Poster Presentation ESA-SRB Conference 2015

Identification of salivary and placental proteins associated with subsequent allergic disease in childhood (#318)

Nurul NHMZ Mohamad Zainal 1 2 , Peter PH Hoffmann 3 , Astrud AT Tuck 1 , Vicki VC Clifton 1
  1. Robinson Research Institute, School of Paediatrics and Reproductive Health, The University of Adelaide, Adelaide, SA, Australia
  2. Department of Human Anatomy, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, UPM Serdang, Selangor, Malaysia.
  3. Adelaide Proteomics Centre, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia

Allergic disease has risen to epidemic proportions during recent years. It has become evident that prenatal events play a critical role in determining disease susceptibility via environmental influences on placental function and fetal programming. We hypothesize that childhood susceptibility to allergy is increased through significant alterations in placental gene expression and products of identified genes are altered in the saliva of allergic children. We aim to identify the proteins associated with childhood allergy using placental tissue from two populations of women whose children have different risks of allergic disease susceptibility. Then, we will determine whether these altered genes are detectable in the children’s salivary proteins. The objective of the study are to identify salivary proteins that could be a potential biomarker, to identify allergy risk in newborns and to identify targets proteins for early allergy interventions. Placenta and saliva will be examined using a proteomic approach that involves quantitative label-free comparative MS. Saliva and placental tissue from children with no allergy will be compared to children with either asthma, eczema and rhinitis (n=18). Six candidate proteins were identified in saliva samples associated with subsequent allergic disease in childhood and will be validated. Five proteins were identified present in all the allergic phenotypes that include Human Mucin-5B and Human Mucin 5AC with the ratio of >2 and Human Serum Albumin, Human Serotransferrin and Human Triosephosphate Isomerase with the ratio <0.5 fold change relative to non-allergic samples. Moreover, one protein was present in high expression in all 3 allergic phenotypes and had very low expression with no calculated ratio when compared with control group that is Human Pyruvate kinase PKM. The current findings suggest protein expression can be altered in utero in children who subsequently develop an allergy and the altered expressions of these proteins are detectable in saliva in early life.