A Human-Curated Annotation of the Candida albicans Genome
Open accessAbstract
Recent sequencing and assembly of the genome for the fungal pathogen Candida albicans used simple automated procedures for the identification of putative genes. We have reviewed the entire assembly, both by hand and with additional bioinformatic resources, to accurately map and describe 6,354 genes and to identify 246 genes whose original database entries contained sequencing errors (or possibly mutations) that affect their reading frame. Comparison with other fungal genomes permitted the identification of numerous fungus-specific genes that might be targeted for antifungal therapy. We also observed that, compared to other fungi, the protein-coding sequences in the C. albicans genome are especially rich in short sequence repeats. Finally, our improved annotation permitted a detailed analysis of several multigene families, and comparative genomic studies showed that C. albicans has a far greater catabolic range, encoding respiratory Complex 1, several novel oxidoreductases and ketone body degrading enzymes, malonyl-CoA and enoyl-CoA carriers, several novel amino acid degrading enzymes, a variety of secreted catabolic lipases and proteases, and numerous transporters to assimilate the resulting nutrients. The results of these efforts will ensure that the Candida research community has uniform and comprehensive genomic information for medical research as well as for future diagnostic and therapeutic applications.
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The ALS gene family encodes eight GPI-linked cell surface proteins that mediate binding to diverse host substrates.
“This gene family encodes eight GPI-linked cell surface proteins that mediate binding to diverse host substrates [20][21][22][23][24][25].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [21]
The Results/Discussion section, under “Multigene Families” (page unavailable), says the ALS family has eight genes encoding cell-surface glycoproteins involved in host–pathogen interactions; it also reports adhesive capability for an Als3p variant. Our copy does not establish that all eight proteins are GPI-linked or that they bind diverse host substrates. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe Als family of proteins contains six members in addition to Als1 and Als3.
“The Als family of proteins contains six members in addition to Als1 and Als3 [20][21][22][23][24][25].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [21]
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Self-citationA High-Affinity Iron Permease Essential for <i>Candida albicans</i> Virulence
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“affinity iron transporters [40], and ferric reductases [41].”
BackgroundFunctional and Structural Diversity in the Als Protein Family of Candida albicans
Sheppard, D. C., Yeaman, M. R., Welch, W. H., Phan, Q. T., Fu, Y., Ibrahim, A. S., Filler, S. G., Zhang, M., Waring, A. J., & Edwards, J. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401929200 · Cited by 300 · cited 1× · see citing works
“The ALS genes encode large cell-surface glycoproteins that function in host–pathogen interactions [50,51].”
BackgroundIdentification and Characterization of a Sphingolipid Δ4-Desaturase Family
Ternes, P., Franke, S., Zähringer, U., Sperling, P., & Heinz, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202947200 · Cited by 293 · see citing works
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“albicans genome project [38,52–54]) and were aided greatly by information that emerged as the genome sequencing effort progressed [55–57].”
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Population genomics of drug resistance in <i>Candida albicans</i>
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Self-citationCharacterization of the gene family encoding alternative oxidase from Candida albicans
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“]. An additional difference is the presence of two alternative oxidases that may be involved in protection against oxidative stress [”
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<i>Candida albicans</i> Cell Wall Proteins
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- Authors
- Braun, B. R., van het Hoog, M., d'Enfert, C., Martchenko, M., Dungan, J., Kuo, A., Inglis, D. O., Uhl, M. A., Hogues, H., Berriman, M., Lorenz, M., Levitin, A., Oberholzer, U., Bachewich, C., Harcus, D., Marcil, A., Dignard, D., Iouk, T., Zito, R., Frangeul, L., Tekaia, F., Rutherford, K., Wang, E., Munro, C. A., Bates, S., Gow, N. A., Hoyer, L. L., Köhler, G., Morschhäuser, J., Newport, G., Znaidi, S., Raymond, M., Turcotte, B., Sherlock, G., Costanzo, M., Ihmels, J., Berman, J., Sanglard, D., Agabian, N., Mitchell, A. P., Johnson, A. D., Whiteway, M., & Nantel, A.
- Affiliations
- University of California, San Francisco (US)
- Biotechnology Research Institute (CA)
- Wellcome Sanger Institute (GB)
- The University of Texas Health Science Center at Houston (US)
- Institut Pasteur (FR)
- University of Aberdeen (GB)
- University of Illinois Urbana-Champaign (US)
- University of Würzburg (DE)
- Montreal Clinical Research Institute (CA)
- Royal Victoria Hospital (CA)
- Stanford Medicine (US)
- Weizmann Institute of Science (IL)
- University of Minnesota (US)
- Centre Hospitalier Universitaire Vaudois (CH)
- New York University (US)
- Corresponding author
- Nantel, André
- ORCID
- Kuo, Alan
- Inglis, Diane O
- Uhl, M. Andrew
- Berriman, Matthew
- Levitin, Anastasia
- Marcil, Anne
- Frangeul, Lionel
- Tekaia, Fredj
- Rutherford, Kim
- Wang, Edwin
- Munro, Carol A
- Gow, Neil A
- Hoyer, Lois L
- Köhler, Gerwald
- Morschhäuser, Joachim
- Znaidi, Sadri
- Turcotte, Bernard
- Sherlock, Gavin
- Costanzo, Maria
- Berman, Judith
- Sanglard, Dominique
- Mitchell, Aaron P
- Johnson, Alexander D
- Whiteway, Malcolm
- Nantel, André
- Venue
- PLoS Genetics
- Publisher
- Public Library of Science (PLoS)
- Published
- 2005-06-17
- Volume
- 1
- Issue
- 1
- Pages
- e1
- ISSN
- 1553-7390 (ISSN-L)
- 1553-7404
- PMC
- PMC1183520
- OpenAlex
- W2060322845
- Cited by
- 342
- References
- 12
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 13 · 2023: 7 · 2022: 6 · 2021: 6 · 2020: 12 · 2019: 11 · 2018: 15 · 2017: 13 · 2016: 15 · 2015: 15 · 2014: 21 · 2013: 17 · 2012: 9
- FWCI
- 12.85
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- PLoS Genetics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Spectrum Research Repository (Concordia University) (acceptedVersion)
- HAL (submittedVersion, cc-by)
- IRIS (submittedVersion)
- Aberdeen University Research Archive (Aberdeen University) (submittedVersion)
- NPARC (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Figshare (submittedVersion, cc-by)
- SERVAL (Université de Lausanne) (submittedVersion, other-oa)
- Funders
- Burroughs Wellcome Fund
- Massachusetts Institute of Technology
- North Carolina State University
- Wellcome Trust
- Broad Institute
- Incyte
- National Institutes of Health
- University of California, San Francisco
- Canadian Institutes of Health Research (MOP42516)
- National Research Council Canada
- National Institute of Allergy and Infectious Diseases (R01AI049187)
- National Institute of Dental and Craniofacial Research (P01DE007946)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Keywords
- Candida albicans, genome annotation, gene identification, fungal pathogens, antifungal drug targets, short sequence repeats, gene family, comparative genomics, catabolic genes, oxidative enzymes, amino acid catabolism, lipase, proteolytic enzymes, transporters, sequencing errors
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