Please use this identifier to cite or link to this item: https://doi.org/10.1046/j.1365-2222.1999.00523.x
Title: Sequence polymorphism of the group 1 allergen of Bermuda grass pollen
Authors: Chang, Z.-N.
Peng, H.-J.
Lee, W.-C.
Chen, T.-S.
Chua, K.-Y. 
Tsai, L.-C.
Chi, C.-W.
Han, S.-H.
Keywords: Bermuda grass pollen
cDNA clone
Group 1 allergen
Isoform
Polymorphism
Issue Date: 1999
Source: Chang, Z.-N.,Peng, H.-J.,Lee, W.-C.,Chen, T.-S.,Chua, K.-Y.,Tsai, L.-C.,Chi, C.-W.,Han, S.-H. (1999). Sequence polymorphism of the group 1 allergen of Bermuda grass pollen. Clinical and Experimental Allergy 29 (4) : 488-496. ScholarBank@NUS Repository. https://doi.org/10.1046/j.1365-2222.1999.00523.x
Abstract: Background: Cyn d 1, the major allergen of Bermuda grass pollen, consists of a number of isoforms. Objective: To examine the extent of sequence variation of Cyn d 1 isoforms at the molecular level. Methods: A Bermuda grass pollen λZAP II cDNA expression library was immunoscreened with anti-Cyn d 1 monoclonal antibodies. The reactive clones were isolated, subcloned into Escherichia coli, and sequenced. Some of them were expressed in the yeast Pichia pastoris to obtain recombinant Cyn d 1 proteins. Results: Ten cDNA clones were obtained, all these clones encode the full length of Cyn d 1 protein. Their deduced mature proteins can be grouped into: the long ones with 246 amino acids, and the short ones with 244 amino acids. The last two amino acids (AG) of the long Cyn d 1 are deleted in the short Cyn d 1. The remaining amino acid sequences share more than 98% identity; a total of nine amino acid variations were observed. Two recombinant Cyn d 1 proteins (rCyn d 3-2 and rCyn d 5-4) with three amino acid substitutions showed differential IgE-binding profiles. Conclusion: The present study extended our understanding of the primary structure of isoforms of Cyn d 1.
Source Title: Clinical and Experimental Allergy
URI: http://scholarbank.nus.edu.sg/handle/10635/107544
ISSN: 09547894
DOI: 10.1046/j.1365-2222.1999.00523.x
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