Yıl: 2018 Cilt: 43 Sayı: 4 Sayfa Aralığı: 435 - 446 Metin Dili: İngilizce DOI: 10.1515/tjb-2017-0260 İndeks Tarihi: 08-10-2019

Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen

Öz:
Objective: Cupressaceae pollen has commonly beenreported to be an important aeroallergen and causal factorof spring, autumn and winter pollinosis in many countries.The aim of this study was to compare of the structureand allergenic protein content of Cupressus arizonicaGreene., Cupressus sempervirens L. and Juniperus oxycedrusL. pollen in detail and contribute to Cupressaceaepollen allergen diagnosis and therapy studies in Turkey.Methods: The pollen structure were examined by LM andSEM. Pollen protein content was investigated by Bradfordprotein assay, sodium dodecyl sulfate polyacrylamide gelelectrophoresis (SDS-PAGE), Western blot analysis andtwo-dimensional polyacrylamide gel electrophoresis (2DEPAGE), respectively. Pectate lyase (PL) enzyme activitieswere compared. Immunoblotting was carried out by usingextracts of the three taxa pollen collected from Turkey.Results: All three taxa was found very similar in termsof pollen morphology however, intine thickness wasprominently different. Cupressus arizonica pollen extractsshowed the lowest PL activity. Five sera specific IgE of allallergic subjects showed reaction with only C. arizonicapollen extracts.Conclusions: As a conclusion, the pollen structure, proteinfunction or protein structure and isoforms of allergenscould affects allergenic properties of the pollen. Thisstudy also may help to improve the Cupressaceae pollenallergen diagnosis and therapy.
Anahtar Kelime:

Konular: Diş Hekimliği Toksikoloji Biyokimya ve Moleküler Biyoloji Farmakoloji ve Eczacılık

Bazı Cupressaceae polenlerinde polen yapısı, alerjik protein içeriği ve pektat liyaz enzim aktivitesi bakımından farklılıklar

Öz:
Amaç: Cupressaceae polenlerinin birçok ülkede ilkbahar, sonbahar ve kış polinizasyon dönemleri için önemli aeroalerjen faktör olduğu sıklıkla bildirilmiştir. Bu çalışmanın amacı, Cupressus arizonica Greene, Cupressus sempervirens L. ve Juniperus oxycedrus L. polenlerin yapısını ve alerjenik protein içeriğini karşılaştırmak ve Türkiye‘de Cupressaceae polen alerjenlerinin tanısına ve alerji tedavisine katkıda bulunmaktır. Yöntemler: Polen yapısı LM ve SEM ile incelendi. Polen proteini içeriği, sırasıyla, Bradford protein testi, SDSPAGE, Western blot analizi ve 2DE PAGE ile araştırıldı. Pektat liyaz enzim aktiviteleri karşılaştırıldı. Immunoblot analizleri çalışılan üç taksona ait polen özütleri kullanılarak gerçekleştirildi. Bulgular: Her üç taksonun polen morfolojisi bakımından birbirine çok benzer olduğu ancak intinin kalınlığının taksonlar arasında belirgin olarak farklı olduğu bulundu. Cupressus arizonica polen özütlerinde en düşük pektat liyaz aktivitesi görülürken, hastaların beş tanesinde serum spesifik IgE, sadece C. arizonica polen ekstraktlarıyla reaksiyon gösterdi. Sonuç: Polen yapısı, protein fonksiyonu veya protein yapısı ve allerjenlerin izoformları polenlerin alerjenitelerini etkileyebilir. Bu çalışma ayrıca, Cupressaceae polen alerjisi tanısı ve tedavisine katkı sağlayabilir.
Anahtar Kelime:

Konular: Diş Hekimliği Toksikoloji Biyokimya ve Moleküler Biyoloji Farmakoloji ve Eczacılık
Belge Türü: Makale Makale Türü: Araştırma Makalesi Erişim Türü: Erişime Açık
  • 1. Charpin D, Hughes B, Mallea M, Sutra JP, Balansard G, Vervloet D. Seasonal allergic symptoms and their relation to pollen exposure in south-east France. Clin Exp Allergy 1993;23:435–9.
  • 2. Charpin D. Epidemiology of cypress allergy. Allerg Immunol 2000;32:83–5.
  • 3. Charpin D, Calleja M, Lahoz C, Pichot C, Waisel Y. Allergy to cypress pollen. Allergy 2005;60:293–301.
  • 4. Mari A, Felice G, Afferni C, Barletta B, Tinghino R, Pini C. Cypress allergy: an underestimated pollinosis. Allergy 1997;52:355–6. 5. Dubus JC, Melluso JP, Bodiou AC, Stremler-lebel N. Allergy to cypress pollen. Allergy 2000;55:410–1.
  • 6. İnceoğlu Ö, Pinar NM, Şakiyan N, Sorkun K. Airborne pollen concentration in Ankara, Turkey 1990–1993. Grana 1994;33:158–61.
  • 7. Pinar NM, Şakiyan N, İnceoğlu Ö, Kaplan A. A one-year aeropalynological study at Ankara, Turkey. Aerobiologia 1999;5:307–10.
  • 8. Erkara IP. Concentrations of airborne pollen grains in Sivrihisar (Eskisehir), Turkey. Environ Monit Assess 2008;138:81–91.
  • 9. Tosunoglu A, Bicakci A. Seasonal and intradiurnal variation of airborne pollen concentrations in Bodrum, SW Turkey. Environ Monit Assess 2015;187:167.
  • 10. Sin AZ, Ersoy R, Gulbahar O, Ardeniz O, Gokmen NM, Kokuludag A. Prevalence of cypress pollen sensitization and its clinical importance in Izmir, Turkey, with cypress allergy assessed by nasal provocation. J Investig Allergol Clin Immunol 2008;18:46–51.
  • 11. Accorsi CA, Mazzanti MB, Dallai D. Flora Palinologica Italiana, Sezione Aeropalinologica – S 103: Cupressus sempervirens L. Aerobiologia 1989;5:161–8.
  • 12. Milanesi C, Cresti M. Pollen morphology and ultrastructure in Cupressus sempervirens. Atti Accad Fisiocrit Siena XV 1997;141:59–61.
  • 13. Caiola MG, Travaglini A, Giuliano M. Palynological study of Cupressus sempervirens L. var. pyramidalis and var. horizontalis. Plant Biosystems 2000;134:99–109.
  • 14. Kurmann MH, Zawada MS. Pollen morphological diversity in extant and fossil gymnosperms. In: Kurmann MH, Doyle JA, editors. Ultrastructure of fossil spores and pollen. England: Royal Botanic Gardens, Kew, 1994:123–37.
  • 15. Heslop-Harrison J, Heslop-Harrison Y. Structural and functional variation in pollen intines. Pollen and spores: patterns of diversification. Oxford: Clarendon Press, 1991;331–43.
  • 16. Bowers JE, Chapman BA, Rong J, Paterson AH. Unravelling angiosperm genome evolution by phylogenetic analysis of chromosomal duplication events. Nature 2003;422:433–8.
  • 17. Adams KL, Wendel JF. Polyploidy and genome evolution in plants. Curr Opin Plant Biol 2005;8:135–41.
  • 18. Chen M, Xu J, Devis DL, Shi J, Ren K, Searle I, et al. Origin and functional prediction of pollen allergens in plants. Plant Physiol 2016;172:341–57.
  • 19. El Maâtaoui M, Christian P. Nuclear and cell fusion cause polyploidy in the megagametophyte of common cypress, Cupressus sempervirens L. Planta 1999;208.3:345–51.
  • 20. Shahali Y, Sutra JP, Charpin D, Mari A, Guilloux L, Sénéchal H, et al. Differential IgE sensitization to cypress pollen associated to a basic allergen of 14 kDa. FEBS J 2012;279:1445–55.
  • 21. Shahali Y, Sutra JP, Fasoli E, D’Amato A, Righetti PG, Futamura N, et al. Allergomic study of cypress pollen via combinatorial peptide ligand libraries. J Proteomics 2012;77:101–10.
  • 22. Shahali Y, Sutra JP, Haddad I, Vinh J, Guilloux L, Peltre G, et al. Proteomics of cypress pollen allergens using double and triple one-dimensional electrophoresis. Electrophoresis 2012;33: 462–9.
  • 23. Di Felice R. The voidage function for fluid particle interaction systems. Int J Multiphase Flow 1994;20:153–9.
  • 24. Arilla MC, Ibarrola I, Garcia R, De La Hoz B, Martinez A, Asturias JA. Quantification of the major allergen from Cypress (Cupressus arizonica) Pollen, Cup a 1, by monoclonal antibody-based ELISA. Int Arch Allergy Immunol 2004;134:10–6.
  • 25. Arilla MC, Ibarrola I, Martinez A, Asturias JA. Quantification assay for the major allergen of Cupressus sempervirens pollen, Cup s 1, by sandwich ELISA. Allergol Immunopathol 2004;32:319–25.
  • 26. Shahali Y, Majd A, Pourpak Z, Tajadod G, Haftlang M, Moin M. Comparative study of the pollen protein contents in two major varieties of Cupressus arizonica planted in Tehran, Iran. J Allergy Asthma Immunol 2007;6:123–7.
  • 27. Alisi C, Afferni C, Iacovacci P, Barletta B, Tinghino R, Butteroni, et al. Rapid isolation characterization and glycan analysis of Cup a 1 the major allergen of Arizona cypress (Cupressus arizonica) pollen. Allergy 2001;56:978–84.
  • 28. Barletta B, Afferni C, Tinghino R, Mari A, Di Felice G, Pini C. Cross-reactivity between Cupressus arizonica and Cupressus sempervirens pollen extracts. J Allergy Clin Immunol 1996;98:797–804.
  • 29. Midoro-Horiuti T, Goldblum RM, Kurosky A, Wood TG, Schein CH, Brooks EG. Molecular cloning of the mountain cedar (Juniperus ashei) pollen major allergen. J Allergy Clin Immunol 1999:104:613–7.
  • 30. Asam C, Hofer H, Wolf M, Aglas L, Wallner M. Tree pollen allergens-an update from a molecular perspective. Allergy 2015;70:1201–11.
  • 31. Wing RA, Yamaguchi J, Larabell SK, Ursin VM, McCormick S. Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia. Plant Mol Biol 1990;14:17–28.
  • 32. Marín-Rodríguez MC, Orchard J, Seymour GB. Pectate lyases, cell wall degradation and fruit softening. J Exp Bot 2002;53:2115–9.
  • 33. De Lorenzo G, Cervone F, Hahn MG, Darvill A, Albersheim, P. Bacterial endopectate lyase: evidence that plant cell wall pH prevents tissue maceration and increases the half-life of elicitor-active oligogalacturonides. Physiol Mol Plant Pathol 1991;39:335–44.
  • 34. Kamen DE, Woody RW. Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization. Biochemistry 2002;41:4713–23.
  • 35. Chichiriccò G, Spanò L, Torraca G, Tartarini A. Hydration, sporoderm breaking and germination of Cupressus arizonica pollen. Plant Biol 2009;11:359–68.
  • 36. Wodehouse RP. Pollen grains. New York: McGraw Hill, 1935. 37. Punt W, Hoen PP, Blackmore S, Nilsson S, Le Thomas A. Glossary of pollen and spore terminology. Rev Palaeobot Palynol 2007;143:1–81.
  • 38. Punt W, Hoen PP. The northwest european pollen flora, 70: asteraceae asteroideae. Rev Palaeobot Palynol 2009;157: 22–183.
  • 39. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248–54.
  • 40. Collmer A, Ried JL, Mount MS. Assay methods for pectic enzymes. Methods Enzymol 1988;161:329–35.
  • 41. Laemmli UK. Cleavege of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680–4.
  • 42. Duhoux E. Mechanism of exine rupture in hydrated taxoid types pollen. Grana 1982;21:1–7.
  • 43. Danti R, Della Rocca G, Mori B, Torraca G, Calamassi R, Lippi MM. Old World and New World Cupressus pollen: morphological and cytological remarks. Plant Syst Evol 2010;287:167–77.
  • 44. Taniguchi Y, Ono A, Sawatani M, Nanba M, Kohno K, Usui M, et al. Cry j I, a major allergen of Japanese cedar pollen, has pectate lyase enzyme activity. Allergy 1995;50:90–3.
  • 45. Aceituno E, Del Pozo V, Minguez A, Arrieta I, Cortegano I, Cardaba B, et al. Molecular cloning of major allergen from Cupressus arizonica pollen: Cup a 1. Clin Exp Allergy 2000;30:1750–8.
  • 46. Di Felice G, Barletta B, Tinghino R, Pini C. Cupressaceae pollinosis: identification, purification and cloning of relevant allergens. Int Arch Allergy immunol 2001;125:280–9.
  • 47. Togawa A, Panzani RC, Garza MA, Kishikawa R, Goldblum RM, Midoro-Horiuti T. Identification of Italian cypress (Cupressus sempervirens) pollen allergen Cup s 3 using homology and cross-reactivity. Ann Allergy Asthma Immunol 2006;97:336–42.
  • 48. Tinghino R, Barletta B, Palumbo S, Afferni C, Iacovacci P, Mari A, et al. Molecular characterization of a cross-reactive Juniperus oxycedrus pollen allergen, Jun o 2: a novel calcium-binding allergen. J Allergy and Clin Immunol 1998;101:772–7.
  • 49. Radauer C, Breiteneder H. Pollen allergens are restricted to few protein families and show distinct patterns of species distribution. J. Allergy Clin Immunol 2006;117:141–7.
  • 50. Pichler U, Hauser M, Wolf M, Bernardi ML, Gadermaier G, Weiss R, et al. Pectate lyase pollen allergens: sensitization profiles and cross-reactivity pattern. PLoS One 2015;10:e0120038.
  • 51. Shahali Y, Sutra JP, Peltre G, Charpin D, Sénéchal H, Poncet P. IgE reactivity to common cypress (C. sempervirens) pollen extracts: evidence for novel allergens. World Allergy Organ 2010;3:229.
  • 52. Swoboda I, Jilek A, Ferreira F, Engel E, Hoffmann-Sommergruber K, Scheiner O, et al. Isoforms of Bet v 1, the major birch pollen allergen, analyzed by liquid chromatography, mass spectrometry, and cDNA cloning. J Biol Chem 1995;270:2607–13.
  • 53. Ferreira F, Hirtenlehner K, Jilek A, Godnik-Cvar J, Breiteneder H, Grimm R, et al. Dissection of immunoglobulin E and T lymphocyte reactivity of isoforms of the major birch pollen allergen Bet v 1: Potential use of hypoallergenic isoforms for immunotherapy. J Exp Med 1996;183:599–609.
APA ACAR ŞAHİN A, Aslim B, TAN S, ALAN S, PINAR N (2018). Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. , 435 - 446. 10.1515/tjb-2017-0260
Chicago ACAR ŞAHİN Aydan,Aslim Belma,TAN Sema,ALAN SENOL,PINAR Nur Münevver Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. (2018): 435 - 446. 10.1515/tjb-2017-0260
MLA ACAR ŞAHİN Aydan,Aslim Belma,TAN Sema,ALAN SENOL,PINAR Nur Münevver Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. , 2018, ss.435 - 446. 10.1515/tjb-2017-0260
AMA ACAR ŞAHİN A,Aslim B,TAN S,ALAN S,PINAR N Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. . 2018; 435 - 446. 10.1515/tjb-2017-0260
Vancouver ACAR ŞAHİN A,Aslim B,TAN S,ALAN S,PINAR N Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. . 2018; 435 - 446. 10.1515/tjb-2017-0260
IEEE ACAR ŞAHİN A,Aslim B,TAN S,ALAN S,PINAR N "Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen." , ss.435 - 446, 2018. 10.1515/tjb-2017-0260
ISNAD ACAR ŞAHİN, Aydan vd. "Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen". (2018), 435-446. https://doi.org/10.1515/tjb-2017-0260
APA ACAR ŞAHİN A, Aslim B, TAN S, ALAN S, PINAR N (2018). Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. Türk Biyokimya Dergisi, 43(4), 435 - 446. 10.1515/tjb-2017-0260
Chicago ACAR ŞAHİN Aydan,Aslim Belma,TAN Sema,ALAN SENOL,PINAR Nur Münevver Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. Türk Biyokimya Dergisi 43, no.4 (2018): 435 - 446. 10.1515/tjb-2017-0260
MLA ACAR ŞAHİN Aydan,Aslim Belma,TAN Sema,ALAN SENOL,PINAR Nur Münevver Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. Türk Biyokimya Dergisi, vol.43, no.4, 2018, ss.435 - 446. 10.1515/tjb-2017-0260
AMA ACAR ŞAHİN A,Aslim B,TAN S,ALAN S,PINAR N Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. Türk Biyokimya Dergisi. 2018; 43(4): 435 - 446. 10.1515/tjb-2017-0260
Vancouver ACAR ŞAHİN A,Aslim B,TAN S,ALAN S,PINAR N Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen. Türk Biyokimya Dergisi. 2018; 43(4): 435 - 446. 10.1515/tjb-2017-0260
IEEE ACAR ŞAHİN A,Aslim B,TAN S,ALAN S,PINAR N "Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen." Türk Biyokimya Dergisi, 43, ss.435 - 446, 2018. 10.1515/tjb-2017-0260
ISNAD ACAR ŞAHİN, Aydan vd. "Differences in structure, allergenic protein content and pectate lyase enzyme activity of some Cupressaceae pollen". Türk Biyokimya Dergisi 43/4 (2018), 435-446. https://doi.org/10.1515/tjb-2017-0260