Expression, cloning, and characterization of a Candida albicans gene, ALA1, that confers adherence properties upon Saccharomyces cerevisiae for extracellular matrix proteins
Open accessAbstract
Adherence of Candida albicans to host tissues is a necessary step for maintenance of its commensal status and is likely a necessary step in the pathogenesis of candidiasis. The extracellular matrix (ECM) proteins are some of the host tissue and plasma proteins to which C. albicans adheres through adhesins located on the fungal cell surface. To isolate genes encoding ECM adhesins, an assay was developed based on the ability of yeast cells to adhere to magnetic beads coated with the ECM protein fibronectin, type IV collagen, or laminin. A C. albicans genomic library was constructed by cloning XbaI-partially-digested and size-selected fragments into pAUR112, an Escherichia coli-yeast low-copy-number shuttle vector. The C. albicans library was transformed into Saccharomyces cerevisiae YPH 499, and clones capable of adherence were selected by using ECM protein-coated magnetic beads. A plasmid containing an approximately 8-kb insert was isolated from 29 adherent clones. These clones exhibited adherence to all ECM protein-coated magnetic beads and to human buccal epithelial cells. The ALA1 gene (for agglutinin-like adhesin) was localized by subcloning it into a 5-kb XbaI fragment which retained the adherence phenotype in both orientations. The complete DNA sequence of the 5-kb insert was determined, and an open reading frame (ORF) encoding 1,419 amino acid residues was identified. Deletions from the 5' and 3' ends extending into the DNA sequence encoding the 1,419-amino-acid ORF product inactivated the adherence phenotype, suggesting that it is the coding region of the ALA1 gene. A database search identified ALA1 to be similar to the C. albicans ALS1 (for agglutinin-like sequence 1) protein and the S. cerevisiae agglutinin protein (AG alpha1), although the homology at the primary amino acid sequence level is limited to the first half of each of these proteins. ALA1 contains a central domain of six tandem repeats of 36 amino acids. We discuss the significance of various predicted ALA1 structural motifs and their relationships to function in the adherence process.
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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 [22]
The paper reports that ALA1 is homologous to ALS1 and confers adherence to several extracellular-matrix proteins and human buccal epithelial cells (opening section). The Discussion describes a predicted GPI-anchor-like region in ALA1, but does not establish that the ALS family comprises eight GPI-linked proteins or that the family as a whole mediates this binding. Page numbers are not available in our copy. (LLM, conf=0.87)
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 [22]
The Results describe homology between ALA1 and ALS1 and say that ALA1 has six tandem repeats; those repeats are not six additional Als proteins. Searches for Als3 and other Als family members found no passage establishing the claimed family size. The available section labels do not provide page numbers. (LLM, conf=0.75)
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“These mannoproteins comprise a family that is termed fungal adhesins, which include Ala1p, Als1p and Hwp1p in C. albicans , and Epa1p in Candida glabrata (Hoyer et al ., 1995; Gaur and Klotz, 1997; Cormack et al ., 1999; Staab et al ., 1999).”
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“The ALS (agglutinin-like sequence) gene family of Candida albicans encodes eight large cell-surface glycoproteins, some of which function in adhesion to host cells ( Gaur & Klotz, 1997; Hoyer, 2001; Fu et al., 2002; Zhao et al., 2004).”
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“The eight ALS genes (ALS1 to ALS7 and ALS9) encode large, cell surface glycoproteins, some of which promote adhesion to host surfaces (6, 7, 10, 35, 36).”
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Strengthening relationships: amyloids create adhesion nanodomains in yeasts
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“Each TR domain is a 36 residue βsheet fold with large surface-exposed regions of aliphatic and aromatic amino acid side chains [24, 38-40].”
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“Accession numbers for other sequences discussed here include L25902 (ALS1 [26]), U87856 (ALS3 [25]), and AF025429 (ALA1/ALS5 [18]).”
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Unfolding individual Als5p adhesion proteins on live cells
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“The protocol that we used for bead adherence assays is similar to that described elsewhere.(10,12) Briefly, Als5p-expressing cells were mixed with fibronectin-coated magnetic beads at a cell-to-bead ratio of 100:1 in Tris-EDTA buffer, vortexed, and incubated at room temperature with gentle shaking for 30 to 45 min.”
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“Many of these proteins are involved in mediating the adhesion of C. albicans cells to host materials and/or inert surfaces (Fu et al., 2002; Gaur & Klotz, 1997; Phan et al., 2007; Staab et al., 1999; Zhao et al., 2005, 2007).”
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“For example, Gaur and Klotz used microscopic magnetic beads coated with extracellular matrix proteins to isolate a C. albicans adhesin gene, ALS5, by expression cloning in S. cerevisiae ( 13 ).”
Flocculation protein structure and cell–cell adhesion mechanism in Saccharomyces cerevisiae
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“2003), inert surfaces such as agar and plastic (Gaur and Klotz 1997; Lo and Dranginis 1998; Reynolds and Fink 2001) and mammalian tissues (Cormack et al.”
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“Data were processed with NMRPipe (6) and analyzed with NMRview (7).”
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“cerevisiae transformants for ECM-coated magnetic beads (9), and Fu et al.”
BackgroundResultInfluentialSelf-citationDegenerate Peptide Recognition by Candida albicans Adhesins Als5p and Als1p
Klotz, S., Gaur, N., Lake, D., Chan, V., Rauceo, J. M., & Lipke, P. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2029-2034.2004 · Cited by 89 · see citing works
“this adherence assay; all are equivalent (6), and the adherence of the fungal cells”
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“We and others have determined that Als proteins function as adhesins to biologically relevant substrates (13, 15 , 32, 54).”
BackgroundWhat We Do Not Know about Fungal Cell Adhesion Molecules
Lipke, P. (2018) · Journal of Fungi · doi:10.3390/jof4020059 · Cited by 81 · see citing works
“cerevisiae has been successfully used for over a decade [22,73,105].”
BackgroundMethodCalera, J. A., & Calderone, R. (1999) · Microbiology · doi:10.1099/13500872-145-6-1431 · Cited by 81 · see citing works
<i>Candida</i> Species: New Insights into Biofilm Formation
Cuéllar-Cruz, M., López-Romero, E., Villagómez-Castro, J. C., & Ruiz-Baca, E. (2012) · Future Microbiology · doi:10.2217/fmb.12.48 · Cited by 80 · see citing works
“In order to adhere, the Als proteins interact with amino acid residues (Ser/ Thr) of different host ligands such as laminin, fibronectin and collagen [101].”
BackgroundProteomic analysis of Candida albicans yeast and hyphal cell wall and associated proteins
Ebanks, R. O., Chisholm, K., McKinnon, S., Whiteway, M., & Pinto, D. M. (2006) · Proteomics · doi:10.1002/pmic.200500100 · Cited by 80 · see citing works
Contribution of Candida albicans ALS1 to the Pathogenesis of Experimental Oropharyngeal Candidiasis
Kamai, Y., Kubota, M., Kamai, Y., Hosokawa, T., Fukuoka, T., & Filler, S. (2002) · Infection and Immunity · doi:10.1128/iai.70.9.5256-5258.2002 · Cited by 80 · see citing works
“Several adherence genes have been characterized (6, 7, 12).”
BackgroundFungal invasion of epithelial cells
Yang, W., Yan, L., Wu, C., Zhao, X., & Tang, J. (2014) · Microbiological Research · doi:10.1016/j.micres.2014.02.013 · Cited by 79 · see citing works
Zhang, N.-X., Harrex, A., Holland, B., Fenton, L., Cannon, R., & Schmid, J. (2003) · Genome Research · doi:10.1101/gr.1024903 · Cited by 79 · see citing works
“…between GPG cluster strains and other strains to identify physiological and genetic traits which are associated with their increased pathogenicity, as a means to identify pathogenicity factors relevant to interactions of C. albicanswith the human host (Schmid et al. 1995; Giblin et al. 2001).”
BackgroundMethodAllelic variation in the contiguous loci encoding Candida albicans ALS5, ALS1 and ALS9.
Zhao, X.-M., Pujol, C., Soll, D., & Hoyer, L. (2003) · Microbiology · doi:10.1099/mic.0.26495-0 · Cited by 78 · see citing works
“Ironically, the coding sequence immediately downstream of ALS9 was ALA1 .I n this case, ALA1 was not a synonym for ALS5 ( Gaur & Klotz, 1997 ), but encoded alanyl-tRNA synthetase.”
BackgroundThe ALS5 gene of Candida albicans and analysis of the Als5p N‐terminal domain
Hoyer, L., & Hecht, J. E. (2001) · Yeast · doi:10.1002/1097-0061(200101)18:1 · Cited by 72 · see citing works
Candida albicans: adherence, signaling and virulence.
Calderone, R., Suzuki, S., Cannon, R. D., Cho, T., Boyd, D., Calera, J. A., Chibana, H., Herman, D., Holmes, A. R., Jeng, H., et al. (2000) · Medical Mycology · doi:10.1080/mmy.38.s1.125.137 · Cited by 72 · see citing works
Fernández-Álvarez, A., Elías-Villalobos, A., & Ibeas, J. (2009) · The Plant Cell Online · doi:10.1105/tpc.109.065839 · Cited by 71 · see citing works
“Cell wall glycoproteins have been identified as fungal adhesives and have been implicated in host cell adhesion in many organisms (Gaur and Klotz, 1997; Buck and Andrews, 1999; Frieman et al., 2002; Sheppard et al., 2004).”
BackgroundInteraction of pathogenic fungi with host cells: Molecular and cellular approaches.
Mendes-Giannini, M., Soares, C., da Silva, J. L. M., & Andreotti, P. F. (2005) · FEMS Immunology & Medical Microbiology · doi:10.1016/j.femsim.2005.05.014 · Cited by 71 · see citing works
“The latter was detected only in a cytoplasmic extract and it may be a precursor of the former [46].”
BackgroundGreen, C. B., Zhao, X.-M., Yeater, K., & Hoyer, L. (2005) · Microbiology · doi:10.1099/mic.0.27696-0 · Cited by 68 · see citing works
“One example is the ALS (agglutinin-like sequence) gene family that encodes cell-surface glycoproteins involved in adhesion to host surfaces and potentially other cellular processes ( Gaur K Hoyer,2001;Fuetal.,2002;Zhaoetal., 2004; Sheppard et al., 2004).”
BackgroundFungal allergy and pathogenicity
Breitenbach, M., Crameri, R., & Lehrer, S. (2002) · doi:10.1590/s0036-46652002000600012 · Cited by 68
Molecular and cellular mechanisms for microbial entry into the CNS.
Zhang, J.-R., & Tuomanen, E. (1999) · Journal of Neurovirology · doi:10.3109/13550289909021288 · Cited by 64 · see citing works
“Other C. albicans proteins such as ALA1 (Gaur and Klotz, 1997) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Gozalbo et al, 1998) have been reported to mediate adherence of the fungus to various extracellular matrix proteins.”
BackgroundUpadhyay, S., Mahajan, L., Ramjee, S., Singh, Y., Basir, S., & Madan, T. (2009) · Journal of Medical Microbiology · doi:10.1099/jmm.0.005991-0 · Cited by 63 · see citing works
“ECM proteins of the host, namely fibronectin, laminin, collagens and proteoglycans, are implicated in attachment of a number of fungal pathogens (Gaur & Klotz, 1997; Gil et al., 1996; Gonzalez et al., 2005; Lopez-Ribot & Chaffin, 1994; Mendes-Giannini et al., 2006; Tronchin et al., 1997; Wasylnka &…”
BackgroundRGD-mediated adhesion in fungal pathogens of humans, plants and insects.
Hostetter, M. K. (2000) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00101-6 · Cited by 63 · see citing works
Bamford, C. V., Nobbs, A., Barbour, M., Lamont, R., & Jenkinson, H. (2015) · Microbiology · doi:10.1099/mic.0.083378-0 · Cited by 62 · see citing works
“…signal peptide, an immunoglobulin (Ig)-like region (~300 aa), a conserved Thr-rich region, a central Thr-rich repeat domain (~470 aa residues), a Ser/Thr-rich C-terminal domain and a Cterminal glycosylphosphatidylinositol modification (Gaur & Klotz, 1997; Sheppard et al., 2004; Phan et al., 2007).”
BackgroundStudy of Candida albicans and its interactions with the host: A mini review
Tsai, P.-W., Chen, Y.-T., Hsu, P., & Lan, C. (2013) · Biomedicine · doi:10.1016/j.biomed.2012.12.004 · Cited by 53 · see citing works
“, fibronectin, laminin, and type IV collagen) and buccal and pharyngeal epithelial and vascular endothelial cells [77,78].”
BackgroundDifferential invasion of Candida albicans isolates in an in vitro model of oral candidosis.
Bartie, K., Williams, D., Wilson, M., Potts, A. J. C., & Lewis, M. (2004) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.2004.00155.x · Cited by 61 · see citing works
Analysis of PRA1 and Its Relationship to Candida albicans- Macrophage Interactions
Marcil, A., Gadoury, C., Ash, J., Zhang, J., Nantel, A., & Whiteway, M. (2008) · Infection and Immunity · doi:10.1128/iai.00588-07 · Cited by 59 · see citing works
“Overall, Candida albicans surface proteins can bind many host proteins, including fibrinogen (10), complement fragments (34), plasminogen (13), and extracellular matrix proteins such as collagen, fibronectin, and laminin (28).”
BackgroundA Genetic Code Alteration Is a Phenotype Diversity Generator in the Human Pathogen Candida albicans
Miranda, I., Rocha, R., Santos, M. C., Mateus, D. D., Moura, G. R., Carreto, L., & Santos, M. A. S. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000996 · Cited by 59 · see citing works
“serines with leucines at CUG positions increases adhesion [36–41].”
BackgroundGonzález, Á., Gómez, B., Díez, S., Hernández, O., Restrepo, A., Hamilton, A., & Cano, L. E. (2005) · Infection and Immunity · doi:10.1128/iai.73.4.2486-2495.2005 · Cited by 58 · see citing works
“Several fungi of clinical importance such as Candida albicans (10, 15, 16, 31); Aspergillus fumigatus (4, 11, 18, 37, 49); Histoplasma capsulatum (33); Cryptococcus neoformans (41); Pneumocystis carinii (27, 34); Sporothrix schenckii (29); and Penicillium marneffei (22, 23) are known to attach to ECM proteins.”
BackgroundHamilton, A., Jeavons, L., Youngchim, S., & Vanittanakom, N. (1999) · Infection and Immunity · doi:10.1128/iai.67.10.5200-5205.1999 · Cited by 56 · see citing works
“The short peptides (RGD and YIGSR) had no detectable effect on the interaction between conidia and fibronectin.”
BackgroundInfluentialAmyloid-Like β-Aggregates as Force-Sensitive Switches in Fungal Biofilms and Infections
Lipke, P., Klotz, S., Dufrêne, Y., Jackson, D., & Garcia-Sherman, M. C. (2017) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00035-17 · Cited by 55 · see citing works
“albicans Als5p in laboratory strains of Saccharomyces cerevisiae leads to the cells becoming adherent and aggregative (63, 68).”
BackgroundSelf-citationIntegrin-like proteins in Candida spp. and other microorganisms.
Hostetter, M. K. (1999) · Fungal Genetics and Biology · doi:10.1006/fgbi.1999.1165 · Cited by 55 · see citing works
Targeting the GPI biosynthetic pathway
Yadav, U., & Khan, M. A. (2018) · Pathogens and Global Health · doi:10.1080/20477724.2018.1442764 · Cited by 55 · see citing works
Chang, H.-T., Tsai, P.-W., Huang, H.-H., Liu, Y.-S., Chien, T.-S., & Lan, C.-Y. (2012) · Biochemical Journal · doi:10.1042/bj20111454 · Cited by 52 · see citing works
Zhao, X.-M., Oh, S.-H., Jajko, R., Diekema, D., Pfaller, M., Pujol, C., Soll, D., & Hoyer, L. (2007) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2007.05.004 · Cited by 49 · see citing works
“Genomic DNA from generation zero and generation 3000 was amplified by PCR to determine the number of copies of the tandem repeat sequence as described above for ALS5 and ALS6.”
BackgroundInfluentialZhao, X.-M., Oh, S.-H., & Hoyer, L. (2007) · Microbiology · doi:10.1099/mic.0.2006/005017-0 · Cited by 48 · see citing works
“Isolation of ALS1 and ALS5 based on their ability to confer adhesive function on the relatively non-adherent S. cerevisiae supported this hypothesis ( Gaur & Klotz, 1997; Fu et al., 1998).”
BackgroundThe Beer Brewing Process: Wort Production and Beer Fermentation
Willaert, R. (2006) · doi:10.1002/9780470113554.ch20 · Cited by 48 · see citing works
Smith, D. F. Q., & Casadevall, A. (2021) · Pathogens and Disease · doi:10.1093/femspd/ftab013 · Cited by 47 · see citing works
Interaction of α-Agglutinin and a-Agglutinin,Saccharomyces cerevisiae Sexual Cell Adhesion Molecules
Zhao, H.-Z. J., Shen, Z.-M., Kahn, P., & Lipke, P. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.9.2874-2880.2001 · Cited by 47 · see citing works
Secreted proteinases and other virulence mechanisms of Candida albicans.
Monod, M., & Borg-von-Zepelin, M. (2002) · Chemical Immunology · doi:10.1159/000058865 · Cited by 47 · see citing works
Dehullu, J., Valotteau, C., Herman-Bausier, P., Garcia-Sherman, M. C., Mittelviefhaus, M., Vorholt, J., Lipke, P., & Dufrêne, Y. (2019) · Nano letters (Print) · doi:10.1021/acs.nanolett.9b01010 · Cited by 46 · see citing works
Gaur, N., Smith, R., & Klotz, S. (2002) · Cell Communication & Adhesion · doi:10.1080/15419060212187 · Cited by 46 · see citing works
“Ala1/Als5p-mediated adherence includes such properties as stability to shear forces, activity over broad pH optima, and resistance to blocking by many biological molecules, and it occurs within seconds of exposure of the fungus to the substrate (4, 5).”
BackgroundMethodResultInfluentialSelf-citationLamarre, C., Deslauriers, N., & Bourbonnais, Y. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01715.x · Cited by 46 · see citing works
“During the course of this study, Gaur and Klotz (1997) reported the cloning of the C. albicans ALA1 gene through sorting of S. cerevisiae transformants with magnetic beads coated with extracellular matrix proteins.”
BackgroundMolecular Genetic and Genomic Approaches to the Study of Medically Important Fungi
Magee, P. T., Gale, C. A., Berman, J., & Davis, D. A. (2003) · Infection and Immunity · doi:10.1128/iai.71.5.2299-2309.2003 · Cited by 45 · see citing works
Manfredi, M., McCullough, M., Al-Karaawi, Z., Vescovi, P., & Porter, S. (2006) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.2006.00275.x · Cited by 42 · see citing works
Li, F., & Palecek, S. (2005) · Biotechnology progress (Print) · doi:10.1021/bp050236c · Cited by 42 · see citing works
- Authors
- Gaur, N. K., & Klotz, S. A.
- Affiliations
- United States Department of Veterans Affairs (US)
- ORCID
- Klotz, S A
- Venue
- Infection and Immunity
- Publisher
- American Society for Microbiology
- Published
- 1997-12
- Volume
- 65
- Issue
- 12
- Pages
- 5289-5294
- ISSN
- 0019-9567 (ISSN-L)
- 1098-5522
- PMC
- PMC175761
- OpenAlex
- W2119843708
- Cited by
- 182
- References
- 0
- Citations by year
- 2025: 1 · 2023: 2 · 2022: 1 · 2021: 4 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 4 · 2016: 5 · 2015: 3 · 2014: 13 · 2013: 5 · 2012: 7
- FWCI
- 2.73
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Infection and Immunity (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
- Keywords
- Candida albicans, adhesins, extracellular matrix proteins, fibronectin, type IV collagen, laminin, fungal adhesion, ALS1, tandem repeats, buccal epithelial cells, candidiasis, gene cloning
- MeSH terms
- Amino Acid Sequence, Candida albicans, Cell Adhesion, Cloning, Molecular, Fungal Proteins, Genes, Fungal, Humans, Molecular Sequence Data, Saccharomyces cerevisiae, Cell Adhesion Molecules, Extracellular Matrix Proteins, Sequence Analysis
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