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 impact of human vaccines on bacterial antimicrobial resistance. A review
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“llowed by binding to microplate-immobilized fibronectin [16]”
BackgroundInfluentialStructure and Function of Glycosylated Tandem Repeats from Candida albicans Als Adhesins
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“albicans to host cells or to each other (Hoyer, 2001; Fu et al., 2002; Sheppard et al., 2004; Hoyer et al., 2008; Phan et al., 2007).”
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“Als3 is able to bind extracellular matrix (ECM) proteins, epithelial and endothelial cells (Fu et al., 1998; Sheppard et al., 2004; Zhao et al., 2004; Liu & Filler, 2011), induce endocytosis via adherence to E- or Ncadherins (Phan et al.”
BackgroundInfluentialStudy of Candida albicans and its interactions with the host: A mini review
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“laminin [80].”
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Candida albicans protein kinase CK2 governs virulence during oropharyngeal candidiasis
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“Adherence assay The adherence of the C. albicans strains to oral epithelial cells and endothelial cells was measured using a minor modification of our previously described assay (Sheppard et al., 2004).”
MethodSelf-citationLemberg, C., Vicente, K. M. D. S., Fróis-Martins, R., Altmeier, S., Tran, V. D. T., Mertens, S., Amorim-Vaz, S., Rai, L. S., d’Enfert, C., Pagni, M., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010012 · Cited by 63
“Among the most strongly downregulated genes in isolate 101 featured genes encoding adhesins and invasins, namely ALS1 and ALS3 (Phan et al., 2007; Sheppard et al., 2004), aspartyl proteases, namely SAP4, SAP6 and SAP8 linked to deep tissue invasion (Schaller et al., 2000), and the damage-inducing factor, namely ECE1 (…”
BackgroundInfluentialStructural correlates of antimicrobial efficacy in IL-8 and related human kinocidins.
Yount, N., Waring, A., Gank, K. D., Welch, W., Kupferwasser, D., & Yeaman, M. (2007) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2006.11.011 · Cited by 58
Self-citationMetabolic Adaptations During Staphylococcus aureus and Candida albicans Co-Infection
Eichelberger, K. R., & Cassat, J. E. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.797550 · Cited by 67
“aureus surface adhesins, such as collagen binding protein and clumping factor (116).”
BackgroundUppuluri, P., Lin, L., Alqarihi, A., Luo, G., Youssef, E. G., Alkhazraji, S., Yount, N. Y., Ibrahim, B. A., Bolaris, M. A., Edwards, J. E., et al. (2018) · PLOS Pathogens · doi:10.1371/journal.ppat.1007056 · Cited by 57
“aureus [42], there are relatively low degrees of sequence identity between Hyr1 and the identified template proteins.”
BackgroundSelf-citationNanoscale analysis of caspofungin-induced cell surface remodelling in Candida albicans
El-Kirat-Chatel, S., Beaussart, A., Alsteens, D., Jackson, D., Lipke, P., & Dufrêne, Y. (2012) · Nanoscale · doi:10.1039/c2nr33215a · Cited by 56
Aspergillus fumigatusInduces Immunoglobulin E–Independent Mast Cell Degranulation
Urb, M., Pouliot, P., Gravelat, F. N., Olivier, M., & Sheppard, D. C. (2009) · The Journal of Infectious Diseases · doi:10.1086/600070 · Cited by 58
Self-citationSilva, D. R., Sardi, J. D. C. O., Freires, I. A., da Silva, A. C. B., & Rosalen, P. L. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.10.016 · Cited by 70
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“The Als1 protein has been shown to be abundantly expressed in various candidiasis models, where it was able to bind to epithelial and endothelial cells (Fu et al., 2002; Kamai et al., 2002; Green et al., 2004; 2006; Sheppard et al., 2004; Cheng et al., 2005).”
BackgroundInfluentialIelasi, F., Alioscha‐Perez, M., Donohue, D. S., Claes, S., Hichem Sahli, B., Schols, D., & Willaert, R. (2016) · mBio · doi:10.1128/mbio.00584-16 · Cited by 63
“The binding of Als proteins to human epithelial tissues has been attributed to the N-terminal part of the protein, which contains tandem immunoglobulin-like domains that are able to adhere to host proteins (17, 18).”
BackgroundChang, 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
Disruption of the Phospholipase D Gene Attenuates the Virulence of Aspergillus fumigatus
Li, X., Gao, M., Han, X., Tao, S., Zheng, D., Cheng, Y., Yu, R., Han, G., Schmidt, M., & Han, L. (2011) · Infection and Immunity · doi:10.1128/iai.05830-11 · Cited by 53
“fumigatus to epithelial cells was determined as described previously (22, 60).”
MethodLee, E. Y., Chan, L. C., Wang, H., Lieng, J., Hung, M., Srinivasan, Y., Wang, J. P., Waschek, J. A., Ferguson, A. L., Lee, K., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917623117 · Cited by 61
Self-citationWiederhold, N., Najvar, L., Fothergill, A., McCarthy, D. I., Bocanegra, R., Olivo, M., Kirkpatrick, W., Everson, M., Duncanson, F., & Patterson, T. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03944-14 · Cited by 50
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“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
“cerevisiae becomes adherent to laminin when overexpressing ALS9 (Sheppard et al., 2004).”
BackgroundInfluentialKarkowska‐Kuleta, J., Kędracka–Krok, S., Rąpała‐Kozik, M., Kamysz, W., Bielińska, S., Karafová, A., & Kozik, A. (2011) · Peptides · doi:10.1016/j.peptides.2011.10.021 · Cited by 50
Is a vaccine needed against Candida albicans?
Mochon, A. B., & Cutler, J. (2005) · Medical Mycology · doi:10.1080/13693780500035979 · Cited by 47
Natural product solasodine-3-O-β-D-glucopyranoside inhibits the virulence factors ofCandida albicans
Li, Y., Chang, W., Zhang, M., Zhao, Y. H., & Lou, H. (2015) · FEMS Yeast Research · doi:10.1093/femsyr/fov060 · Cited by 44
“These include members of the agglutin-like (Als) family of adhesins such as Als3 (Sheppard et al. 2004), hyphal wall protein 1 (Hwp1) (Staab et al. 1999) and enhance adherence to polystyrene protein 1 (Eap1) (Li and Palecek 2003).”
BackgroundSelf-citationHuman serum inhibits adhesion and biofilm formation in Candida albicans
Ding, X., Liu, Z., Su, J., & Yan, D. (2014) · BMC Microbiology · doi:10.1186/1471-2180-14-80 · Cited by 50
“Most Als proteins have adhesin functions [34,35].”
Candida Biofilms: Is Adhesion Sexy?
Soll, D. R. (2008) · Current Biology · doi:10.1016/j.cub.2008.07.014 · Cited by 43
Fungal cell wall vaccines: an update
Edwards, J. E. (2012) · Journal of Medical Microbiology · doi:10.1099/jmm.0.041665-0 · Cited by 68
“albicans to human cells, we performed molecular modelling of all the Als proteins (Sheppard et al., 2004).”
BackgroundMethodCandida albicans virulence and drug-resistance requires the O-acyltransferase Gup1p
Ferreira, C., Silva, S. M., Faria‐Oliveira, F., Pinho, E., Henriques, M., & Lucas, C. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-238 · Cited by 43
“Additionally, several other factors have been described in association with virulence, including the production of proteins that mediate adherence, the colonization and invasion of host tissues, the maintenance of cell wall integrity, phenotypic switching, and the avoidance of the host immune response [12-18].”
BackgroundIs Candida albicans a contributor to cancer? A critical review based on the current evidence
Wang, X., Zhang, W., Wu, W., Wu, S., Young, A., & Yan, Z. (2023) · Microbiological Research · doi:10.1016/j.micres.2023.127370 · Cited by 44
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“[31], but it has only begun to be addressed in other pathogenic fungi.”
BackgroundRole of Endothelial Cell Septin 7 in the Endocytosis of Candida albicans
Phan, Q. T., Eng, D. K.-M., Mostowy, S., Park, H., Cossart, P., & Filler, S. G. (2013) · mBio · doi:10.1128/mbio.00542-13 · Cited by 44
“Both of these strains are avidly endocytosed by endothelial cells (19, 20).”
BackgroundSelf-citationThe molecular basis of sex: linking yeast to human.
Swanson, W., Aagaard, J., Vacquier, V., Monné, M., Hosseini, H. S. A., & Jovine, L. (2011) · Molecular biology and evolution · doi:10.1093/molbev/msr026 · Cited by 42
“Moreover, specific adherence of Candida to human endothelial and epithelial cells requires Als1p Ig III amino acids centered around V285 (Fu et al. 1998; Loza et al. 2004; Sheppard et al. 2004; Dranginis et al. 2007), a residue that is also predicted to be exposed on the same region of the ZP-N domain (fig.”
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“2003a,b; Li and Palecek 2003), many of which are thought to mediate adhesion to host epithelial and endothelial cells as well as to extracellular matrix proteins (Hoyer 2001; Li and Palecek 2003; Sheppard et al. 2004; Klotz et al. 2004; Hoyer et al. 2008).”
BackgroundCandida albicans Adhesins Als1 and Hwp1 Modulate Interactions with Streptococcus mutans
Martorano-Fernandes, L., Goodwine, J. S., Ricomini-Filho, A. P., Nobile, C. J., & Cury, A. A. D. B. (2023) · Microorganisms · doi:10.3390/microorganisms11061391 · Cited by 42
“Als3 is a GPI-anchored adhesin with 88% amino acid sequence similarity to Als1 [32] that is involved in C.”
BackgroundOpportunistic yeast pathogen Candida spp.: Secreted and membrane-bound virulence factors
Lim, S. J., Ali, M. S. M., Sabri, S., Noor, N. D. M., Salleh, A. B., & Oslan, S. N. (2021) · Medical Mycology · doi:10.1093/mmy/myab053 · Cited by 43
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“albicans Als3 are avidly endocytosed by endothelial cells in vitro (3, 7).”
BackgroundSelf-citationMicrobial cell surface proteins and secreted metabolites involved in multispecies biofilms
Demuyser, L., Jabra‐Rizk, M. A., & Dijck, P. V. (2013) · Pathogens and Disease · doi:10.1111/2049-632x.12123 · Cited by 36
Goossens, K. V. Y., & Willaert, R. (2012) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2011.00766.x · Cited by 37
“, 2001); the N-terminal part of Als1p from Candida albicans interacts with extracellular matrix proteins, epithelial and endothelial cells (Loza et al., 2004; Sheppard et al., 2004; Donohue et al., 2011).”
BackgroundLachat, J., Pascault, A., Thibaut, D., Borgne, R. L., Verbavatz, J., & Weiner, A. (2022) · Nature Communications · doi:10.1038/s41467-022-31237-z · Cited by 44
Lagree, K., & Mitchell, A. P. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.funk-0024-2016 · Cited by 41
“Mutants defective in expression of ALS1 and ALS3 have decreased adherence to host and abiotic substrates (68, 93, 111).”
BackgroundKarkowska‐Kuleta, J., Wronowska, E., Satała, D., Zawrotniak, M., Braś, G., Kozik, A., Nobbs, A. H., & Rąpała‐Kozik, M. (2020) · Cellular Microbiology · doi:10.1111/cmi.13297 · Cited by 35
“These proteins are glycosylphosphatidylinositol (GPI) linked to β-1,6-glucans of the fungal cell wall (Gaur & Klotz, 1997; Hoyer, 2001; Sheppard et al., 2004); some are preferentially expressed by germ tubes and hyphae (Als1–4), and others by yeastlike cells (Als5–7, Als9) (Modrzewska &…”
BackgroundMonniot, C., Boisramé, A., Costa, G. D., Chauvel, M., Sautour, M., Bougnoux, M., Bellon‐Fontaine, M., Dalle, F., d’Enfert, C., & Richard, M. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082395 · Cited by 41
“Expression of ALS3 in a Saccharomyces cerevisiae surface display system allowed attachment of the recombinant strain to epithelial cells, endothelial cells and extracellular matrix proteins [12] as well as to polystyrene [13].”
BackgroundLaforce‐Nesbitt, S. S., Sullivan, M. A., Hoyer, L. L., & Bliss, J. M. (2008) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2008.00465.x · Cited by 31
“, 1996), or its derivatives that provide constitutive expression of ALS1 or ALS3 (Sheppard et al., 2004) were generously provided by Scott Filler and were grown in yeast nitrogen base broth (Difco) supplemented with 2% glucose and yeast synthetic drop-out medium supplement without uracil (Sigma) at 30 1C.”
Short, B., Delaney, C., McKloud, E., Brown, J. L., Kean, R., Litherland, G. J., Williams, C., Martin, L., Mackay, W. G., & Ramage, G. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.791523 · Cited by 32
“These Candida-bacteria interactions may be reciprocal, as it has been reported that C. albicans Als3 shares over 80% homology with S. aureus collagen binding factor (Sheppard et al., 2004).”
BackgroundComprehensive genetic analysis of adhesin proteins and their role in virulence ofCandida albicans
Rosiana, S., Zhang, L., Kim, G. H., Revtovich, A. V., Uthayakumar, D., Sukumaran, A., Geddes‐McAlister, J., Kirienko, N. V., & Shapiro, R. S. (2021) · Genetics · doi:10.1093/genetics/iyab003 · Cited by 41
The vaccines and antibodies associated with Als3p for treatment of Candida albicans infections
Sui, X., Yan, L., & Jiang, Y. (2017) · Vaccine · doi:10.1016/j.vaccine.2017.08.082 · Cited by 38
Neonatal Candidiasis: New Insights into an Old Problem at a Unique Host-Pathogen Interface
Arsenault, A. B., & Bliss, J. M. (2015) · Current Fungal Infection Reports · doi:10.1007/s12281-015-0238-x · Cited by 41
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“HYPOTHESIS AND THEORY ARTICLE published: 04 November 2014 doi: 10.3389/fmicb.2014.00564”
InfluentialRole of Force-Sensitive Amyloid-Like Interactions in Fungal Catch Bonding and Biofilms
Chan, C. X. J., & Lipke, P. (2014) · Eukaryotic Cell · doi:10.1128/ec.00068-14 · Cited by 31
“albicans expresses many adhesins, so it is difficult to attribute a specific behavior to any specific cell surface component (21, 23, 24).”
BackgroundMartínez-Duncker, I., Díaz-Jiménez, D. F., & Mora-Montes, H. M. (2014) · International Journal of Microbiology · doi:10.1155/2014/267497 · Cited by 30
“Adhesins of the Als family are known to be GPI-proteins [140], so it is not surprising that virulence is attenuated in GPI mutants.”
BackgroundMoonlighting proteins in medically relevant fungi
Arvizu-Rubio, V., García-Carnero, L. C., & Mora-Montes, H. M. (2022) · PeerJ · doi:10.7717/peerj.14001 · Cited by 33
“Als3 has a canonical function of adhesin and invasin that binds to gelatin, fibronectin, fibrinogen, type IV collagen, laminin, salivary pellicle, and E- and N-cadherin, thus mediating adherence and internalization to endothelial and epithelial cells (Sheppard et al., 2004; Phan et al., 2007; Nobbs, Vickerman & Jenkin…”
BackgroundPadovan, A. C. B., Chaves, G. M., Colombo, A. L., & Briones, M. R. S. (2009) · Medical Mycology · doi:10.3109/13693780802669574 · Cited by 28
An Amyloid Core Sequence in the Major Candida albicans Adhesin Als1p Mediates Cell-Cell Adhesion
Ho, V., Herman‐Bausier, P., Shaw, C. E., Conrad, K. A., Garcia, M. C., Draghi, J. A., Dufrêne, Y. F., Lipke, P. N., & Rauceo, J. M. (2019) · mBio · doi:10.1128/mbio.01766-19 · Cited by 37
“albicans adhesion, including binding to human epithelial and endothelial cells and abiotic surfaces such as silicone and plastic (6, 8, 9).”
Identification of Candida albicans regulatory genes governing mucosal infection
Meir, J., Hartmann, E., Eckstein, M., Guiducci, E., Kirchner, F., Rosenwald, A., LeibundGut‐Landmann, S., & Pérez, J. C. (2018) · Cellular Microbiology · doi:10.1111/cmi.12841 · Cited by 28
“In fact, several proteins on the surface of the fungus have been shown to mediate attachment to oral epithelial cells (Fu et al., 2013; Lopez, Wallich, Riesbeck, Skerka, & Zipfel, 2014; Sheppard et al., 2004; Staab et al., 1999).”
BackgroundAdhesins in Opportunistic Fungal Pathogens
Zordan, R. E., & Cormack, B. P. (2014) · ASM Press eBooks · doi:10.1128/9781555817176.ch16 · Cited by 24
Evolutionary Overview of Molecular Interactions and Enzymatic Activities in the Yeast Cell Walls
Teparić, R., Lozančić, M., & Mrša, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238996 · Cited by 28
“Als1 and Als10/Als2 were shown to be involved in epithelial adhesion and invasiveness due to their adhesion properties [81].”
BackgroundSeweryn, K., Karkowska‐Kuleta, J., Wolak, N., Bocheńska, O., Kędracka–Krok, S., Kozik, A., & Rąpała‐Kozik, M. (2015) · Acta Biochimica Polonica · doi:10.18388/abp.2015_1142 · Cited by 34
“The involvement of Als proteins in the contact factorbinding is consistent with the universal, major role of these proteins in the fungus-host adhesion (Sheppard et al., 2004).”
BackgroundApplying Convergent Immunity to Innovative Vaccines Targeting Staphylococcus aureus
Yeaman, M. R., Filler, S. G., Schmidt, C. S., Ibrahim, A. S., Edwards, J. E., & Hennessey, J. P. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00463 · Cited by 24
“aureus MSCRAMMS considered virulence factors, including clumping factor A (ClfA) (Figures 2 and 3; Table 4) (139).”
BackgroundInfluentialSelf-citationPeptide Detection of Fungal Functional Amyloids in Infected Tissue
Garcia, M. C., Lysak, N., Filonenko, A., Richards, H., Sobonya, R. E., Klotz, S. A., & Lipke, P. N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086067 · Cited by 29
“Among the adhesins, the Agglutininlike sequence (Als) family includes cell wall-linked glycoproteins encoded at 8 loci [29,30].”
BackgroundFehrmann, C., Jurk, K., Bertling, A., Seidel, G., Fegeler, W., Kehrel, B. E., Peters, G., Becker, K., & Heilmann, C. (2013) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2013.02.011 · Cited by 26
“genes of the ALS (agglutinin-like sequence) gene family (O’Connor et al., 2005; Sheppard et al., 2004) as well as the adhesin genes HWP1 (Staab et al.”
BackgroundInteraction of human fibronectin with Candida glabrata epithelial adhesin 6 (Epa6)
Zajac, D., Karkowska-Kuleta, J., Bochenska, O., Rapala-Kozik, M., & Kozik, A. (2016) · Acta Biochimica Polonica · doi:10.18388/abp.2016_1328 · Cited by 26
“…Flo proteins and the members of the C. albicans Als family of typical adhesins that comprise three regions: a C-terminal domain with a GPI-anchor, a central domain with a heavily glycosylated Ser/Thr-rich region, and an N-terminal domain required for ligand recognition (Sheppard et al., 2004).”
BackgroundMechanisms of NDV-3 vaccine efficacy in MRSA skin versus invasive infection
Yeaman, M. R., Filler, S. G., Chaili, S., Barr, K., Wang, H., Kupferwasser, D., Hennessey, J. P., Fu, Y., Schmidt, C. S., Edwards, J. E., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415610111 · Cited by 75
Self-citationCandidaantigens and immune responses: implications for a vaccine
Moragues, M. D., Rementerı́a, A., Sevilla, M. J., Eraso, E., & Quindós, G. (2014) · Expert Review of Vaccines · doi:10.1586/14760584.2014.932253 · Cited by 28
Biochemistry of Beer Fermentation
Willaert, R. (2012) · doi:10.1002/9781118308035.ch33 · Cited by 26
Promising immunotherapeutic targets for treating candidiasis
Feng, Z. C., Lu, H., & Jiang, Y. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1339501 · Cited by 28
“…that demonstrates a wide range of substrates for adhesion, including human fi bronectin, laminin, collagen, gp96, EGFR (epidermal growth factor receptor), HER2 (human epidermal growth factor receptor-2), N-cadherin, E-cadherin, fi brinogen, casein, and bovine serum albumin (Sheppard et al., 2004).”
BackgroundSticking to the Subject: Multifunctionality in Microbial Adhesins
Lipke, P. N., & Ragonis‐Bachar, P. (2023) · Journal of Fungi · doi:10.3390/jof9040419 · Cited by 28
“The N-terminal region Ig-like domains region of Als adhesins are structurally similar to the Ig-like domains of MSCRAMMs and Als3 (Figure 8) [48,72,80,95].”
BackgroundKarkowska‐Kuleta, J., Smolarz, M., Seweryn-Ozog, K., Satała, D., Zawrotniak, M., Wronowska, E., Bocheńska, O., Kozik, A., Nobbs, A. H., Gogól, M., et al. (2021) · Cells · doi:10.3390/cells10102736 · Cited by 31
“albicans’ adhesive properties [71,72], with the largest contribution in the adhesion to human cells [73],”
BackgroundNeale, M. N., Glass, K. A., Longley, S. J., Kim, D. J., Laforce‐Nesbitt, S. S., Wortzel, J. D., Shaw, S. K., & Bliss, J. M. (2018) · Infection and Immunity · doi:10.1128/iai.00892-17 · Cited by 27
Rąpała‐Kozik, M., Surowiec, M., Juszczak, M., Wronowska, E., Kulig, K., Bednarek, A., Gonzalez‐Gonzalez, M., Karkowska‐Kuleta, J., Zawrotniak, M., Satała, D., et al. (2023) · Yeast · doi:10.1002/yea.3855 · Cited by 24
“A representative— Als3—also participates in iron acquisition by ferritin binding (Sheppard et al., 2004; Wilson et al., 2016).”
Youssef, E. G., Alkhazraji, S., Ghebremariam, T., Zhang, L., Singh, S., Yount, N. Y., Yeaman, M. R., Uppuluri, P., & Ibrahim, A. S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00076 · Cited by 25
Self-citationMillar, E. V., Bennett, J. W., Barin, B., Carey, P. M., Law, N. N., English, C. E., Schwartz, M. M., Cochrane, T., Ellis, M. W., Tribble, D. R., et al. (2021) · Vaccine · doi:10.1016/j.vaccine.2021.04.031 · Cited by 24
Wiederhold, N. P., & Patterson, T. F. (2015) · Current Opinion in Infectious Diseases · doi:10.1097/qco.0000000000000203 · Cited by 16
Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion
Lipke, P., Ramsook, C. B., Garcia-Sherman, M. C., Jackson, D., Chan, C. X. J., Bois, M., & Klotz, S. (2014) · New Journal of Science · doi:10.1155/2014/815102 · Cited by 22
Hernández, R., & Rupp, S. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-204-5_10 · Cited by 21
Coding fungal tandem repeats as generators of fungal diversity
Levdansky, E., Sharon, H., & Osherov, N. (2008) · Fungal Biology Reviews · doi:10.1016/j.fbr.2008.08.001 · Cited by 22
A novel flow cytometric protocol for assessment of yeast cell adhesion
Silva‐Dias, A., Miranda, I. M., Rocha, R., Monteiro‐Soares, M., Salvador, A., Rodrigues, A. G., & Pina‐Vaz, C. (2012) · Cytometry Part A · doi:10.1002/cyto.a.21170 · Cited by 19
“(11) using the six-well plate assay method.”
BackgroundMethodResultInfluentialIslam, A., Tebbji, F., Mallick, J., Regan, H., Dumeaux, V., Omran, R. P., & Whiteway, M. (2018) · Genetics · doi:10.1534/genetics.118.301769 · Cited by 19
Tamm-Horsfall Protein Protects the Urinary Tract against Candida albicans
Coady, A. M., Ramos, A. R., Olson, J., Nizet, V., & Patras, K. A. (2018) · Infection and Immunity · doi:10.1128/iai.00451-18 · Cited by 19
Overview on the Fungal Metabolites Involved in Mycopathy
Al-Fakih, A. (2014) · Open Journal of Medical Microbiology · doi:10.4236/ojmm.2014.41006 · Cited by 19
“albicans has flexibility and adaptability and can invade different environments in the host [247].”
BackgroundEfg1 and Cas5 Orchestrate Cell Wall Damage Response to Caspofungin in Candida albicans
Xiong, K., Su, C., Sun, Q., & Lü, Y. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01584-20 · Cited by 19
To Repeat or Not to Repeat: Repetitive Sequences Regulate Genome Stability in Candida albicans
Dunn, M., & Anderson, M. Z. (2019) · Genes · doi:10.3390/genes10110866 · Cited by 16
Ahmad, M. F., Yadav, B., Kumar, P., Puri, A., Mazumder, M., Ali, A., Gourinath, S., Muthuswami, R., & Komath, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035305 · Cited by 16
“The protein has also been shown to be capable of mediating endothelial cell invasion and its N-terminal domain has been shown to be important for adherence [10,11].”
BackgroundTropic Orientation Responses of Pathogenic Fungi
Brand, A., & Gow, N. (2012) · Topics in current genetics · doi:10.1007/978-3-642-22916-9_2 · Cited by 16
“…adhesion profiles were identified for individual Als proteins, suggesting that this gene family contributes significantly to the predicted overall heterogeneity of surface adhesive molecules in C. albicans (Hoyer and Hecht 2001; Sheppard et al. 2004; Hoyer et al. 2008; Liu and Filler 2011).”
BackgroundPotential of Polyethyleneimine as an Adjuvant To Prepare Long-Term and Potent Antifungal Nanovaccine
Jin, Z., Dong, Y., Liu, S., Liu, J., Qiu, X.-R., Zhang, Y., Zong, H., Hou, W.-T., Guo, S.-Y., Sun, Y.-F., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.843684 · Cited by 15
“albicans, which is one of the most promising vaccine strategies ever tested (40, 41).”
BackgroundLipke, P., Mathelié-Guinlet, M., Viljoen, A., & Dufrêne, Y. (2021) · Pathogens · doi:10.3390/pathogens10081013 · Cited by 15
Yeast Nanometric Scale Oscillations Highlights Fibronectin Induced Changes in C. albicans
Kohler, A., Venturelli, L., Kannan, A., Sanglard, D., Dietler, G., Willaert, R., & Kasas, S. (2020) · Fermentation · doi:10.3390/fermentation6010028 · Cited by 15
Staphylococcus aureus in Atopic Dermatitis: Past, Present, and Future
Hwang, J., Jaros, J., & Shi, V. Y. (2020) · Dermatitis · doi:10.1097/der.0000000000000589 · Cited by 18
“NDV-3 is another potential vaccine whose main antigen is agglutinin-like sequence 3 protein, a cell surface protein extracted from Candida albicans that has structural homology with cell surface proteins in SA; it is being studied in healthy military recruits at increased risk of SA infection with a primary end point…”
BackgroundDoes Candida albicans Als5p Amyloid Play a Role in Commensalism in Caenorhabditis elegans?
Bois, M., Singh, S., Samlalsingh, A., Lipke, P., & Garcia, M. C. (2013) · Eukaryotic Cell · doi:10.1128/ec.00020-13 · Cited by 14
“When transgenically expressed in Saccharomyces cerevisiae, Als5p mediates fungal aggregation and also causes adherence to laminin, gelatin, fibronectin, and epithelial cells, as well as endothelial cells in vitro (5, 6).”
BackgroundMoazeni, M., Khorramizadeh, M. R., Teimoori‐Toolabi, L., Noorbakhsh, F., Fallahi, A. A., & Rezaie, S. (1996) · Europe PMC (PubMed Central) · doi:10.6091/ibj.1093.2012 · Cited by 11
“This function can be leaded to produce biofilm, which is a kind of specialized form of adherence [11, 12].”
BackgroundVandermeulen, M. D., & Cullen, P. J. (2020) · Genetics · doi:10.1534/genetics.120.303369 · Cited by 18
“Given the large number of adhesion molecules in C. albicans and other species (Tronchin et al. 1991; Brandhorst et al. 1999; Sheppard et al. 2004; Dranginis et al. 2007; Linder and Gustafsson 2008; Younes et al. 2011; de Groot et al. 2013; Lipke 2018; Takahashi-Nakaguchi et al. 2018), it is likely…”
BackgroundMillar, E. V., Schlett, C. D., Law, N. N., Whitman, T., Ellis, M. W., Tribble, D., & Bennett, L. (2019) · Military Medicine · doi:10.1093/milmed/usz105 · Cited by 13
“aureus infection.(36) Prevention of SSTIs among Military Personnel”
BackgroundThe Cell Wall: Glycoproteins, Remodeling, and Regulation
Munro, C. A., & Richard, M. L. (2014) · ASM Press eBooks · doi:10.1128/9781555817176.ch14 · Cited by 13
Candida albicans Cell Wall Mediated Virulence
Munro, C. A. (2009) · Springer eBooks · doi:10.1007/978-3-642-03150-2_4 · Cited by 9
Wendland, J., Hellwig, D., Walther, A., Sickinger, S., Shadkchan, Y., Martin, R., Bauer, J., Osherov, N., Tretyakov, A. N., & Saluz, H. (2006) · Journal of Basic Microbiology · doi:10.1002/jobm.200610167 · Cited by 11
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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