Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An egg protein, lysozyme, is a still unlabeled additive currently used in cheese preparation. Furthermore, the WHO-FAO committee considers it innocuous. However, 31% of children and 8% of adults with food allergies are allergic to eggs. This work aimed to determine the percentage of patients sensitized to lysozyme from a population of egg-allergic patients. Specific IgE was determined with Cap RAST in 52 patients clinically allergic to egg. Thirty-five percent of egg-allergic patients had antilysozyme IgE. Given this high incidence of lysozyme sensitization, it seems that the presence of lysozyme should be indicated on food labels.
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PMID:Prevalence of lysozyme sensitization in an egg-allergic population. 910 30

Serum levels of immuno-globulin G, A, M, D and E were determined using single radial immuno-diffusion technique in 52 Nigerian primary school children with urinary schistosomiasis and 39 age and sex matched controls. The mean values of IgA, IgM and IgE in the school children with S. haematobium infection were significantly higher than in controls. These findings suggest that urinary schistosomiasis in these subjects was in the acute stage.
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PMID:Serum immunoglobins in Nigerians with urinary schistosomiasis. 933 15

Human foods are usually prepared by cooking. Boiling of chicken egg-white (EW) led to decreased allergenicity, and abrogated intestinal uptake of immunoreactive ovalbumin (OVA) when fed to mice. Therefore, the effects of oral administration of boiled EW were examined further in BALB/c mice. Specific IgE, IgG1 and IgG antibody responses were suppressed by raw EW, but not by EW boiled for 5 or 60 min, fed prior to sensitization with 10 microg OVA or 1 microg DNP-OVA in alum. Similar results were obtained when mice were sensitized with 10 microg conalbumin, ovomucoid or lysozyme in alum. BALB/c spleen cell proliferation and secretion of Th2 cytokines IL-4 and IL-5 during in vitro stimulation with OVA were also suppressed by feeding raw EW, but not by boiled EW. Although heat denaturation of proteins can minimize allergenicity, the present results suggest that over-cooking of proteins may affect their intestinal antigen processing and thus prevent the induction of oral tolerance.
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PMID:Heat denaturation of egg-white proteins abrogates the induction of oral tolerance of specific Th2 immune responses in mice. 982 57

Immediate-type allergic reactions to latex products made from natural rubber are called latex allergy. One of the notable features of latex-allergic people is their cross-reactivity to various vegetable foods and pollen. The structurally similar proteins which most kinds of plants potentially induce must be responsible for these cross-reactions. However, the taxonomical dissimilarity among the causative plants has kept us from concrete explanations of such cross-reactive allergens. We have speculated that plant defense-related proteins are a possible cause of the latex allergy. The well-known serologic relationships and sequence similarities of these ubiquitous plant proteins can explain the cross-reactivity without difficulty. Rubber trees cultured in plantation farms are repeatedly tapped and treated with phytohormones. These stresses would result in the significant induction of defense-related proteins. Indeed, we were able to detect defense-related enzymes in latex extracts. Moreover, three hydrolytic enzymes (beta-1,3-glucanase, chitinase/lysozyme, and carboxylesterase) that are very likely to take a defensive role were specifically recognized by the IgE antibodies of latex-allergic people and atopic patients. These experimental results strongly support our hypothesis. Because of their conserved structures, defense-related proteins should form a family of plant pan-allergens.
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PMID:[Plant defense-related proteins as latex allergens]. 1009 12

One of the major challenges of molecular allergy is to predict the allergenic potential of a protein, particularly in novel foods. Two aspects have to be distinguished: immunogenicity and cross-reactivity. Immunogenicity reflects the potential of a protein to induce IgE antibodies, whereas cross-reactivity is the reactivity of (usually preexisting) IgE antibodies with the target protein. In addition to these two issues, the relation between IgE-binding potential and clinical symptoms is of interest. This is influenced by physical properties (eg, stability and size) and immunologic properties (affinity and epitope valence). Discussions on immunogenicity and cross-reactivity of allergens rely on the establishment of structural similarities and differences among allergens and between allergens and nonallergens. For comparisons between the 3-dimensional protein folds, the representation as 2-dimensional proximity plots provides a convenient visual aid. Analysis of approximately 40 allergenic proteins (or parts of these proteins), of which the protein folds are either known or can be predicted on the basis of homology, indicates that most of these can be classified into 4 structural families: (1) antiparallel beta-strands: the immunoglobulin-fold family (grass group 2, mite group 2), serine proteases (mite group 3, 6, and 9), and soybean-type trypsin inhibitor (Ole e 1, grass group 11); (2) antiparallel beta-sheets intimately associated with one or more alpha-helices: tree group 1, lipocalin, profilin, aspartate protease (cockroach group 2); (3) (alpha+beta) structures, in which the alpha- and beta-structural elements are not intimately associated: mite group 1, lysozyme/lactalbumin, vespid group 5; and (4) alpha-helical: nonspecific lipid transfer protein, seed 2S protein, insect hemoglobin, fish parvalbumin, pollen calmodulin, mellitin from bee venom, Fel d 1 chain 1, serum albumin. Allergens with parallel beta-strands (in combination with an alpha-helix linking the two strands, a motif commonly found in, for example, nucleotide-binding proteins) seem to be underrepresented. The conclusion is that allergens have no characteristic structural features other than that they need to be able to reach (and stimulate) immune cells and mast cells. Within this constraint, any antigen may be allergenic, particularly if it avoids activation of T(H)2-suppressive mechanisms (CD8 cells and T(H)1 cells).
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PMID:Structural biology of allergens. 1093 64

Infections with parasitic helminths such as Nippostronglyus brasiliensis induce dominant type 2 responses from antigen-specific T helper cells. The potency of the Th2 bias can also drive Th2 responses to bystander antigens introduced at the same time as infection. We now report that the Th2-promoting effect of infection can be reproduced with soluble N. brasiliensis excretory-secretory proteins (NES) released by adult parasites in vitro. Immunization of BALB/c mice with NES results in the production of IL-4 with elevated total serum IgE and specific IgG1 antibodies. NES is also able to stimulate IL-4 and polyclonal IgE production in other mouse strains (C57BL/6, B10.D2, CBA). These features are seen whether NES is administered without adjuvant as soluble protein in phosphate-buffered saline or with complete Freund's adjuvant which normally favors Th1 responses. Thus, NES possesses intrinsic adjuvanticity. Moreover, co-administration of hen egg lysozyme (HEL) with NES in the absence of other adjuvants results in generation of HEL-specific lymphocyte proliferation, IL-4 release and IgG1 antibody responses, documenting that NES can act as an adjuvant for third-party antigens. Proteinase K digestion or heat treatment of NES before immunization abolished the IL-4-stimulating activity, indicating that the factors acting to promote Th2 induction are proteins secreted by the adult parasite.
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PMID:Proteins secreted by the parasitic nematode Nippostrongylus brasiliensis act as adjuvants for Th2 responses. 1094 Aug 87

Glycosylation-inhibiting factor (GIF) is a 13-kDa cytokine secreted from T cells. Administration of bioactive recombinant GIF inhibits IgG1 and IgE Ab responses in vivo. Treatment of B cells with the cytokine reduces the secretion of IgG1 and IgE induced by LPS and IL-4. To examine the effect on cognate T-B interaction, GIF was added to low-density B cells from MD4 transgenic (Tg) mice, which express B cell receptor specific for hen egg lysozyme (HEL). The B cells were subsequently pulsed with HEL-OVA conjugate and cultured with OVA-specific naive CD4 T cells from DO11.10 Tg mice. Treatment of Ag-presenting B cells with GIF reduced expansion and IL-2 secretion of naive T cells and rendered them hyporesponsive to antigenic restimulation, resulting in 50--95% reduction of IL-4 and IFN-gamma secretion upon restimulation with Ag. GIF dramatically inhibited Th effector generation when it was added to B cells before pulsing with HEL-OVA, whereas it showed little to no effect when added after B cells were pulsed with Ag. GIF was more effective when B cells from MD4 Tg mice were pulsed with HEL-OVA than when they were pulsed with OVA. This cytokine did not affect Th effector generation when B cells or irradiated splenocytes pulsed with OVA(323--339) peptide stimulated naive DO11.10 T cells. Confocal microscopy revealed that GIF inhibited internalization of HEL by B cells from MD4 Tg mice. Therefore, the cytokine may regulate early steps of Ag presentation involving B cell receptors to diminish Th effector generation from naive CD4 T cells.
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PMID:GIF inhibits Th effector generation by acting on antigen-presenting B cells. 1125 3

To investigate the effect of polysaccharide attachment to proteins on the production of IgG and IgE, the genetic attachment of polysaccharide to lysozymes (G49N and R21T) using the yeast expression system (Saccharomyces cerevisiae AH 22) and the Maillard-type polysaccharide attachment to native lysozyme and soybean P34 protein were attempted. The production of IgG and IgE was investigated by using mice immunized with the protein-polysaccharide conjugates or native proteins. The attachment of polysaccharide to lysozyme using the yeast expression system greatly suppressed the production level of IgG and IgE. The attachment of polysaccharide to native lysozyme and soybean P34 protein using the Maillard-type reaction was also found to be effective in reducing the production level of IgE compared to IgG.
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PMID:Effect of chemical and genetic attachment of polysaccharides to proteins on the production of IgG and IgE. 1130 63

One hundred and forty five patients with different forms of dust-induced lung disease and 57 controls having no contacts with industrial aerosols were examined. It was ascertained that clinical and functional evidence cannot predict the course of the disease and the development of infectious complications (silicotuberculosis, mechanic bronchitis). Impaired humoral immunity and nonspecific resistance in dust-induced lung disease depend on the type of disease and predispose to infectious complications. Predisposition to occupational lung diseases (pneumoconioses, mechanical bronchitis) is associated with increases in the concentrations of plasma fibronectin and serum IgA and a decrease in serum mucin antigen levels. In chronic mechanical bronchitis, there were lower activities of lysozyme and complement and elevated serum IgM and IgG concentrations. Fibronectin, total IgE and the inflammatory marker the mucin antigen 3EG5 are involved in immunological inflammation in dust-induced lung disease. It is worth of determining the factors of humoral immunity and nonspecific resistance in workers contacting with high concentrations of industrial aerosols and in patients with dust-induced diseases to make a precise assessment of the time course of changes in a pathological process and to define a risk for infectious complications.
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PMID:[Immunological changes in dust-induced lung diseases]. 1131 68

Allergies to various inhalative allergens are a serious problem in the bakery and confectionery industry. Sensitization to wheat flour and enzymes such as alpha-amylase are a frequent cause of occupational asthma. Airborne egg allergens have been reported as another cause of respiratory allergy. We examined bakery and confectionery workers with respiratory symptoms due to egg aerosols. Skin tests (SPT), scratch tests (ST), nasal provocation tests (NPT) and serological examinations (IgE) were performed. Lung function was assessed by spirometry, and continuous registration of aerosols and particulates as well as gravimetric sampling was done at the workplace. Four bakery and two confectionery workers intensively exposed to airborne egg proteins suffered from conjunctivitis and rhinitis, four also from asthma. Subsequently, three of these four workers reported symptoms after ingestion of food that contained egg. SPT with commercial egg white and egg yolk extracts were negative in four cases. Only two employees had clearly positive SPT to commercial egg allergens and reacted also to wheat flour extracts. Scratch tests with native egg proteins were positive in four employees. Specific IgE to egg white and egg yolk were positive (CAP > or = 2) in three and in four cases, respectively, whereas they were negative in two cases. Elevated levels of specific IgE to lysozyme were detected in four employees. Two workers were sensitized to lysozyme but not to other egg proteins. The clinical relevance of egg sensitization was confirmed by continuous air sampling and by correlating the onset of the respiratory symptoms which were reflected by a significant decline (> or = 30%) of the forced one second capacity (FEV1) in two workers. Sieving of egg white powder and an inadequate spray station for liquid eggs were identified as sources of excessive allergen exposure. Bakery and confectionery workers exposed to airborne egg proteins are at risk of developing occupational asthma and subsequent nutritive egg allergy. To our knowledge, these are the first cases of inhalative egg allergy and subsequent nutritive egg allergy reported in the literature, which we refer to as the "egg-egg syndrome" in analogy to the already known "bird-egg" and "egg-bird" syndromes.
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PMID:The "egg-egg" syndrome: occupational respiratory allergy to airborne egg proteins with consecutive ingestive egg allergy in the bakery and confectionery industry. 1164 78


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