One Hundred Years of Grain Omics: Identifying the Glutens That Feed the World

Abstract

Glutens, the storage proteins in wheat grains, are a major source of protein in human nutrition. The protein composition of wheat has therefore been an important focus of cereal research. Proteomic tools have been used to describe the genetic diversity of wheat germplasms from different origins at the level of polymorphisms in alleles encoding glutenin and gliadin, the two main proteins of gluten. More recently, proteomics has been used to understand the impact of specific gluten proteins on wheat quality. Here we review the impact of proteomics on the study of gluten proteins as it has evolved from fractionation and electrophoretic techniques to advanced mass spectrometry. In the postgenome era, proteomics is proving to be essential in the effort to identify and understand the interactions between different gluten proteins. This is helping to fill in gaps in our knowledge of how the technological quality of wheat is determined by the interaction between genotype and environment. We also collate information on the various storage protein alleles identified and their prevalence, which makes it possible to infer the effects of wheat selection on grain protein content. We conclude by reviewing the more recent use of transgenesis aimed at improving the quality of gluten.

A B-Cell Gene Signature Correlates With the Extent of Gluten-Induced Intestinal Injury in Celiac Disease

“…Although not well understood, oral tolerance to a food protein is an active immune response whose function is to suppress inflammatory immune responses to the same food protein when presented to the immune system for a second time. In celiac disease (CeD), a lack of oral tolerance develops to a family of cereal proteins collectively referred to as gluten, 2 resulting in a pathogenic and inflammatory immune response.…”

Serologic Assay for Diagnosis of Celiac Disease Based on a Patient-Derived Monoclonal Antigliadin Antibody

“…[4][5][6][7] Gluten is a heterogeneous mixture of proteins, and in wheat, gluten consists of many different gliadin and glutenin proteins. 8 Upon gastrointestinal digestion, these proteins are proteolyzed to shorter peptides by digestive enzymes. Both T cells 9 and antibodies 10,11 of celiac disease patients demonstrate better reactivity to gluten peptides that have become deamidated.…”

The effect of gluten on intestinal fermentation, gastric and gallbladder emptying in healthy volunteers

“…Gluten is a very complex compound, characterised by a high allelic polymorphism encoding its specific proteins, glutenin and gliadin [3], and by difficult digestion due to its high content of the amino acids proline and glutamine, which are resistant to cleavage by the major human gastrointestinal digestive enzymes [4]. The introduction of gluten occurred late in the Greek and Roman diet and represented an important evolutionary challenge that created the condition for human disease [5]: gluten exposure in genetically susceptible subjects determines coeliac disease (CD), a condition characterised by severe but reversible immuno-mediated lesions of the intestinal mucosa and increased morbidity and mortality [6].…”