Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major storage protein, as an allergen in seeds of Lupinus angustifolius and Lupinus albus. Purification of conglutin beta from L. angustifolius flour confirmed that serum IgE binds to this protein. Where IgE in sera recognized lupin proteins on Western blots, it recognized conglutin beta, suggesting this protein is a major allergen for lupin. The L. angustifolius conglutin beta allergen has been designated Lup an 1 by the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee.

Lupin seeds are high in protein and dietary fibre but low in fat and starch and a number of health benefits have been associated with their consumption. As a result of these positive characteristics lupin seed components are increasingly being used as foods and food ingredients. However, allergic reactions to lupin have been reported on ingestion or inhalation of lupin seed proteins. In this study we have characterised the proteins from Lupinus angustifolius (narrow-leafed lupin) seeds that are allergens and also analysed genes encoding major seed storage proteins. To identify the allergenic proteins, L. angustifolius seed proteins were separated by two dimensional (2D) gel electrophoresis. Western blots of these gels were screened with serum from individuals allergic to lupin and the proteins that bound IgE (allergens) were identified by mass spectrometry. IgE reactive spots were positively identified (had two or more peptide matches to the same protein) and 32 corresponded to conglutin β β β β, one of the major seed storage proteins. In the initial part of the study, sera from individuals allergic to lupin but not peanut was used to characterise allergenic proteins. There is evidence that some individuals who are allergic to peanuts are more likely to be allergic to lupin and it is possible that these people react to different allergens. We are now investigating which lupin proteins are allergens for these people who react to lupin and peanut and conducting challenge tests to determine the identity of the cross-reactive allergens.

A study was undertaken to investigate whether the levels of carcino-embryonic antigen (CEA) in serous effusions helped distinguish between primary mesothelioma and metastatic adenocarcinoma in a body cavity. The investigation was designed to assess the role of the assay only when cytological analysis of the fluid had already shown the presence of malignant cells. No case of mesothelioma studied had levels of CEA above 2.9 ng/ml, whereas 67% of the adenocarcinomas tested were above 15 ng/ml. The test is helpful, therefore, in differentiating between these two types of malignant effusions.

Dermatophagoides mite concentrations in household dust have been measured in three Australian towns with contrasting geographical features, climate, and degree of urbanisation. Mite allergen skin tests on school children living in these areas showed that the prevalence of positive reactions varied with mite concentrations. In Belmont, D. farinae as well as D. pteronyssinus were present in some of the dust samples. Skin test weals were larger in Busselton than in either Wagga Wagga or Belmont. The importance and practical implications of these findings are discussed.

A 10-year-old boy with confirmed congenital agammaglobulinæmia presented with polyarthritis while on gammaglobulin replacement therapy. Initial cultures of material aspirated from an abscess and of joint fluid were negative, and symptoms progressed despite antibiotic therapy. Synovial-biopsy material, cultured specifically for mycoplasmas, was positive for Ureaplasma urealyticum as were the blood, abscess fluids, throat-swab, and nasopharyngeal secretions. Therapy, based on in-vitro studies of antibiotic susceptibilities of the organism, resulted in the eradication of the infection and resolution of the arthritis. These findings suggest that U. urealyticum may be capable of inducing polyarthritis in man.

Immunological and biochemical studies were carried out in two patients with the Lesch-Nyhan syndrome. No abnormalities of T- or B-lymphocyte function could be demonstrated in the presence of hypoxanthine-guanine phosphoribosyl transferase (HGPRT) deficiency.

Lupin seeds are high in protein and dietary fibre but low in fat and starch and a number of health benefits have been associated with their consumption. As a result of these positive characteristics lupin seed components are increasingly being used as foods and food ingredients. However, allergic reactions to lupin have been reported on ingestion or inhalation of lupin seed proteins. In this study we have characterised the proteins from Lupinus angustifolius (narrow-leafed lupin) seeds that are allergens and also analysed genes encoding major seed storage proteins. To identify the allergenic proteins, L. angustifolius seed proteins were separated by two dimensional (2D) gel electrophoresis. Western blots of these gels were screened with serum from individuals allergic to lupin and the proteins that bound IgE (allergens) were identified by mass spectrometry. IgE reactive spots were positively identified (had two or more peptide matches to the same protein) and 32 corresponded to conglutin β, one of the major seed storage proteins. In the initial part of the study, sera from individuals allergic to lupin but not peanut was used to characterise allergenic proteins. There is evidence that some individuals who are allergic to peanuts are more likely to be allergic to lupin and it is possible that these people react to different allergens. We are now investigating which lupin proteins are allergens for these people who react to lupin and peanut and conducting challenge tests to determine the identity of the cross-reactive allergens.