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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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“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]
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“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]
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“The emergence of initial functional data for Als1p and Als5p is important because they have the most similar N-terminal domain sequences (87% amino acid identity) within the ALS family (Hoyer et al., 1995; Gaur & Klotz, 1997; Hoyer & Hecht, 2000; Fu et al., 2002).”
InfluentialCandida albicans binds human plasminogen: identification of eight plasminogen‐binding proteins
Crowe, J. D., Sievwright, I. K., Auld, G. C., Moore, N. R., Gow, N. A. R., & Booth, N. A. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03390.x · Cited by 246
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ResultInfluentialGozalbo, D., Gil-Navarro, I., Azorín, I., Renau-Piqueras, J., Martínez, J. P., & Gil, M. (1998) · Infection and Immunity · doi:10.1128/iai.66.5.2052-2059.1998 · Cited by 231
“(4) and for the ALA1 gene product (15).”
BackgroundHoefs, S., Mogavero, S., & Hube, B. (2016) · The Journal of Microbiology · doi:10.1007/s12275-016-5514-0 · Cited by 251
“The eight members that are encoded by the ALS gene family (ALS1-7 and ALS9) are cell surface proteins and are glycosylphosphatidylinositol (GPI)linked to the ß-1,6-glucans of the fungal cell wall (Gaur and Klotz, 1997; Hoyer, 2001; Sheppard et al., 2004).”
BackgroundInfluentialInteractions of Candida albicans with epithelial cells
Zhu, W., & Filler, S. G. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01412.x · Cited by 223
“encodes eight glycosylphosphatidylinositol (GPI)-linked cell surface proteins that mediate binding to diverse host substrates (Gaur and Klotz, 1997; Hoyer, 2001; Sheppard et al., 2004; Zhao et al., 2004; 2005; Braun et al., 2005).”
BackgroundInfluentialAntifungal proteins: targets, mechanisms and prospective applications
Theis, T., & Stahl, U. (2004) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-003-3231-4 · Cited by 222
Bougnoux, M., Morand, S., & d'Enfert, C. (2002) · Journal of Clinical Microbiology · doi:10.1128/jcm.40.4.1290-1297.2002 · Cited by 216
“c CaSYA1 is the ortholog of the ScALA1 gene encoding alanyl-tRNA synthetase; however, the designation CaALA1 could not be used because it corresponds to a gene encoding an agglutinin-like adhesin (11).”
BackgroundOrigins of variation in the fungal cell surface
Verstrepen, K. J., Reynolds, T. B., & Fink, G. R. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro927 · Cited by 204
Jong, A. Y., Chen, S. H. M., Stins, M. F., Kim, K. S., Tuan, T.-L., & Huang, S.-H. (2003) · Journal of Medical Microbiology · doi:10.1099/jmm.0.05060-0 · Cited by 206
“Downloaded from www.microbiologyresearch.org by IP: 54.70.40.11 On: Wed, 05 Dec 2018 12:28:50 ofC. albicans INT1 (Gale et al., 1998),ALS1 (Fu et al., 1998b), ALA1 (Gaur & Klotz, 1997) or CAD1/AAF1 (Fu et al., 1998a) genes in S. cerevisiae is sufficient to direct the adhesion of this normally non-adherent yeast to huma…”
BackgroundInfluentialEAP1 , a Candida albicans Gene Involved in Binding Human Epithelial Cells
Li, F., & Palecek, S. P. (2003) · Eukaryotic Cell · doi:10.1128/ec.2.6.1266-1273.2003 · Cited by 189
Hoyer, L. L., & Cota, E. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00280 · Cited by 229
“Additional effort revealed the full nature of the ALS family in C. albicans (Gaur and Klotz, 1997; Hoyer et al., 1998b; Hoyer and Hecht, 2000, 2001; Zhao et al., 2007a), which proved to be essential for accurate assembly of the C. albicans genome sequence Abbreviations: AFR, amyloid-forming region;…”
BackgroundGreen, C. B., Cheng, G., Chandra, J., Mukherjee, P. K., Ghannoum, M. A., & Hoyer, L. L. (2004) · Microbiology · doi:10.1099/mic.0.26699-0 · Cited by 159
“Among these is the ALS (agglutinin-like sequence) family that encodes cell-wall glycoproteins, some of which are involved in adherence to host surfaces ( Gaur & Klotz, 1997; Hoyer, 2001; Fu et al., 2002).”
BackgroundAspects of Fungal Pathogenesis in Humans
van Burik, J. H., & Magee, P. T. (2001) · Annual Review of Microbiology · doi:10.1146/annurev.micro.55.1.743 · Cited by 176
Candida albicans-epithelial interactions and pathogenicity mechanisms: scratching the surface
Moyes, D. L., Richardson, J. P., & Naglik, J. R. (2015) · Virulence · doi:10.1080/21505594.2015.1012981 · Cited by 197
Zhao, X.-M., Oh, S.-H., Yeater, K., & Hoyer, L. (2005) · Microbiology · doi:10.1099/mic.0.27763-0 · Cited by 166
“Overproduction of other Als proteins in Saccharomyces cerevisiae produced an adherent phenotype for this normally non-adherent organism, suggesting they may also play a role in C. albicans adhesion (Gaur & Klotz, 1997; Sheppard et al., 2004).”
BackgroundNugaeva, N., Gfeller, K. Y., Backmann, N., Lang, H., Düggelin, M., & Hegner, M. (2005) · Biosensors & bioelectronics · doi:10.1016/j.bios.2005.02.004 · Cited by 164
“Pathogenic yeast and mycelial fungi adhere to Fn molecules at different sites: the 40-kDa GAG-binding domain, the 120-kDa domain and the RGD sequence ( Guar and Klotz, 1997; Lima et al., 2001).”
BackgroundFu, Y., Rieg, G., Fonzi, W. A., Belanger, P. H., Edwards, J. E., & Filler, S. G. (1998) · Infection and Immunity · doi:10.1128/iai.66.4.1783-1786.1998 · Cited by 159
“Recently, Gaur and Klotz (4) described another member of the ALS gene family, ALA1.”
BackgroundFrieman, M. B., McCaffery, J. M., & Cormack, B. P. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03166.x · Cited by 150
“A particularly well-characterized family of GPI-CWPs in C. albicans is encoded by the ALS genes (Hoyer, 2001), at least two members of which, ALS1 and ALA1, encode adhesins (Gaur and Klotz, 1997; Fu et al., 1998).”
BackgroundInfluentialYeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences
Ramsook, C. B., Tan, C., Garcia, M. C., Fung, R., Soybelman, G., Henry, R., Litewka, A., O'Meally, S., Otoo, H., Khalaf, R. A., et al. (2009) · Eukaryotic Cell · doi:10.1128/ec.00068-09 · Cited by 156
“Aggregation assays for Als adhesins were carried out as previously described (15).”
MethodSelf-citationSundstrom, P. (1999) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(99)80062-9 · Cited by 134
Eap1p, an Adhesin That Mediates Candida albicans Biofilm Formation In Vitro and In Vivo
Li, F., Svarovsky, M. J., Karlsson, A. J., Wagner, J. P., Marchillo, K., Oshel, P. E., Andes, D. R., & Palecek, S. P. (2007) · Eukaryotic Cell · doi:10.1128/ec.00049-07 · Cited by 154
“albicans genes encoding GPI-CWP adhesins, including ALS1, ALS2, ALS4, ALS5 (ALA1), HWP1, and EAP1, mediate adhesion to organic and inorganic surfaces, extracellular matrix proteins, human endothelial cells, and epithelial cells (15, 17, 32, 51, 61).”
BackgroundGlycan microarray analysis of Candida glabrata adhesin ligand specificity
Zupancic, M. L., Frieman, M., Smith, D., Alvarez, R. A., Cummings, R. D., & Cormack, B. P. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06184.x · Cited by 143
“…of several of the Als proteins have been characterized – for example,Als1,Als3 andAls5 have been found to adhere, to varying degrees, to both epithelial and endothelial cell types, as well as to extracellular matrix proteins (Gaur and Klotz, 1997; Fu et al., 1998; Sheppard et al., 2004).”
BackgroundCandida albicans Als Adhesins Have Conserved Amyloid-Forming Sequences
Otoo, H., Lee, K., Qiu, W.-G., & Lipke, P. (2007) · Eukaryotic Cell · doi:10.1128/ec.00309-07 · Cited by 139
“These cell wall-bound adhesins bind to diverse mammalian peptide ligands, cause cellular aggregation through homotypic adhesion (8, 16, 17), and also coaggregate with other microbial pathogens to mediate polymicrobial infections (15).”
BackgroundAdherence mechanisms in human pathogenic fungi
Tronchin, G., Pihet, M., Lopes-Bezerra, L. M., & Bouchara, J. (2008) · Medical Mycology · doi:10.1080/13693780802206435 · Cited by 139
A Role for Amyloid in Cell Aggregation and Biofilm Formation
Garcia, M. C., Lee, J. T., Ramsook, C. B., Alsteens, D., Dufrêne, Y. F., & Lipke, P. N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017632 · Cited by 128
“Generation of V5-tagged Als5p and Als5p V5-tagged Als5p was generated by restriction digestion of pGK114 with BamHI and XhoI which released the Als5p sequence from the vector backbone [39].”
BackgroundMethodResultCandida albicans Als proteins mediate aggregation with bacteria and yeasts.
Klotz, S., Gaur, N., Armond, R. L. D., Sheppard, D., Khardori, N., Edwards, J., Lipke, P., & El-azizi, M. (2007) · Medical Mycology · doi:10.1080/13693780701299333 · Cited by 125
Self-citationTsukahara, K., Hata, K., Nakamoto, K., Sagane, K., Watanabe, N.-A., Kuromitsu, J., Kai, J.-K., Tsuchiya, M., Ohba, F., Jigami, Y., et al. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03481.x · Cited by 117
“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).”
BackgroundThreonine-Rich Repeats Increase Fibronectin Binding in the Candidaalbicans Adhesin Als5p
Rauceo, J. M., De Armond, R., Otoo, H., Kahn, P. C., Klotz, S. A., Gaur, N. K., & Lipke, P. N. (2006) · Eukaryotic Cell · doi:10.1128/ec.00120-06 · Cited by 115
“The TR region of Als5p consists of six copies of a 36-mer repeat that is rich in Thr and other -branched amino acids (8).”
BackgroundSelf-citationOh, S.-H., Cheng, G., Nuessen, J. A., Jajko, R., Yeater, K. M., Zhao, X., Pujol, C., Soll, D. R., & Hoyer, L. L. (2005) · Microbiology · doi:10.1099/mic.0.27680-0 · Cited by 108
“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).”
BackgroundImproved efficacy of antifungal drugs in combination with monoterpene phenols against Candida auris
Shaban, S., Patel, M., & Ahmad, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-58203-3 · Cited by 107
Cheng, G., Wozniak, K. L., Wallig, M. A., Fidel, P. L., Trupin, S. R., & Hoyer, L. L. (2005) · Infection and Immunity · doi:10.1128/iai.73.3.1656-1663.2005 · Cited by 93
“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).”
BackgroundN-Glycosylation of yeast, with emphasis onCandida albicans
Cutler, J. E. (2001) · Medical Mycology · doi:10.1080/mmy.39.1.75.86 · Cited by 76
Strengthening relationships: amyloids create adhesion nanodomains in yeasts
Lipke, P. N., Garcia, M. C., Alsteens, D., Ramsook, C. B., Klotz, S. A., & Dufrêne, Y. F. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2011.10.002 · Cited by 104
“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].”
BackgroundInfluentialSelf-citationCandida albicans Interactions with Mucosal Surfaces during Health and Disease
Nikou, S.-A., Kichik, N., Brown, R., Ponde, N., Ho, J., Naglik, J., & Richardson, J. (2019) · Pathogens · doi:10.3390/pathogens8020053 · Cited by 103
Hoyer, L. L., Payne, T. L., & Hecht, J. E. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.20.5334-5343.1998 · Cited by 103
“Accession numbers for other sequences discussed here include L25902 (ALS1 [26]), U87856 (ALS3 [25]), and AF025429 (ALA1/ALS5 [18]).”
BackgroundFrieman, M., & Cormack, B. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03722.x · Cited by 98
Unfolding Individual Als5p Adhesion Proteins on Live Cells
Alsteens, D., Duprès, V., Klotz, S. A., Gaur, N. K., Lipke, P. N., & Dufrêne, Y. F. (2009) · ACS Nano · doi:10.1021/nn900078p · Cited by 92
“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.”
BackgroundMethodSelf-citationLi, F., & Palecek, S. P. (2008) · Microbiology · doi:10.1099/mic.0.2007/013789-0 · Cited by 91
“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).”
BackgroundDouglas, L., Li, L., Yang, Y., & Dranginis, A. (2007) · Eukaryotic Cell · doi:10.1128/ec.00284-06 · Cited by 94
“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
Goossens, K. V. Y., & Willaert, R. (2010) · Biotechnology Letters · doi:10.1007/s10529-010-0352-3 · Cited by 92
“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.”
BackgroundSalgado, P. S., Yan, R., Taylor, J. D., Burchell, L., Jones, R., Hoyer, L. L., Matthews, S., Simpson, P. J., & Cota, E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103496108 · Cited by 85
“Data were processed with NMRPipe (6) and analyzed with NMRview (7).”
BackgroundMethodGaur, N. K., Klotz, S. A., & Henderson, R. L. (1999) · Infection and Immunity · doi:10.1128/iai.67.11.6040-6047.1999 · Cited by 84
“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
“this adherence assay; all are equivalent (6), and the adherence of the fungal cells”
BackgroundSelf-citationIbrahim, A. S., Spellberg, B. J., Avenissian, V., Fu, Y., Filler, S. G., & Edwards, J. E. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.999-1005.2005 · Cited by 83
“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. N. (2018) · Journal of Fungi · doi:10.3390/jof4020059 · Cited by 99
“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 80
Candida 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
“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. A., McKinnon, S., Whiteway, M. S., & Pinto, D. M. (2006) · PROTEOMICS · doi:10.1002/pmic.200500100 · Cited by 78
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
“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
Zhang, N., Harrex, A. L., Holland, B. R., Fenton, L. E., Cannon, R. D., & Schmid, J. (2003) · Genome Research · doi:10.1101/gr.1024903 · Cited by 76
“…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., Pujol, C., Soll, D. R., & Hoyer, L. L. (2003) · Microbiology · doi:10.1099/mic.0.26495-0 · Cited by 74
“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.”
BackgroundNissen, T. L., Anderlund, M., Nielsen, J., Villadsen, J., & Kielland‐Brandt, M. C. (2000) · Yeast · doi:10.1002/1097-0061(200101)18:1 · Cited by 125
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.-L., et al. (2000) · Medical Mycology · doi:10.1080/mmy.38.s1.125.137 · Cited by 60
Fernández-Álvarez, A., Elías-Villalobos, A., & Ibeas, J. (2009) · The Plant Cell Online · doi:10.1105/tpc.109.065839 · Cited by 71
“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. J. S., Soares, C. P., da Silva, J. L. M., & Andreotti, P. F. (2005) · FEMS Immunology & Medical Microbiology · doi:10.1016/j.femsim.2005.05.014 · Cited by 77
“The latter was detected only in a cytoplasmic extract and it may be a precursor of the former [46].”
BackgroundGreen, C. B., Zhao, X., Yeater, K. M., & Hoyer, L. L. (2005) · Microbiology · doi:10.1099/mic.0.27696-0 · Cited by 64
“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
“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
“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
Bamford, C. V., Nobbs, A. H., Barbour, M. E., Lamont, R. J., & Jenkinson, H. F. (2014) · Microbiology · doi:10.1099/mic.0.083378-0 · Cited by 61
“…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
“, 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
Analysis ofPRA1and Its Relationship toCandida albicans- Macrophage Interactions
Marcil, A., Gadoury, C., Ash, J., Zhang, J., Nantel, A., & Whiteway, M. S. (2008) · Infection and Immunity · doi:10.1128/iai.00588-07 · Cited by 57
“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
“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
“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
“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. N., Klotz, S. A., Dufrêne, Y. F., Jackson, D. N., & Garcia, M. C. (2017) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00035-17 · Cited by 64
“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
Targeting the GPI biosynthetic pathway
Yadav, U., & Khan, M. A. (2018) · Pathogens and Global Health · doi:10.1080/20477724.2018.1442764 · Cited by 55
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
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
“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., Oh, S.-H., & Hoyer, L. L. (2007) · Microbiology · doi:10.1099/mic.0.2006/005017-0 · Cited by 46
“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
Smith, D. F. Q., & Casadevall, A. (2021) · Pathogens and Disease · doi:10.1093/femspd/ftab013 · Cited by 48
Zhao, H. F., Shen, Z., Kahn, P. C., & Lipke, P. N. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.9.2874-2880.2001 · Cited by 53
Secreted Proteinases and Other Virulence Mechanisms of Candida albicans
Monod, M., & Zepelin, M. B. (2002) · KARGER eBooks · doi:10.1159/000058865 · Cited by 44
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
Gaur, N., Smith, R., & Klotz, S. (2002) · Cell Communication & Adhesion · doi:10.1080/15419060212187 · Cited by 46
“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
“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. G., & Davis, D. A. (2003) · Infection and Immunity · doi:10.1128/iai.71.5.2299-2309.2003 · Cited by 42
Manfredi, M., McCullough, M. J., Al‐Karaawi, Z. M., Vescovi, P., & Porter, S. R. (2006) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.2006.00275.x · Cited by 37
Li, F., & Palecek, S. P. (2005) · Biotechnology Progress · doi:10.1021/bp050236c · Cited by 32
Metadata
- 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 › Infectious Diseases › 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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