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Rates of international migration are increasing, which raises the question of how migration might influence couple relationship standards and impact on the standards of migrants forming intercultural relationships. We compared relationship standards in n = 286 Chinese living in Hong Kong, China with standards in n = 401 Chinese migrants to a Western country (Australia) by administering the Chinese-Western Intercultural Couple Standards Scale (CWICSS). We also compared these two groups to n = 312 Westerners living in Australia. We first tested the structural invariance of the CWICSS across the three samples with a multi-group confirmatory factor analysis. There was marginal but acceptable fit of a model of two positively correlated latent factors: Couple Bond (with four indicators, such as demonstration of love and caring) and Family Responsibility (also with four indicators, such as extended family relations and preserving face). Within the limitations of the study, results suggest migration is associated predominantly with differences in women’s but not men’s relationship standards. Migrant Chinese women show alignment of Couple Bond standards toward Western standards, and conversely greater distance away from Western standards with stronger endorsement of Family Responsibility standards. Discussion focused on how migration and intercultural relationship experiences might differentially influence different domains of relationship standards, gender differences in migration effects on standards, and the implications for working with culturally diverse couples.

BACKGROUND Shellfish allergy is one of the most common food hypersensitivities worldwide but allergen-specific immunotherapy for shellfish allergy is not yet available. We believe that T cell peptide-based immunotherapy holds the potential for modulating allergic responses without IgE cross-linking. OBJECTIVE We sought to identify the immunodominant T cell epitopes of tropomyosin, the major shrimp allergen of Metapenaeus ensis (Met e 1), and to evaluate their therapeutic effects in a Balb/c mouse model of Met e 1 hypersensitivity. METHODS T cell epitopes of Met e 1 were first identified based on the proliferation and cytokine responses of splenocytes isolated from Met e 1-sensitized Balb/c mice upon stimulation by 18 synthetic peptides that span the full-length Met e 1. The immunodominant T cell peptides identified were then fed orally to Met e 1-sensitized Balb/c mice twice a week for four weeks. Allergic responses, serological antibody levels, intestinal histology and systemic and local cytokine profiles were compared between the treated and the untreated groups. RESULTS Six major Met e 1 T cell epitopes were identified. Mice treated with the T cell epitope peptide mixture demonstrated an amelioration of systemic allergic symptoms and a significant reduction in Th2-associated antibody and cytokine responses. These benefits were accompanied by a shift to a balanced Th1/Th2 response, induction of IgG2a antibodies possessing in vitro and in vivo blocking activities and the induction of regulatory T cell responses. CONCLUSIONS AND CLINICAL RELEVANCE T cell epitope-based oral immunotherapy is effective in reducing allergic responses towards shrimp tropomyosin. This is a novel strategy for clinical management of shellfish allergy and is a model for mechanistic studies of oral immunotherapy.

With the progressive aging of the world's population, immunosenescence is rapidly becoming a clinical concern as it accounts for a higher incidence of severe infections and poor response to vaccines. To identify nutritional approaches that may counteract immunosenescence is of obvious importance in clinical practice. Dairy products in general and whey proteins in particular share the capacity to stimulate the immune system within the digestive tract while the antibody response to Streptococcus pneumoniae vaccine is a good marker of the immune function. We performed a controlled, randomized, double-blind pilot study to determine if an eight-week supplementation with whey protein (or soy protein used as control) could enhance the serum response to pneumococcal vaccine in healthy senior citizens. Out of 127 volunteers, 17 subjects were eligible and completed the study receiving the vaccine after four weeks of supplementation. Antibody levels were measured at baseline and the end of the study against 14 pneumococcal types and a detailed nutritional questionnaire was administered to all subjects. Subjects receiving whey protein manifested a serum response higher compared to the control soy supplementation against 12/14 bacterial types. In particular, whey led to a higher frequency of response to all four more virulent types (4, 9, 14, and 23). Calorie and protein intake data suggest a better nutritional status in the whey group. Whey protein supplementation is a promising supplement to stimulate the immune response to vaccine in senior citizens and possibly to counteract immunosenescence while larger studies are warranted.

Background Shellfish is one of the most common food allergens. Despite the recent cloning and molecular identification of the major heat stable crustacean allergens in shrimp, lobster and crab, there have been no similar studies on molluscs to which a significant portion of populations allergic to shellfish are also hypersensitive. Recent biochemical evidence suggests that tropomyosin is also an allergen in molluscs, but data on the molecular cloning, nucleotide sequencing, expression and IgE binding to mollusc tropomyosin are lacking. Objective This study was undertaken to clone, identify and determine the primary structure of a major IgE-reactive mollusc allergen in oyster at the DNA and protein level. Methods We constructed an expression cDNA library from the Pacific oyster Crassostrea gigas. This library was screened for IgE binding clones using sera from 15 subjects with a well-documented history of type I hypersensitivity reactions to oysters. An IgE reactive clone was selected and sub-cloned into plasmids for nucleotide sequence determination and expression in E. coli. Results We identified a 1.3-kb cDNA designated as Cra g 1.03. Expression of Cra g 1.03 in plasmid vector pGEX produced a 59-kDa recombinant fusion protein reactive to the IgE antibodies from patients with oyster allergies but not non-allergic controls. Cra g 1.03 has an open reading frame of 233 amino acids and demonstrates marked similarity in amino acid composition and peptide sequence with mollusc and crustacean tropomyosins. Absorption of oyster allergic sera with Cra g 1.03 totally removed IgE reactivity to oyster extract. Moreover, absorption of allergic sera with recombinant shrimp tropomyosin (Met e 1), lobster tropomyosin (Pan s 1) and crab tropomyosin (Cha f 1) removed most of the IgE reactivity to Cra g 1.03. Conclusion Cra g 1.03 is the first oyster allergen identified at the molecular level. Nucleotide and amino acid comparison shows that this protein is the oyster tropomyosin.

Mitochondrial autoantibodies, a hallmark of primary biliary cirrhosis (PBC), have been widely described for many years in patients with systemic sclerosis, and there have been several reports of the concurrence of systemic sclerosis and PBC. However, there is very little information with respect to the significance of these autoantibodies or any definitive evidence that the antigens involved represent the mitochondrial autoantigens (M2 complex) described in PBC. We have cloned and sequenced a rat complementary DNA which encodes for all the epitopes recognized by autoantibodies to the major, or 70-kd, mitochondrial autoantigen in patients with PBC. Using this recombinant fused autoantigen, as well as by immunoblotting with human placental mitochondria, we tested for antimitochondrial antibody specificity in sera from 250 patients with systemic sclerosis. Nineteen sera (7.6%), including those from patients with CREST (calcinosis, Raynaud's phenomenon, esophageal dysmotility, sclerodactyly, telangiectasias) and diffuse scleroderma, had reactivity with human placental mitochondria proteins by immunoblot testing. All 19 sera reacted with the M2 complex. All sera that reacted with the 70-kd protein likewise reacted with the recombinant cloned autoantigen. The predominant autoantibody isotype to the 70-kd protein was IgG3. Interestingly, the 70-kd protein is 11% proline, an amino acid which is frequently preceded by hydrophobic amino acids.