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Currrent Issue: Volume 4, Number 2, 2016


Characterization of Pollen Specific Proteins SF3 and SF21 from Sunflower (Helianthus annuus L.) for the Allergenicity Potential

1Department of Science and Laboratory Technology, Dar es Salaam Institute of Technology, P. O. Box 2958, Dar es Salaam, Tanzania

American Journal of Medical and Biological Research. 2016, 4(2), 13-19
doi: 10.12691/ajmbr-4-2-1
Copyright © 2016 Science and Education Publishing

Cite this paper:
Ezekiel Amri. Characterization of Pollen Specific Proteins SF3 and SF21 from Sunflower (Helianthus annuus L.) for the Allergenicity Potential. American Journal of Medical and Biological Research. 2016; 4(2):13-19. doi: 10.12691/ajmbr-4-2-1.

Correspondence to: Ezekiel  Amri, Department of Science and Laboratory Technology, Dar es Salaam Institute of Technology, P. O. Box 2958, Dar es Salaam, Tanzania. Email:


Pollen from different type of plants carry different proteins that are more likely to become allergenic than others. In this study pollen specific proteins SF3 and SF21 from Sunflower (Helianthus annuus) were in-silico characterized for allergenicity potential. Bioinformatics allergen prediction tools were employed for prediction of SF3 and SF21 as candidate allergens. The phylogenetic relationship between the pollen specific proteins and protein allergens of Asteraceae family was also analyzed to unveil their similarity. The results by Bepipred Linear Epitope prediction demonstrated a good number of epitopes in pollen specific protein SF3 and SF21 signifying that both are potential allergens. However, further analysis through ConSurf revealed the presence of allergen-specific patches with remarkably higher proportion of surface-exposed hydrophobic residue in SF3 than SF21. Further prediction by AlgPred and ProAp methods with Support Vector Machines (SVMs) revealed that only SF3 contained IgE epitope thus confirming it as a potential allergen. The phylogenetic analysis revealed a close identity of SF3 with the major allergen of Ambrosia artemisiifolia pollen, Amb a 3. The study has demonstrated high allergenic activity of SF3 protein with shared similarity with the pollen protein allergens of Asteraceae family. This study forms a basis in predicting cross-reactivity of pollen specific proteins, designing of therapeutic procedures and evaluating the allergenic potential of novel proteins.



[1]  Furmonaviciene, R., Sutton, B. J., Glaser, F., Laughton, C. A., Jones, N., Sewell, H. F., and Shakib, F. (2005). An attempt to define allergen-specific molecular surface features: a bioinformatic approach. Bioinformatics, 21(23): 4201-4204.
[2]  Songnuan, W. (2013). Wind-pollination and the roles of pollen allergenic proteins. Asian Pac J Allergy Immunol, 31:261-270.
[3]  Radauer, C. and Breiteneder, H. (2006). Pollen allergens are restricted to few protein families and show distinct patterns of species distribution. Journal of Allergy and Clinical Immunology, 117(1): 141-147.
[4]  Skjoth, C.A., Sommer, J., Stach, A., Smith, M., Brandt, J. (2007). The long-range transport of birch (Betula) pollen from Poland and Germany causes significant pre-season concentrations in Denmark. Clin Exp Allergy, 37:1204-1212.
[5]  Taketomi, E.A., Sopelete, M.C., Moreira, P.F.D.S. and Vieira, F.D.A.M. (2006). Pollen allergic disease: pollens and its major allergens. Revista Brasileira de Otorrinolaringologia, 72(4): 562-567.
Show More References
[6]  Bousquet, P.J., Bachert, C., Canonica, G.W., Casale, T.B., Mullol, J., Klossek, J.M., Zuberbier, T., and Bousquet, J. (2010) Uncontrolled allergic rhinitis during treatment and its impact on quality of life: acluster randomized trial. J Allergy Clin Immunol 126(3): 666-668.
[7]  Asam, C., Hofer, H., Wolf, M., Aglas, L., and Wallner, M. (2015). Tree pollen allergens—an update from a molecular perspective. Allergy, 70(10): 1201-1211.
[8]  Baltz, R., Schmit, A.-C., Kohnen, M., Hentges, F. and Steinmetz, A. (1999). Differential localization of the LIM domain protein PLIM-1 in microspores and mature pollen grains from sunflower, Sex. Plant Reprod., 12: 60-65.
[9]  Kräuter-Canham, R., Bronner, R., and Steinmetz, A. (2001). SF21 is a protein which exhibits a dual nuclear and cytoplasmic localization in developing pistils of sunflower and tobacco. Annals of Botany, 87(2): 241-249.
[10]  Lundberg, J. (2009). Asteraceae and relationships within Asterales. Systematics, evolution, and biogeography of Compositae, 157-169.
[11]  Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A. (2005). Protein Identification and Analysis Tools on the ExPASy Server; (In) John M. Walker (ed): The Proteomics Protocols Handbook, Humana Press. pp. 571-607
[12]  Larsen, J.E.P., Lund, O. and Nielsen, M. (2006). Improved method for predicting linear B-cell epitopes. Immunome research, 2(1): 1.
[13]  Berezin, C., Glaser, F., Rosenberg, J., Paz, I., Pupko, T., Fariselli, P and Ben-Tal, N. (2004). ConSeq: the identification of functionally and structurally important residues in protein sequences. Bioinformatics, 20(8): 1322-1324.
[14]  Saha, S., Raghava ,G.V (2006). AlgPred: prediction of allergenic proteins and mapping of IgE epitopes. Nucleic Acids Research 34(2):W202-W209
[15]  Wang, J., Yu, Y., Zhao, Y., Zhang, D., and Li, J. (2013). Evaluation and integration of existing methods for computational prediction of allergens. BMC bioinformatics, 14(Suppl 4), S1.
[16]  Singh, S., Taneja, B., Salvi, S. S., and Agrawal, A. (2009). Physical properties of intact proteins may predict allergenicity or lack thereof. PloS one, 4(7): e6273.
[17]  Shakushiro, K., Yamasaki, Y., Nishikawa, M. and Takakura, Y. (2004). Efficient scavenger receptor-mediated uptake and cross-presentation of negatively charged soluble antigens by dendritic cells. Immunology 112: 211-218.
[18]  Bowyer, P., Fraczek, M., and Denning, D.W. (2006). Comparative genomics of fungal allergens and epitopes shows widespread distribution of closely related allergen and epitope orthologues. BMC genomics, 7(1): 251.
[19]  Pomés, A. (2009). Relevant B cell epitopes in allergic disease. International archives of allergy and immunology, 152(1): 1-11
[20]  Meno, K. H. (2011). Allergen structures and epitopes. Allergy, 66(95):19-21.
[21]  Seong, S.Y. and Matzinger, P. (2004) Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses. Nat. Rev. Immunol., 4:469-478.
[22]  Glaser, A. G., Menz, G., Kirsch, A. I., Zeller, S., Crameri, R., and Rhyner, C. (2008). Auto‐and cross‐reactivity to thioredoxin allergens in allergic bronchopulmonary aspergillosis. Allergy, 63(12): 1617-1623.
[23]  Oezguen, N., Zhou, B., Negi, S.S., Ivanciuc, O., Schein, C.H., Labesse, G., and Braun, W. (2008). Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes. Molecular immunology, 45(14): 3740-3747.
[24]  Kumar, H.G.A. and Venkatesh, Y.P. (2014). In silico analyses of structural and allergenicity features of sapodilla (Manilkara zapota) acidic thaumatin-like protein in comparison with allergenic plant TLPs. Molecular immunology, 57(2): 119-128.
[25]  Sharma, R., Singh, A.K., and Umashankar, V. (2009). Characterization of allergenic epitopes of Ory s1 protein from Oryza sativa and its homologs. Bioinformation, 4(1): 12-18.
[26]  Huby, R.D., Dearman, R.J., and Kimber, I. (2000). Why are some proteins allergens?. Toxicol. Sci., 55:235-246.
[27]  Umetsu, D. T., Akbari, O., DeKruyff, R.H., Shearer, W.T., Rosenwasser, L. J., and Bochner, B.S. (2003). Regulatory T cells control the development of allergic disease and asthma. Journal of Allergy and Clinical Immunology, 112(3): 480-487.
[28]  Dimitrov, I., Naneva, L., Doytchinova, I., and Bangov, I. (2014). AllergenFP: allergenicity prediction by descriptor fingerprints. Bioinformatics, 30(6): 846-851.
[29]  FAO/WHO, (2003): Evaluation of allergenicity of Genetically Modified Foods. Report of a Joint FAO/WHO Expert Consultation on Allergenicity of Foods Derived from Biotechnology, Rome.
[30]  Pichler, U., Hauser, M., Wolf, M., Bernardi, M. L., Gadermaier, G., Weiss, R. and Rafaiani, C. (2015). Pectate lyase pollen allergens: sensitization profiles and cross-reactivity pattern. PloS one, 10(5): e0120038.
[31]  Vieths, S., Scheurer, S., and BALLMER‐WEBER, B.A. (2002). Current understanding of cross‐reactivity of food allergens and pollen. Annals of the New York Academy of Sciences, 964(1): 47-68.
[32]  Ribeiro, H., Oliveira, M., Ribeiro, N., Cruz, A., Ferreira, A., Machado, H. and Abreu, I. (2009). Pollen allergenic potential nature of some trees species: A multidisciplinary approach using aerobiological, immunochemical and hospital admissions data. Environmental research, 109(3): 328-333.
Show Less References