Cross-Species Comparative Analysis of Plant Expansin Allergens: Sequence, Structure, and Allergenicity Perspectives
DOI:
https://doi.org/10.31305/rrijm.2022.v07.i10.026Keywords:
Expansin, Allergens, in silico, epitope, prediction, hydrophilicAbstract
Plant-derived proteins represent a major source of allergens, contributing to respiratory, cutaneous, and food-related allergic disorders worldwide. While grass and tree pollen allergens are well recognized, emerging evidence indicates that expansins, a family of cell wall–loosening proteins, may also exhibit allergenic properties. In this study, expansin sequences from Zea mays, Oryza sativa, Arabidopsis thaliana and Paspalum notatum were subjected to in silico characterization to assess their allergenic potential. Multiple sequence alignment revealed conserved glycine residues. Expansins were classified within the DPBB_RlpA_EXP_N–like superfamily, associated with cell wall metabolism. Immunoinformatics predicted B-cell epitopes with scores > 0.500, supporting their potential allergenicity. Physicochemical analyses showed expansins to be stable (instability index < 40), moderately variable in isoelectric points (pI 3–10), and hydrophilic (negative GRAVY values). Collectively, these findings highlight expansins as structurally conserved proteins with probable allergenic potential, underscoring the need for experimental validation and consideration in allergy diagnostics and management.
References
Artimo, P., Jonnalagedda, M., Arnold, K., Baratin, D., Csardi, G., de Castro, E., Duvaud, S., Flegel, V., Fortier, A., Gasteiger, E., Grosdidier, A., Hernandez, C., Ioannidis, V., Kuznetsov, D., Liechti, R., Moretti, S., Mostaguir, K., Redaschi, N., Rossier, G., … Stockinger, H. (2012). ExPASy: SIB bioinformatics resource portal. Nucleic Acids Research, 40(Web Server issue), W597–W603. https://doi.org/10.1093/nar/gks400
Cosgrove, D. J. (2015). Plant expansins: diversity and interactions with plant cell walls. Current Opinion in Plant Biology, 25, 162–172. https://doi.org/10.1016/j.pbi.2015.05.014.
Cosgrove, D. J. (2022). Expansin research in plant biology: a historical overview. Plant Physiology, 188(1), 1–13. https://doi.org/10.1093/plphys/kiab463
Dimitrov, I., Bangov, I., Flower, D. R., & Doytchinova, I. (2014). AllerTOP v.2—a server for in silico prediction of allergens. Journal of Molecular Modeling, 20(6), 2278. https://doi.org/10.1007/s00894-014-2278-5
Georgelis, N., Cosgrove, D. J., & Dellaporta, S. L. (2015). The expansin superfamily. Plant Physiology, 169(2), 738–749. https://doi.org/10.1104/pp.15.00946
Grobe, K., Pöppelmann, M., Becker, W. M., & Petersen, A. (1999). Grass group I allergens (β-expansins): An extended family of proteins with homology to bacterial expansins. FEBS Letters, 458(3), 357–361. https://doi.org/10.1016/S0014-5793(99)01155-6
Hepler, P. K., Winship, L. J., & Vidali, L. (2019). Expansin action in plant cell walls: a biophysical perspective. Journal of Experimental Botany, 70(15), 3617–3626. https://doi.org/10.1093/jxb/erz226
Knox, R. B., & Suphioglu, C. (1996). Grass pollen allergens: the role of group I allergens in allergy. Clinical & Experimental Allergy, 26(6), 657–662. https://doi.org/10.1111/j.1365-2222.1996.tb00595.x
Li, J., Schäppi, G. F., Wallner, M., Briza, P., Wagner, B., Obermeyer, G., & Ferreira, F. (2001). Sequence polymorphisms in major pollen allergens of rye grass (Lolium perenne): Implications for diagnosis and therapy. Journal of Allergy and Clinical Immunology, 107(5), 925–930. https://doi.org/10.1067/mai.2001.115645
Lu, S., Wang, J., Chitsaz, F., Derbyshire, M. K., Geer, R. C., Gonzales, N. R., Gwadz, M., Hurwitz, D. I., Marchler, G. H., Song, J. S., Thanki, N., Yamashita, R. A., Yang, M., Zhang, D., Zheng, C., Lanczycki, C. J., & Marchler-Bauer, A. (2020). CDD/SPARCLE: the conserved domain database in 2020. Nucleic Acids Research, 48(D1), D265–D268. https://doi.org/10.1093/nar/gkz991
Salcedo, G., Sanchez-Monge, R., Diaz-Perales, A., Garcia-Casado, G., & Barber, D. (2004). Plant non-specific lipid transfer proteins and food allergy. Clinical & Experimental Allergy, 34(4), 564–570. https://doi.org/10.1111/j.1365-2222.2004.01973.x
Sievers, F., & Higgins, D. G. (2014). Clustal Omega, accurate alignment of very large numbers of sequences. Methods in Molecular Biology, 1079, 105–116. https://doi.org/10.1007/978-1-62703-646-7_6
The UniProt Consortium. (2015). UniProt: a hub for protein information. Nucleic Acids Research, 43(Database issue), D204–D212. https://doi.org/10.1093/nar/gku989
Tovar-Herrera, O. E., Batista-García, R. A., Anducho-Reyes, M. A., Arévalo-Niño, K., Balcázar-López, E., Sánchez-Carbente, M. D. R., Folch-Mallol, J. L., & Martínez-Anaya, C. (2018). Expansin-like Exlx1 from Bacillus subtilis binds cellulose and enhances cell growth and biomass yield in cellulolytic bacteria. Applied and Environmental Microbiology, 84(18), e00239-18. https://doi.org/10.1128/AEM.00239-18
Valenta, R., Twaroch, T., & Swoboda, I. (2010). The recombinant allergen-based concept of component-resolved diagnostics and immunotherapy (CRD and CRIT). Clinical & Experimental Allergy, 40(9), 1429–1440. https://doi.org/10.1111/j.1365-2222.2010.03571.
Vita, R., Mahajan, S., Overton, J. A., Dhanda, S. K., Martini, S., Cantrell, J. R., Wheeler, D. K., Sette, A., & Peters, B. (2019). The Immune Epitope Database (IEDB): 2018 update. Nucleic Acids Research, 47(D1), D339–D343. https://doi.org/10.1093/nar/gky1006.
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