Displaying publications 1 - 20 of 109 in total

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  1. Wafriy CI, Kamsani YS, Nor-Ashikin MNK
    Cells Dev, 2023 Sep;175:203864.
    PMID: 37321350 DOI: 10.1016/j.cdev.2023.203864
    The incidence of allergic asthma has been increasing worldwide in recent decades. Also, an increasing number of women are suffering from poor pregnancy outcome. However, the causal relationship between allergic asthma and embryonic growth in terms of cell morphogenesis has not been well elucidated. Here, we investigated the impact of allergic asthma on the morphogenesis of preimplantation embryos. Twenty-four female BALB/c were randomly divided into control (PBS), 50-μg (OVA1), 100-μg (OVA2) and 150-μg (OVA3). On Days-0 and -14, mice were induced intraperitoneally (i.p) with ovalbumin (OVA). On Days-21 until -23, mice were challenged with OVA via intranasal instillation (i.n). Control animals were sensitized and challenged with PBS. At the end of treatment (Day-25), 2-cell embryos were retrieved and cultured in vitro until the blastocysts hatched. Results showed reduced number of preimplantation embryos at all developing stages in all treated groups (p ≤ 0.0001). Uneven blastomere size, partial compaction- and cavitation-activity, low formation of trophectoderm (TE), as well as cell fragmentation were noted in all the treated groups. Maternal serum interleukin (IL)-4, immunoglobulin (Ig)-E and 8-hydroxydeoxyguanosine (8-OHdG) were notably high (p ≤ 0.0001, p ≤ 0.01) in contrast with low total antioxidant capacity (TAOC) (p ≤ 0.0001). Our findings indicated that OVA-induced allergic asthma had compromised cell morphogenesis through reduced blastomere cleavage division, partial compaction and cavitation-activity, impairment of TE production, and cell fragmentation leading to embryonic cell death via OS mechanism.
    Matched MeSH terms: Immunoglobulin E/adverse effects; Immunoglobulin E/metabolism
  2. Tiew PY, Narayana JK, Quek MSL, Ang YY, Ko FWS, Poh ME, et al.
    Eur Respir J, 2023 Jan;61(1).
    PMID: 35926878 DOI: 10.1183/13993003.00507-2022
    BACKGROUND: Variable clinical outcomes are reported with fungal sensitisation in chronic obstructive pulmonary disease (COPD), and it remains unclear which fungi and what allergens associate with the poorest outcomes. The use of recombinant as opposed to crude allergens for such assessment is unknown.

    METHODS: A prospective multicentre assessment of stable COPD (n=614) was undertaken in five hospitals across three countries: Singapore, Malaysia and Hong Kong. Clinical and serological assessment was performed against a panel of 35 fungal allergens including crude and recombinant Aspergillus and non-Aspergillus allergens. Unsupervised clustering and topological data analysis (TDA) approaches were employed using the measured sensitisation responses to elucidate if sensitisation subgroups exist and their related clinical outcomes.

    RESULTS: Aspergillus fumigatus sensitisation was associated with increased exacerbations in COPD. Unsupervised cluster analyses revealed two "fungal sensitisation" groups. The first was characterised by Aspergillus sensitisation and increased exacerbations, poorer lung function and worse prognosis. Polysensitisation in this group conferred even poorer outcome. The second group, characterised by Cladosporium sensitisation, was more symptomatic. Significant numbers of individuals demonstrated sensitisation responses to only recombinant (as opposed to crude) A. fumigatus allergens f 1, 3, 5 and 6, and exhibited increased exacerbations, poorer lung function and an overall worse prognosis. TDA validated these findings and additionally identified a subgroup within Aspergillus-sensitised COPD of patients with frequent exacerbations.

    CONCLUSION: Aspergillus sensitisation is a treatable trait in COPD. Measuring sensitisation responses to recombinant Aspergillus allergens identifies an important patient subgroup with poor COPD outcomes that remains overlooked by assessment of only crude Aspergillus allergens.

    Matched MeSH terms: Immunoglobulin E
  3. Jambari NN, Wang X, Alcocer M
    Methods Mol Biol, 2017;1592:129-137.
    PMID: 28315216 DOI: 10.1007/978-1-4939-6925-8_10
    Protein microarray is a miniaturized multi-analyte, solid-phased immunoassay where thousands of immobilized individual protein spots on a microscopic slide bind are bound to specific antibodies (immunoglobulins) from serum samples, which are then detected by fluorescent labeling. The image processing and pattern recognition are then quantitatively analyzed using advanced algorithms. Here, we describe the use of an in-house-produced complex protein microarray containing extracts and pure proteins that has been probed with antibodies present in the horse sera and detection by fluorophore-conjugated antibody and data analysis. The flexibility of the number and types of proteins that can be printed on the microarray allows different set of specific IgE immunoassay analysis to be carried out.
    Matched MeSH terms: Immunoglobulin E/immunology*
  4. Pang SL, Matta SA, Sio YY, Ng YT, Say YH, Ng CL, et al.
    Sci Rep, 2021 01 13;11(1):921.
    PMID: 33441720 DOI: 10.1038/s41598-020-79820-y
    House dust mites (HDMs) are one of the major causes of allergies in the world. The group 23 allergen, Der p 23, from Dermatophagoides pteronyssinus, is a major allergen amongst HDM-sensitized individuals. This study aims to determine the specific immunoglobulin E (sIgE) binding frequency and IgE-binding residues of recombinant Der p 23 (rDer p 23) allergen amongst a cohort of consecutive atopic individuals in a tropical region. We performed site-directed mutagenesis and carried out immuno-dot blot assays using 65 atopic sera. The immuno-dot blot assays results indicated that the two residues K44 and E46 which are located at the N-terminal region are the major IgE-binding residues. The rDerp-23 sIgE titers are strongly correlated to the number of IgE-binding residues for rDer p 23 (P 
    Matched MeSH terms: Immunoglobulin E/blood; Immunoglobulin E/immunology; Immunoglobulin E/metabolism
  5. Misnan R, Murad S, Yadzir ZH, Abdullah N
    Asian Pac J Allergy Immunol, 2012 Dec;30(4):285-93.
    PMID: 23393908
    Tropomyosin and arginine kinase have been identified as the major allergens in multiple species of crab. Charybdis feriatus is an important commercial crab in this country.
    Matched MeSH terms: Immunoglobulin E/blood; Immunoglobulin E/immunology*
  6. Yeang HY, Chow KS, Yusof F, Arif SA, Chew NP, Loke YH
    J Investig Allergol Clin Immunol, 2000 Jul-Aug;10(4):215-22.
    PMID: 11039838
    Six Hevea brasiliensis latex protein allergens, Hevb 1, Hev b 2, Hev b 3, Hev b 4, and two variants of Hev b 7 (7b and 7c), were purified from Hevea latex, while a seventh protein, Hev b 5, was prepared in recombinant form. The presence of these proteins in glove extracts was indicated by their respective antibodies in the serum of rabbits immunized against the extracts. The relative propensities of IgE binding to the individual latex allergens were compared using sera from latex-allergic patients. IgE recognition of Hev b 4, Hev b 7b, Hev b 5 and Hev b 2 was most frequently encountered, with 75, 61, 31 and 28%, respectively, of the patient sera reacting. Sensitivity to multiple latex proteins was common, and out of the 31 seropositive patients, 23 (74%/ ) had IgE against at least two latex allergens, while 12 (39%) had IgE specific for at least three allergens. Statistical analysis of the data suggested that many patients might have acquired sensitivity to Hev b 2, Hev b 4 and Hev b 7b from a common source. (e.g., from latex products). On the other hand, sensitivity to Hev b 5 and to Hev b 7c were interrelated. It is plausible that sensitivity to these two proteins might have been acquired from sources other than latex products (e.g., from certain foods).
    Matched MeSH terms: Immunoglobulin E/blood; Immunoglobulin E/metabolism
  7. Hamizan AW, Rimmer J, Alvarado R, Sewell WA, Tatersall J, Barham HP, et al.
    Am J Rhinol Allergy, 2019 Mar;33(2):178-183.
    PMID: 30656948 DOI: 10.1177/1945892418825224
    BACKGROUND: Specific immunoglobulin E (sIgE) within the nasal airway is likely to be the most ideal marker of allergic status, but little is known of the normative values in asymptomatic patients and those with rhinitis.

    OBJECTIVE: The aim of this study was to assess the diagnostic characteristics of inferior turbinate tissue biopsy sIgE in asymptomatic and rhinitic patients.

    METHODS: A diagnostic cross-sectional study was undertaken, involving patients who underwent inferior turbinate surgery with or without other surgical interventions. Inferior turbinate tissue biopsy was performed during surgery and was assessed for allergen sIgE (dust mite, grass [temperate or subtropical], and animal epithelium) using an automated immunoassay. Tissue sIgE was assessed among asymptomatic patients and those with nasal symptoms. Data were presented as median (interquartile range). A receiver operating curve was used to predict the diagnostic utility of turbinate tissue sIgE in determining allergic rhinitis.

    RESULTS: A total of 160 patients (41.89 ± 14.65 years, 36.9% females) were included. The median tissue sIgE concentration among the asymptomatic nonatopic group of patients was 0.09 (0.08-0.10) kUA/L and tissue sIgE > 0.10 kUA/L was determined as a positive threshold. Inferior turbinate tissue sIgE was shown to be a predictive test for allergic rhinitis (area under curve: 0.87, 95% confidence interval: 0.84-0.90) with 90% sensitivity and 89% negative predictive value.

    CONCLUSION: Inferior turbinate tissue biopsy sIgE is a sensitive tool to predict allergic rhinitis. The threshold value of 0.1 kUA/L corresponded well with the asymptomatic nonatopic group of patients. This method detects sIgE in the nasal mucosa and may be a useful test for allergic rhinitis in future research.

    Matched MeSH terms: Immunoglobulin E/analysis*; Immunoglobulin E/immunology
  8. Rosmilah M, Shahnaz M, Meinir J, Masita A, Noormalin A, Jamaluddin M
    Int Arch Allergy Immunol, 2013;162(4):299-309.
    PMID: 24193115 DOI: 10.1159/000354544
    The longtail tuna (Thunnus tonggol) is widely consumed in Asia. Parvalbumin, the main major allergen of fish, has been well identified in multiple fish species, yet little is known about the allergenic proteins in T. tonggol. Thus, the aim of this study was to characterize the major allergens of T. tonggol using a proteomics approach.
    Matched MeSH terms: Immunoglobulin E/blood; Immunoglobulin E/immunology
  9. Reginald K, Tan CL, Chen S, Yuen L, Goh SY, Chew FT
    Sci Rep, 2018 08 06;8(1):11743.
    PMID: 30082894 DOI: 10.1038/s41598-018-30224-z
    We previously identified an expressed sequence tag clone, Der f 22, showing 41% amino acid identity to published Der f 2, and show that both genes are possible paralogues. The objective of this study was to characterize the genomic, proteomic and immunological functions Der f 22 and Der f 2. The full-length sequence of Der f 2 and Der f 22 coded for mature proteins of 129 and 135 amino acids respectively, both containing 6 cysteine residues. Phylogenetic analysis of known group 2 allergens and their homologues from our expressed sequence tag library showed that Der f 22 is a paralogue of Der f 2. Both Der f 2 and Der f 22 were single gene products with one intron. Both allergens showed specific IgE-binding to over 40% of the atopic patients, with limited of cross-reactivity. Both allergens were detected at the gut region of D. farinae by immunostaining. Der f 22 is an important allergen with significant IgE reactivity among the atopic population, and should be considered in the diagnostic panel and evaluated as future hypoallergen vaccine therapeutic target.
    Matched MeSH terms: Immunoglobulin E/metabolism; Immunoglobulin E/chemistry
  10. Goh DL, Chua KY, Chew FT, Liang RC, Seow TK, Ou KL, et al.
    J Allergy Clin Immunol, 2001 Jun;107(6):1082-7.
    PMID: 11398089
    BACKGROUND: We have previously described anaphylaxis induced by edible bird's nest (BN) and demonstrated that this condition is IgE mediated.

    OBJECTIVES: This study aimed at describing the immunochemical properties of the BN allergens. Comparative studies between 3 commercially available sources (according to the country of origin) of BN were also made.

    METHODS: Crude extracts of commercially available processed BN from Sarawak (Malaysia), Thailand, and Indonesia and fresh unprocessed BN from the caves of Sarawak were obtained by means of aqueous extraction. Specific IgE toward these sources were determined by using fluorescence allergosorbent tests (FASTs). Cross-reactivity studies between the 3 sources of commercially available processed BN were carried out by means of FAST inhibition. Immunochemical characterization by means of IgE immunoblot, periodate treatment, and heat stability studies were carried out on fresh unprocessed BN from Sarawak.

    RESULTS: Serum from allergic patients showed differences in IgE binding to the 3 sources of commercially available BN, with the highest levels of specific IgE recorded with the Sarawak source (P

    Matched MeSH terms: Immunoglobulin E/blood; Immunoglobulin E/immunology; Immunoglobulin E/metabolism
  11. Roslan Abdul Rahman, Fadzilah Ismail, Roszalina Ramli, Ghazali Mat Nor, Sha Primuharsa Putra
    MyJurnal
    Kimura's disease is a chronic inflammatory disorder which affects the subcutaneous tissues of the head and neck, axilla and upper limb as well as the groin region. In the head and neck region, major salivary glands and regional lymph nodes are mainly involved with associated eosinophilia and an elevated IgE concentration. Three cases of Kimura's disease involving the parotid glands, lymph nodes and cheek are presented with a brief review of the literature.
    Matched MeSH terms: Immunoglobulin E
  12. Kok A, Robinson MJ
    Lancet, 1976 Sep 18;2(7986):633.
    PMID: 61371
    Matched MeSH terms: Immunoglobulin E
  13. Hamizan AW, Azer M, Alvarado R, Earls P, Barham HP, Tattersall J, et al.
    Am J Rhinol Allergy, 2019 Sep;33(5):524-530.
    PMID: 31106562 DOI: 10.1177/1945892419850750
    Matched MeSH terms: Immunoglobulin E/blood; Immunoglobulin E/immunology; Immunoglobulin E/metabolism
  14. Pang SL, Ho KL, Waterman J, Rambo RP, Teh AH, Mathavan I, et al.
    Sci Rep, 2019 Mar 20;9(1):4933.
    PMID: 30894561 DOI: 10.1038/s41598-019-40879-x
    Group 21 and 5 allergens are homologous house dust mite proteins known as mid-tier allergens. To reveal the biological function of group 21 allergens and to understand better the allergenicity of the rDer f 21 allergen, we determined the 1.5 Å crystal structure of rDer f 21 allergen from Dermatophagoides farinae. The rDer f 21 protein consists of a three helical bundle, similar to available structures of group 21 and homologous group 5 allergens. The rDer f 21 dimer forms a hydrophobic binding pocket similar to the one in the Der p 5 allergen, which indicates that both of the homologous groups could share a similar function. By performing structure-guided mutagenesis, we mutated all 38 surface-exposed polar residues of the rDer f 21 allergen and carried out immuno-dot blot assays using 24 atopic sera. Six residues, K10, K26, K42, E43, K46, and K48, which are located in the region between the N-terminus and the loop 1 of rDer f 21 were identified as the major IgE epitopes of rDer f 21. Epitope mapping of all potential IgE epitopes on the surface of the rDer f 21 crystal structure revealed heterogeneity in the sIgE recognition of the allergen epitopes in atopic individuals. The higher the allergen-sIgE level of an individual, the higher the number of epitope residues that are found in the allergen. The results illustrate the clear correlation between the number of specific major epitope residues in an allergen and the sIgE level of the atopic population.
    Matched MeSH terms: Immunoglobulin E
  15. Ibrahim ZH, Al-Diwan JK
    Med J Malaysia, 2023 Nov;78(6):717-720.
    PMID: 38031212
    INTRODUCTION: Coronavirus disease 2019 (COVID-19) has high morbidity and mortality especially in preexisting risk groups. In atopic diseases the IgE and eosinophils are commonly elevated. This study aims to determine the potential association between COVID-19 and atopic diseases in Iraqi patients.

    MATERIALS AND METHODS: A cross-sectional study done in Baghdad on 112 patients who attended Al-Zahraa Allergic Center. Their demographic characteristics, total IgE, eosinophil counts and PCR result for COVID-19 were determined.

    RESULTS: The means for IgE and eosinophils were 245.7±260.1IU/ml and 444.5±117.1cells/microliter sequentially. Around 32.1% had high IgE level (i.e., atopic) and 11.6% had COVID-19. Among the atopic patients, 33.3%, 30.5% and 36.2% had atopic dermatitis, allergic rhinitis and asthma respectively. More than half (58.3%) of them were male, 55.5% aged <45 years, 36.2% were retired or had no job, 69.5% were graduated from secondary school or more and 88.8% lived in urban areas. There is no significant association in IgE level between those with and without COVID-19, which means that exposure to SARS Cov2 virus could not be a trigger or exacerbation for atopic diseases. Also, there was no association between atopic patients with COVID-19 and those without it regarding type of atopy, age, sex, occupation, education, type of living area.

    CONCLUSIONS: Atopy is not a risk factor for COVID-19.

    Matched MeSH terms: Immunoglobulin E
  16. Othman SK, Daud KM, Othman NH
    Malays J Med Sci, 2011 Oct;18(4):88-90.
    PMID: 22589678
    Kimura's disease is a rare condition and typically presents as non-tender subcutaneous swellings in the head and neck region, usually in the pre-auricular and submandibular areas. It is associated with lymphadenopathy (both local and distal), marked peripheral eosinophilia, and an elevated IgE level. It can easily be mistaken for a malignant disorder. Fine needle aspiration can be misleading, and a diagnosis is established only by histopathological examination. Renal involvement, which may affect up to 60% of patients, is the only systemic manifestation. We report a case of Kimura's disease in a Malay patient who was associated with steroid-responsive nephrotic syndrome.
    Matched MeSH terms: Immunoglobulin E
  17. Misnan R, Murad S, Jones M, Taylor G, Rahman D, Arip M, et al.
    Asian Pac J Allergy Immunol, 2008 Dec;26(4):191-8.
    PMID: 19317337
    The purpose of this study was to characterize major allergens of Indian scad (Decapterus russelli) which is among the most commonly consumed fish in Malaysia. Raw and cooked extracts of the fish were prepared. Protein profiles and IgE binding patterns were produced by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting using sera from subjects with fish allergy. The major allergens of the fish were then identified by two-dimensional electrophoresis (2-DE), followed by mass spectrometry of the peptide digests. The SDS-PAGE of the raw extract revealed 27 protein fractions over a wide molecular weight range, while the cooked extract demonstrated only six protein fractions. The 1-DE immunoblotting detected 14 IgE-binding proteins, with a molecular weight range from 90 to < 6.5 kDa. Three protein fractions with molecular weights of approximately 51, 46 and 12 kDa were identified as the major allergens of this fish. The approximately 12 kDa band was a heat-resistant protein while the approximately 51 and 46 kDa proteins were sensitive to heat. The 2-DE gel profile of the raw extract demonstrated > 100 distinct protein spots and immunoblotting detected at least 10 different major IgE reactive spots with molecular masses as expected and isoelectric point (pI) values ranging from 4.0 to 7.0. A comparison of the major allergenic spot sequences of the 12 kDa proteins with known protein sequences in databases revealed extensive similarity with fish parvalbumin. In conclusion, this study demonstrated that a parvalbumin which is similar to Gad c 1 is the major allergen of Indian scad. Interestingly, we also detected heat-sensitive proteins as major allergenic components in our fish allergy patients.
    Matched MeSH terms: Immunoglobulin E/blood*
  18. Yadav A, Naidu R
    Allergol Immunopathol (Madr), 2013 Nov-Dec;41(6):364-8.
    PMID: 23276420 DOI: 10.1016/j.aller.2012.08.007
    Cord IgE and ECP levels are major atopic markers implicated in early childhood allergy development. Most epidemiological studies to date have not utilised current technology to establish baseline cord IgE levels, further aggravated by lack of data in this region. This study also attempts to identify a relationship between cord IgE and ECP levels as a mean to improve sensitivity for early prediction of atopy.
    Matched MeSH terms: Immunoglobulin E/blood*
  19. Kurup VP, Kelly KJ, Turjanmaa K, Alenius H, Reunala T, Palosuo T, et al.
    J Allergy Clin Immunol, 1993 Jun;91(6):1128-34.
    PMID: 8509575
    BACKGROUND: Patients with latex sensitivity and latex antigens from the United States and Finland, two countries where allergic reactions to latex have been widely reported, were evaluated to determine the spectrum of immune responses.

    METHODS: Sera from 27 patients from Finland and 18 from the United States with latex allergy and control sera from nonsensitive individuals were studied for latex-specific IgE antibodies. Four antigen preparations were used: two extracted from gloves and one each extracted from rubber tree sap from Malaysia and India. All 45 patients had skin prick test results that were positive to latex antigens, and all sera were evaluated by enzyme-linked immunosorbent assay (ELISA) with the various antigens.

    RESULTS: There were considerable differences in the reactivity of patient sera with the different antigens. Only 50% of the sera from patients with latex allergy from Finland demonstrated significant levels of IgE to latex as determined by enzyme-linked immunosorbent assay. These patients showed more reactivity with rubber tree sap antigens than with glove antigens. However, 72% of the patients from the United States demonstrated antibodies to latex, and no marked differences were noted between the antigen extracts.

    CONCLUSIONS: The results indicate that reagents such as rubber tree sap, which contain multiple clinically significant antigenic components, should be included in evaluation of latex allergy and that differences in patient populations may result in serologic variances.

    Matched MeSH terms: Immunoglobulin E/blood*
  20. Lim SB, Chua CT, Hashim OH
    J Immunol Methods, 1997 Dec 01;209(2):177-86.
    PMID: 9461333
    A mannose-binding lectin, termed champedak lectin-M, was isolated from an extract of the crude seeds of champedak (Artocarpus integer). On gel filtration chromatography, the lectin eluted in a single peak at elution volumes corresponding to 64 kDa. SDS-PAGE showed the mannose-binding lectin to be composed of 16.8 kDa polypeptides with some of the polypeptides being disulphide-linked to give dimers. When tested with all isotypes of immunoglobulins, champedak lectin-M demonstrated a selective strong interaction with human IgE and IgM, and a weak interaction with IgA2. The binding interactions of lectin-M were metal ion independent. The lectin was also shown to interact with horseradish peroxidase, ovalbumin, porcine thyroglobulin, human alpha1-acid glycoprotein, transferrin and alpha1-antitrypsin. It demonstrated a binding preference to Man alpha 1-3Man ligands in comparison to Man alpha 1-6Man or Man alpha 1-2Man.
    Matched MeSH terms: Immunoglobulin E/metabolism*
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