The DOI matches its Crossref record; 56 of the 59 references it cites were found in a registry or an index.
Functional and Structural Diversity in the Als Protein Family of Candida albicans
Open accessAbstract
The human fungal pathogen Candida albicans colonizes and invades a wide range of host tissues. Adherence to host constituents plays an important role in this process. Two members of the C. albicans Als protein family (Als1p and Als5p) have been found to mediate adherence; however, the functions of other members of this family are unknown. In this study, members of the ALS gene family were cloned and expressed in Saccharomyces cerevisiae to characterize their individual functions. Distinct Als proteins conferred distinct adherence profiles to diverse host substrates. Using chimeric Als5p-Als6p constructs, the regions mediating substrate-specific adherence were localized to the N-terminal domains in Als proteins. Interestingly, a subset of Als proteins also mediated endothelial cell invasion, a previously unknown function of this family. Consistent with these results, homology modeling revealed that Als members contain anti-parallel beta-sheet motifs interposed by extended regions, homologous to adhesins or invasins of the immunoglobulin superfamily. This finding was confirmed using circular dichroism and Fourier transform infrared spectrometric analysis of the N-terminal domain of Als1p. Specific regions of amino acid hypervariability were found among the N-terminal domains of Als proteins, and energy-based models predicted similarities and differences in the N-terminal domains that probably govern the diverse function of Als family members. Collectively, these results indicate that the structural and functional diversity within the Als family provides C. albicans with an array of cell wall proteins capable of recognizing and interacting with a wide range of host constituents during infection.
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In the citing paper
“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 [23]
In the citing paper
“We found that Saccharomyces cerevisiae expressing Als3 were avidly endocytosed by endothelial cells.”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
In the citing paper
“Also, we found that S. cerevisiae expressing Als3 bound to both endothelial cells and FaDu oral epithelial cells [23].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
In the citing paper
“Similar experiments suggested that Als1 and Als5 could also induce endocytosis, although with considerably less efficiency than Als3 [23].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
In the citing paper
“The N-terminal domain contains the substratebinding region [23,26].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
In the citing paper
“Computer-assisted modeling of the N-termini of Als1, Als3, and Als5 predicts the presence of antiparallel b sheets that define the immunoglobulin superfamily [23].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
In the citing paper
“Previously, we determined that the N-terminal region of Als proteins contains the substrate-binding site [23,26].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
In the citing paper
“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 [23]
In the citing paper
“When expressed in S. cerevisiae, Als5 induces weak endothelial cell endocytosis similar to that induced by Als1 [23].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
In the citing paper
“Previously, we have reported that S. cerevisiae expressing Als1 or Als3 binds to a variety of host constituents, including endothelial cells, epithelial cells, laminin, and fibronectin [23].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [23]
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“The N-terminal domain has been directly involved in the binding of different cell types (Loza et al. 2004) and is predicted to have an immunoglobulin-like fold (Sheppard et al. 2004).”
BackgroundEncounters with Mammalian Cells: Survival Strategies ofCandidaSpecies
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“…native like conditions, (iii) A central region of a variable number of 36 amino acid tandem repeats, and (iv) A C-terminal domain that is rich in serine and threonine, which is relatively variable among the Als members (Salgado et al., 2011; Sheppard et al., 2004; Zhao, Pujol, Soll, & Hoyer, 2003).”
BackgroundResultAncient Phylogenetic Beginnings of Immunoglobulin Hypermutation
Kubrycht, J., Sigler, K., Růz̆ic̆ka, M., Souček, P., Borecký, J., & Ježek, P. (2006) · Journal of Molecular Evolution · doi:10.1007/s00239-006-0051-9 · Cited by 7
“Despite this result, other different structural relationships to Ig domains or Ig superfamily were described in several papers dealing with unicellular Eukaryota (Wojciechowicz et al. 1993; Chiang et al. 2001, 2002; Sheppard et al. 2004).”
BackgroundGenetic Basis of Biofilm Formation and Spread of Nosocomial Infections
Koley, S., & Mukherjee, M. (2021) · Springer protocols handbooks/Springer protocols · doi:10.1007/978-1-0716-1378-8_12 · Cited by 5
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Self-citationPathogenicity and virulence of Candida auris
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“Of note, Als4112 is also recognized by the Als3-targeting fungal vaccine NDV-3A [132], suggesting functional similarities with C. albicans Als3 [133].”
Kim, D., Kim, J.-S., Bai, X., Zhang, J., Park, M., Lee, U., Lee, J., Bahn, Y., Xu, Y., & Ha, N. (2025) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2411.11076 · Cited by 7
“The NT domain is directly involved in the adhesion of Als proteins to various substrates and contains two immunoglobulin-like (Ig-like) domains with a peptide-binding cavity (PBC) between them [17, 18].”
Satała, D., Karkowska‐Kuleta, J., Braś, G., Rąpała‐Kozik, M., & Kozik, A. (2023) · Yeast · doi:10.1002/yea.3847 · Cited by 7
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“Each Als adhesin has two Ig-like invasin domains at the N-terminal (Figure 1, colored purple) [14–16].”
Chabane, M., Touil, A. T., Khelladi, B., Meddah, B., & Mokhtar, M. (2020) · Pharmaceutical Sciences · doi:10.34172/ps.2020.35 · Cited by 5
“Several mechanisms of virulence are known to contribute to the ability of this fungus to colonize and invade the cells, the expression of the molecules of recognition of the host or of adhesion molecules, the secretion of hydrolytic enzymes such as lipases, phospholipases and aspartyl proteases.(66)”
BackgroundCandida albicans: Clinical Relevance, Pathogenesis, and Host Immunity
Correia, A., Sampaio, P., Vilanova, M., & Pais, C. (2015) · Wiley eBooks · doi:10.1002/9781118644843.ch50 · Cited by 4
Recent advances in understanding human opportunistic fungal pathogenesis mechanisms
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“albicans ALA1 gene product can bind to fibronectin, laminin and type IV collagen, all components either of the basal membrane or the extracellular matrix [21,22].”
BackgroundEffect of tobacco tar on Staphylococcus aureus and Candida albicans biofilm formation
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“Most ALS proteins have adhesin functions (Sheppard et al., 2004; Zhao et al., 2005).”
Salgado, P. S., Yan, R., Rowan, F. C., & Cota, E. (2011) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309111003460 · Cited by 3
“The N-terminal region, in which the observed cell-adhesion properties have been shown to reside (Sheppard et al., 2004; Loza et al., 2004), is predicted to form a predominant -structure.”
BackgroundTranscriptional Regulation of Azole Antifungal Resistance and Tolerance in Candida Glabrata
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“Targeting antimicrobial fight by blocking adhesins ALS3 against adhesins of Candida can be very promising as well to combat S. aureus due to the sequence and structural homology of ALS3 with cell surface proteins on S. aureus [57].”
Candida auris adhesins, specifically Als3, a key target to understand and mitigate
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“Mutations in the PBC significantly impair adhesion and biofilm formation, underscoring its essential role in host-pathogen interactions (Kim et al. 2025; Lin et al. 2014) (Cota and Hoyer 2015; Liu and Filler 2011).”
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“Consistent with this defect in hyphal morphogenesis, strain JL01 was also defective in the expression of hypha-specific genes, including HWP1 (Staab et al. 1999), ECE1 (Birse et al. 1993), and ALS3 (Sheppard et al. 2004) (FIG.”
BackgroundInfluentialAdvances in Genomics of Human Fungal Pathogens
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Molecular Pathogenesis of Fungal Infections
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Kulig, K., Zuzanna, M., Kowalik, K., Michalina, M., Bednarek, A., Satała, D., Juszczak, M., Łabędzka-Dmoch, K., Woźnicka, O., Pyza, E., et al. (2026) · Archives of Microbiology · doi:10.1007/s00203-026-04713-z · Cited by 1
“…an adhesin from the agglutinin-like protein family, which plays a crucial role in binding various host proteins, including laminin and fibronectin (Sheppard et al. 2004 ), high-molecular-weight kininogen and coagulation factor XII (Seweryn et al. 2015 ), as well as neutrophil extracellular traps…”
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BackgroundIdentification of heparin‐binding proteins expressed on Trichosporon asahii cell surface
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“Several adhesive molecules, such as agglutinin ‐ like sequence family proteins and hyphal wall protein 1, have been reported in pathogenic yeast (de Groot et al., 2013; Sheppard et al., 2004).”
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“…de la cellule à écoulement à l’étude de la formation du biofilm à C. albicans, dans les différentes conditions étudiées dans ce travail (silice seule, conditionnée par des protéines, avec AgNPs,…) (Skerl et al., 1984; Chandra et al., 2001; Sheppard et al., 2004; Nett et al., 2016; Willaert, 2018).”
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“Este agente de amplio espectro (figura 1), conocido por su acción inhibitoria sobre la inositol acetiltransferasa del hongo, altera la maduración de las proteínas ancladas al glicosilfosfatidilinositol (GPI) (56) y, por tanto, impide que actúen como adhesinas (57) para los hongos que entran a las células (58).”
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Bruchlen, D. (2016) · theses.fr (ABES) · doi:10.70675/862d474az0392z478bza236zfef48870b895 · Cited by 1
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“albicans ALS gene family mediate endothelial cell adherence.(12-18) Also, C.”
BackgroundSelf-citationCaracterização funcional dos genes PGA13 e PGA58 de Candida albicans
Fernandes, F. F. (2008) · doi:10.11606/d.17.2008.tde-17122008-132351 · Cited by 1
“Fatores de virulência em C. albicans incluem proteínas que medeiam aderência e invasão ao tecido do hospedeiro (Sheppard et al., 2004), mudanças morfológicas de levedura para hifa (Mitchell, 1998), secreção de enzimas líticas (Sanglard et al., 1997), supressão da resposta do sistema imunológico…”
Candida Albicans: New Insights in Infection, Disease, and Treatment
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“NDV-3 was initially developed as a vaccine against candidemia (184) and contains a recombinant form of the agglutinin-like sequence 3 protein (Als3p) of Candida albicans (183, 280).”
Javaid, A., Tabassum, N., Siddiqui, Y. M., Karthikeyan, A., Charway, G. N. A., Hassan, M. I., Kim, Y., & Khan, F. (2026) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2026.2727092
“…molecules; these are multi-domain, cell wall-anchored polypeptides of S. gordonii that act as multifunctional surface molecules and bind both host proteins like salivary gp-340 and fibronectin, as well as bacteria of other species (Figure 6 ; table 1) (Sheppard et al. 2004; Hoyer et al. 2014).”
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Rosiana, S., Zhang, L.-Y., Kim, G. H. E., Revtovich, A. V., Sukumaran, A., Geddes-McAlister, J., Kirienko, N. V., & Shapiro, R. S. (2020) · bioRxiv · doi:10.1101/2020.10.22.350991
“…aspects of adhesion, host-pathogen interactions, filamentation, and fungal virulence (Fu et al. 1998, 2002; Hoyer et al. 1998; Zhao et al. 2004; Sheppard et al. 2004; Ibrahim et al. 2005; Phan et al. 2007; Nobile et al. 2008; Almeida et al. 2008; Donohue et al. 2011; Cleary et al. 2011), while…”
BackgroundChoteau, L. (2016) · theses.fr (ABES) · doi:10.70675/683e2513z5ac6z4a43z8ec5z40068786c8b6
“Ces protéines permettent l’adhésion aux cellules épithéliales par des liaisons non covalentes alors que d’autres adhésines, comme Hwp1, permettent une adhésion par liaison covalente (Sheppard et al. 2004).”
Poissy, J. (2014) · theses.fr (ABES) · doi:10.70675/ddead8ccz638fz4c1dz9850z72dc9db47c65
“Cette partie est variable, similaire à la partie N-terminale des immunoglobulines, et cette variabilité explique les nombreux ligands possibles en fonction de l'Als [71].”
BackgroundHao, Y., Wang, R., Liao, H., Wang, M., Ye, Z., Liu, Y., Quanzhen, L., Zhang, D., Yan, L., & Xie, F. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.118991
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Self-citationSahni, N. (2010) · doi:10.17077/etd.ue8df5vw
“, 2006a), exhibit reduced adherence to vascular endothelial cells and oral epithelial cells (Fu et al., 2002; Zhao et al., 2004; Sheppard et al., 2004).”
BackgroundInfluentialSong, Y. (2009) · doi:10.17077/etd.w1r9nmxk
“These mutants also exhibited reduced adherence to vascular endothelial cells and oral epithelial cells (Fu et al., 2002; Zhao et al., 2004; Sheppard et al., 2004).”
BackgroundInteractions of Fungi with Endothelial Cells
Filler, S. G., & Sheppard, D. C. (2005) · Springer eBooks · doi:10.1007/0-387-25445-5_20
“In vitro, Als1p, Als3p, and Als5p mediate binding to multiple substrates in addition to endothelial cells, including fibronectin, laminin, collagen, and an oral epithelial cell line (Gaur and Klotz, 1997; Fu et al., 1998; Gauret al., 1999; Klotz et al., 2004; Sheppard et al., 2004b ).”
BackgroundInfluentialSelf-citation(2004) · Yeast · doi:10.1002/yea.1157
Metadata
- Authors
- 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.
- Affiliations
- University of California, Los Angeles (US)
- University of Nevada, Reno (US)
- California State University, Long Beach (US)
- Corresponding author
- Sheppard, Donald C.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-07
- Volume
- 279
- Issue
- 29
- Pages
- 30480-30489
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1968095975
- Cited by
- 300
- References
- 59
- Citations by year
- 2026: 9 · 2025: 7 · 2024: 5 · 2023: 9 · 2022: 10 · 2021: 15 · 2020: 15 · 2019: 7 · 2018: 14 · 2017: 11 · 2016: 11 · 2015: 12 · 2014: 27 · 2013: 16 · 2012: 13
- FWCI
- 6.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (P01 AI-37194, R01AI019990, R01 AI-48031, R03AI054531, R01-AI19990, R01AI054928, R01AI048031, P01AI037194)
- National Institute of Dental and Craniofacial Research (R01DE013974, 5R01 DE13974)
- National Center for Research Resources (M01RR000425, M01-RR00425)
- 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, fungal adhesion, endothelial cell invasion, N-terminal domain, antiparallel beta-sheet, cell wall proteins, host-pathogen interaction, fusion protein
- MeSH terms
- Amino Acid Sequence, Candida albicans, Cell Adhesion, Cell Wall, Circular Dichroism, Cloning, Molecular, Endothelium, Vascular, Epithelial Cells, Flow Cytometry, Fungal Proteins, Multigene Family, Humans, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Plasmids, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Substrate Specificity, Cell Adhesion Molecules, Polymerase Chain Reaction, Protein Structure, Secondary, Protein Structure, Tertiary, Spectroscopy, Fourier Transform Infrared, DNA Primers, Amino Acid Motifs, Cell Line, Tumor
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