Similar is the case with the status of salivary IgA AGA estimation for CD. – antigliadin antibody, Immunoglobulin G – IgG. Keywords: Celiac disease, gliadin, peptides, immunoglobulins, autoimmunity Background Celiac disease (CD) is definitely a chronic illness which is characterized by mucosal lesion of the small intestine and impaired nutrient absorption from the bowel that enhances on gluten free diet. Its analysis is based on demonstration of villous atrophy in jejunal mucosa. The jejunal cells is generally acquired by endoscopoic biopsy, which is an invasive procedure. To select the subjects for invasive jejunal cells biopsy there exist a handful of serologic screening test that are commonly used in routine medical practice [1]. In CD the part of cells transglutaminase (TTG) and gliadin is definitely proved beyond any doubt. The disease entails antibody formation against both of these proteins. Diet containing gluten materials gliadin, a glutamine rich protein to the intestine. The elevated level of activated TTG in CD deamidate gliadin and Immunoglobulin A (IgA) antibody is definitely generated against both TTG and gliadin, which are utilized for serologic screening of the disease [2]. Gliadin is recognized as one of the important immune activator in CD [3]. Although gliadin is definitely a key pathogenic molecule of CD, serum IgA antigliadin antibody (IgA AGA) is not observed to be always an efficient tool for screening of CD. Some studies advocate its good level of sensitivity and specificity for such screening purpose [4], while other studies express an reverse view [5]. Currently no authority is definitely advocating the use of serum IgA AGA like a testing tool for CD [6]. Related is the case with the status of Rabbit Polyclonal to HBP1 salivary IgA AGA SKI-II estimation for CD. Some studies demonstrate positive result for the purpose while others show the opposite [7]. Contrary to IgA AGA estimation, in both serum and SKI-II saliva IgA TTG seems to be encouraging for the purpose of screening for CD [8]. The reason SKI-II behind such disparity of immuno-elevation of IgA-AGA and IgA-TTG in CD is currently not recognized. Some aspects are often overlooked in the immunodetection of IgAAGA in the context of CD. For immunodetection of IgA-AGA, generally gliadin antigen is definitely immobilized inside a well over which the sample is applied and that follows addition of secondary labeled antibody. It is intended that gliadin antigen will react with sample IgA antigliadin antibody [9]. With this modality of immunodetection, a CD specific fundamental switch of gliadin molecule is definitely ignored. In CD tissue trans-glutaminase functions on glutamine residues of gliadin and convert it to glutamate. Cells trans-glutaminase is significantly elevated in CD and it is known to cause deamidation of gliadin molecule and this modified gliadin molecule evokes immune response in CD [8]. Therefore it is quite possible the generated IgA antigliadin antibody will better react with the modified gliadin with glutamine residues changed to glutamate. Recently it is proved beyond any doubt that IgA raised against deamidated gliadin is definitely superior for the analysis/testing of celiac disease [10]. Assisting this view there is evidence that two stretches of nonapeptides derived from gliadins with glutamine changed to glutamate interact well with sera of CD patients,however the quantity of amino acids that binds with antibody can be actually less than nine [11]. For practical reason, involvement of peptides inside a diagnostic test with more quantity of amino acids will increase the cost of the analysis. Keeping SKI-II this fundamental inappropriateness we have designed a shorter peptide using tools of computational biology that may be experimentally verified for the purpose. The designed peptide is supposed to overcome the current limitations of IgA antigliadin antibody estimation in bio -fluids of CD individuals and if found adequate after experimental validation is definitely expected.