invasive growth defect of a bni1Δ mutant that mislocalizes actin due to lack of the Bni1 formin was also reversed at high agar concentrations. This suggests that a denser matrix provides a signal that compensates for the actin defects. The nce102Δ mutant displayed decreased virulence and formed abnormal hyphae in mice. These studies identify novel ways that Nce102 and the physical environment surrounding C. albicans regulate morphogenesis and pathogenesis. American Society of Microbiology 2013-11-26 /pmc/articles/PMC3870249/ /pubmed/24281718 http://dx.doi.org/10.1128/mBio.00723-13 Text en Copyright © 2013 Douglas et al. http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license (http://creativecommons.org/licenses/by-nc-sa/3.0/) , which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Douglas, Lois M. Wang, Hong X. Konopka, James B. The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans |
title | The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans |
title_full | The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans |
title_fullStr | The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans |
title_full_unstemmed | The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans |
title_short | The MARVEL Domain Protein Nce102 Regulates Actin Organization and Invasive Growth of Candida albicans |
title_sort | marvel domain protein nce102 regulates actin organization and invasive growth of candida albicans |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3870249/ https://www.ncbi.nlm.nih.gov/pubmed/24281718 http://dx.doi.org/10.1128/mBio.00723-13 |
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