Diversità genetica del grano
Wheat occurs in a range of diploid, tetraploid and hexaploid forms (summarised in Table 1). The earliest cultivated forms were the A genome diploid einkorn (T. monococcum var monococcum) and tetraploid emmer (T. turgidum var. dicoccum) with the A and B genomes. These are closely related to wild forms: diploid T. monococcum var. monococcum and T. ururtu and tetraploid T. turgidum var. dicoccoides, respectively. Modern tetraploid durum (pasta) wheat (T. turgidum var. durum) probably arose from mutations in cultivated emmer.
Hexaploid wheat (Triticum aestivum) (genomes ABD)
Hexaploid wheat (Triticum aestivum) (genomes ABD) has never existed as a wild species and no wild hexaploid wheats are known. It probably arose by hybridization of cultivated emmer with the related wild grass T. tauschii (goat grass, also called Aegilops tauschii and Ae. squarossa). This hybridization probably occurred in south-eastern Turkey about 9000 years ago (Feldman, 1995, Dubcovsky and Dvorak, 2007) and contributed the D genome. All cultivated hexaploid wheats, including spelt, are forms of T. aestivum.
A major difference between “ancient” cultivated wheats (einkorn, emmer, spelt) and their wild relatives and modern durum and bread wheats is whether the grain are hulled or free threshing. In hulled wheats the glumes and palea adhere to the grain and the threshed material consists of intact spikelets.
As the most coeliac-active T-cell epitopes are present on the α-gliadins, emphasis has been placed on exploring differences in the amounts and sequences of proteins of this class. Kasarda et al. (1976)
33mer fragment of α-gliadin
The studies of van Herpen et al. (2006) showed that T-cell stimulatory epitopes were more abundant in α-gliadins encoded by the D genome, and Molberg et al. (2005) who demonstrated that the immunodominant 33mer fragment of α-gliadin was encoded by chromosome 6D (and hence absent from diploid einkorn and tetraploid wheats).
The absence of the D genome from durum wheat
The absence of the D genome from durum wheat could result in lower coeliac activity due to the absence of the T-cell stimulatory epitopes at the Gli-D2 locus. van den Broeck et al. (2010a) therefore screened 103 accessions of tetraploid wheat by immunoblotting of gluten protein extracts with monoclonal antibodies against the Glia-α9 and Glia-α20 epitopes. This identified three accessions with significantly reduced levels of both epitopes. Further analysis of 61 durum wheat accessions by high throughput transcript sequencing similarly identified some accessions with lower abundances of transcripts containing coeliac disease epitopes (Salentjin et al., 2013).
Other gluten proteins
Although impressive progress has been made with identifying variation in the abundances of coeliac disease epitopes in α-gliadins, it must be borne in mind that other groups of gluten protein also contain coeliac active sequences. This was demonstrated in the survey of gluten protein sequences in the Uniprot protein sequence database by Spaenij-Dekking et al. (2005) which is referred to above. They showed that T-cell stimulatory epitopes were present in all γ-gliadin sequences (17/17), in 95.5% (21/22) of HMW subunit sequences and in 5% of LMW subunit sequences (3/57), in addition to 66% (19/29) of α-gliadin sequences. (Improving wheat to remove coeliac epitopes but retain functionality. Peter R. Shewry and Arthur S. Tatham 2016).