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Fulltext Absence of milk-specific IgE in infants with cow's milk protein-sensitive enteropathy

Yadav M, Iyngkaran N, Seow IKG

Med J Malaysia, 1983 Dec;38(4):266-71.
PMID: 6599980

Infants, one to 56-weeks-old, presenting with persistent diarrhoea were placed on a diet free of cow's milk protein which improved their clinical condition. Six weeks later, 67 infants were challenged with a low-lactose cow's milk formula and jejunal biopsy was taken before and 24-hours after challenge. On the basis of histological changes in the intestinal mucosa and development of clinical symptoms the infants were categorised into three groups: Group 1 (n = 16) with no clinical or mucosal abnormality, Group 2 (n = 20) with mucosal abnormality but lacking clinical symptoms, and Group 3 (n 31) with manifestation of mucosal abnormality and clinical symptoms. In addition to the total IgE the radioallergosorbent test (RAST) was performed on sera from the infants taken before and after milk provocation. The mean total serum IgE level ranged from 288 to 560 IU/ml. In Groups 2 and 3 the prechallenge serum IgE levels were significantly higher than the postchallenge levels but in Group 1 the levels remained unchanged on challenge. A positive RAST to milk proteins was observed in five infants (7.4%), that is, one in Group 2 and four in Group 3, of 67 infants studied. In a survey of 405 consecutive paediatric-age patients admitted for a variety of symptoms, 90 were positive for RAST specific for milk proteins. Interestingly the majority of the patients positive for RAST presented with gastrointestinal ailments. The measurement of specific IgE appears not to be a useful adjunct in the diagnosis of CMPSE in Malaysian children.

Matched MeSH terms: Food Hypersensitivity/immunology*
Allergen concentration in natural rubber latex

Yeang HY, Hamilton RG, Bernstein DI, Arif SA, Chow KS, Loke YH, et al.

Clin Exp Allergy, 2006 Aug;36(8):1078-86.
PMID: 16911364 DOI: 10.1111/j.1365-2222.2006.02531.x

BACKGROUND:
Hevea brasiliensis latex serum is commonly used as the in vivo and in vitro reference antigen for latex allergy diagnosis as it contains the full complement of latex allergens.

OBJECTIVE:
This study quantifies the concentrations of the significant allergens in latex serum and examines its suitability as an antigen source in latex allergy diagnosis and immunotherapy.

METHODS:
The serum phase was extracted from centrifuged latex that was repeatedly freeze-thawed or glycerinated. Quantitation of latex allergens was performed by two-site immunoenzymetric assays. The abundance of RNA transcripts of the latex allergens was estimated from the number of their clones in an Expressed Sequence Tags library.

RESULTS:
The latex allergens, Hev b 1, 2, 3, 4, 5, 6, 7 and 13, were detected in freeze-thawed and glycerinated latex serum at levels ranging from 75 (Hev b 6) to 0.06 nmol/mg total proteins (Hev b 4). Hev b 6 content in the latex was up to a thousand times higher than the other seven latex allergens, depending on source and/or preparation procedure. Allergen concentration was reflected in the abundance of mRNA transcripts. When used as the antigen, latex serum may bias the outcome of latex allergy diagnostic tests towards sensitization to Hev b 6. Tests that make use of latex serum may fail to detect latex-specific IgE reactivity in subjects who are sensitized only to allergens that are present at low concentrations.

CONCLUSION:
Latex allergy diagnostics and immunotherapy that use whole latex serum as the antigen source may not be optimal because of the marked imbalance of its constituent allergens.

Matched MeSH terms: Latex Hypersensitivity/immunology
Allergenic proteins of natural rubber latex

Yeang HY, Arif SA, Yusof F, Sunderasan E

Methods, 2002 May;27(1):32-45.
PMID: 12079415 DOI: 10.1016/S1046-2023(02)00049-X

As the living cytoplasm of laticiferous cells, Hevea brasiliensis latex is a rich blend of organic substances that include a mélange of proteins. A small number of these proteins have given rise to the problem of latex allergy. The salient characteristics of H. brasiliensis latex allergens that are recognized by the International Union of Immunological Societies (IUIS) are reviewed. These are the proteins associated with the rubber particles, the cytosolic C-serum proteins and the B-serum proteins that originate mainly from the lutoids. Procedures for the isolation and purification of latex allergens are discussed, from latex collection in the field to various preparative approaches adopted in the laboratory. As interest in recombinant latex allergens increases, there is a need to validate recombinant proteins to ascertain equivalence with their native counterparts when used in immunological studies, diagnostics, and immunotherapy.

Matched MeSH terms: Latex Hypersensitivity/immunology*
Fulltext Atopic sensitization of children with rhinitis in Malaysia

Gendeh BS, Mujahid SH, Murad S, Rizal M

Med J Malaysia, 2004 Oct;59(4):522-9.
PMID: 15779586 MyJurnal

Atopy is defined as the genetic propensity to develop immunoglobulin E antibodies in response to exposure to allergens and assessed by skin prick test (SPT) responses to common allergens, which may contribute to the development of the clinical disorders (phenotype). Although it is generally agreed that atopy is an important risk factor for allergic diseases such as asthma, rhinitis, and eczema, the extent to which atopy accounts for these diseases is controversial. One hundred forty one children (up to 12 years) were skin prick tested to evaluate 16 foods common to the Malaysian diet and 4 common aeroallergens. Eighty-five percent of patients had positive SPT reactivity. The most commonly implicated aeroallergen and food allergen was house dust mite (HDM) and Prawn. Seventy percent had positive SPT reactivity results to HDM and 24.8% to prawns. Fifty five percent were positive to more than one allergen and 17.7% positive to single aeroallergen. The prevalence of atopy in children with history of eczema was 90%. The incidence of HDM and food allergy especially crabs and prawns, is significantly greater in Malaysian Children with rhinitis symptoms.

Matched MeSH terms: Food Hypersensitivity/immunology
Characterization of glutathione S-transferase from dust mite, Der p 8 and its immunoglobulin E cross-reactivity with cockroach glutathione S-transferase

Huang CH, Liew LM, Mah KW, Kuo IC, Lee BW, Chua KY

Clin Exp Allergy, 2006 Mar;36(3):369-76.
PMID: 16499649

Sensitization to mite and cockroach allergens is common, and diagnosis and therapy of allergy can be further complicated by the presence of allergen isoforms and panallergens. Purified recombinant and native allergens are useful for studies to resolve such problems.

Matched MeSH terms: Hypersensitivity/immunology
Cloning, expression, and characterization of recombinant Hev b 3, a Hevea brasiliensis protein associated with latex allergy in patients with spina bifida

Wagner B, Krebitz M, Buck D, Niggemann B, Yeang HY, Han KH, et al.

J Allergy Clin Immunol, 1999 Nov;104(5):1084-92.
PMID: 10550757

BACKGROUND: Two natural rubber latex proteins, Hev b 1 and Hev b 3, have been described in spina bifida (SB)-associated latex allergy.
OBJECTIVE: The aim of this study was to clone and express Hev b 3 and to obtain the immunologic active and soluble recombinant allergen for diagnosis of SB-associated latex allergy.
METHODS: A complementary DNA (cDNA) coding for Hev b 3 was amplified from RNA of fresh latex collected from Malaysian rubber trees (Hevea brasiliensis). PCR primers were designed according to sequences of internal peptide fragments of natural (n) Hev b 3. The 5'-end sequence was obtained by specific amplification of cDNA ends. The recombinant (r) Hev b 3 was produced in Escherichia coli as a 6xHis tagged protein. Immunoblotting and inhibition assays were performed to characterize the recombinant allergen.
RESULTS: An Hev b 3 cDNA clone of 922 bp encoding a protein of 204 amino acid residues corresponding to a molecular weight of 22.3 kd was obtained. In immunoblots 29/35, latex-allergic patients with SB revealed IgE binding to rHev b 3, as did 4 of 15 of the latex-sensitized group. The presence of all IgE epitopes on rHev b 3 was shown by its ability to abolish all IgE binding to nHev b 3. Hev b 3 is related to Hev b 1 by a sequence identity of 47%. Cross-reactivity between these 2 latex allergens was illustrated by the large extent of inhibition of IgE binding to nHev b 1 by rHev b 3.
CONCLUSION: rHev b 3 constitutes a suitable in vitro reagent for the diagnosis of latex allergy in patients with SB. The determination of the full sequence of Hev b 3 and the production of the recombinant allergen will allow the epitope mapping and improve diagnostic reagents for latex allergy.

Matched MeSH terms: Latex Hypersensitivity/immunology*
Cord IgE and ECP levels of Malay neonates

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: Hypersensitivity/immunology
Current Trend in Immunotherapy for Peanut Allergy

Joo Chan C, Richardo T, Lim RLH

Int Rev Immunol, 2018;37(6):279-290.
PMID: 30638084 DOI: 10.1080/08830185.2018.1509967

Peanut allergy is a hypersensitivity reaction with symptoms varying from mild to severe anaphylaxis, tends to be lifelong and very few are able to outgrow this allergy. The prevalence of peanut allergy is highest among the Western countries and over the past decade, a 3.5 fold increase in prevalence of peanut allergy was reported among children in the United States. Increasing prevalence has also been observed among the Asian countries. As with other food allergies, peanut allergy reduces quality of life for the affected individuals and the social and economy burden of healthcare for peanut allergy is substantial. To date, there is no effective treatment for peanut allergy and disease management is by avoidance or relieve of symptoms via administration of epinephrine. Peanut allergy is a type-1 hypersensitivity reaction due to specific IgE production by activated T-helper type 2 (TH2) cells. Studies on various immunotherapy routes such as oral immunotherapy (OIT), sublingual immunotherapy and epicutaneous immunotherapy trials using peanut have shown the ability to induce desensitisation, shifting the allergen-specific cytokine production away from a TH2 respond. In the recent years, lactic acid bacteria probiotics have been reported to down-regulate allergy due to its inherent immunomodulatory properties. Wild-type probiotic in combination with peanut proteins or recombinant probiotics harbouring peanut allergens have been explored for OIT due to its ability to down-regulate allergen-specific-IgE production and the TH2 responses, while increasing the beneficiary population of TH1 regulatory T cells (Treg). This review discusses the current strategies in immunotherapy for peanut allergy.

Matched MeSH terms: Peanut Hypersensitivity/immunology
Detection of immunoglobulin antibodies in the sera of patients using purified latex allergens

Kurup VP, Yeang HY, Sussman GL, Bansal NK, Beezhold DH, Kelly KJ, et al.

Clin Exp Allergy, 2000 Mar;30(3):359-69.
PMID: 10691894

BACKGROUND: Latex allergy is largely an occupational allergy due to sensitization to natural rubber latex allergens present in a number of health care and household products. Although several purified allergens are currently available for study, information on the usefulness of these purified, native or recombinant allergens in the demonstration of specific immunoglobulin (Ig) E in the sera of patients is lacking.
OBJECTIVE: To evaluate the purified latex allergens and to demonstrate specific IgE antibody in the sera of health care workers and spina bifida patients with clinical latex allergy.
METHODS: Two radioallergosorbent and an enzyme-linked immunosorbent assay (ELISA) using latex proteins Hev b 1, 2, 3, 4, 6 and 7 along with two glove extracts and Malaysian nonammoniated latex (MNA) were evaluated to demonstrate IgE in the sera of health care workers and spina bifida with latex allergy and controls with no history of latex allergy.
RESULTS: ELISA using the purified latex allergens demonstrated specific IgE in 32-65% health care workers and 54-100% of spina bifida patients with latex allergy. The corresponding figures for RAST were 13-48 and 23-85 for RAST-1 and 19-61 and 36-57 for RAST-2. These results were comparable with the results obtained with glove extracts and crude rubber latex proteins.
CONCLUSIONS: When used simultaneously, latex proteins Hev b 2 and Hev b 7 reacted significantly with specific serum IgE in 80% of health care workers and 92% of spina bifida patients with latex allergy by ELISA technique, while this combination gave lower positivity when the RASTs were used. By the addition of Hev b 3, specific IgE was detected in all spina bifida patients with latex allergy. Both RASTs failed to show specific IgE in the control subjects, while the ELISA showed significant latex-specific IgE in 22% of controls.

Matched MeSH terms: Latex Hypersensitivity/immunology*
Distinct "Immunoallertypes" of Disease and High Frequencies of Sensitization in Non-Cystic Fibrosis Bronchiectasis

Mac Aogáin M, Tiew PY, Lim AYH, Low TB, Tan GL, Hassan T, et al.

Am J Respir Crit Care Med, 2019 04 01;199(7):842-853.
PMID: 30265843 DOI: 10.1164/rccm.201807-1355OC

RATIONALE: Allergic sensitization is associated with poor clinical outcomes in asthma, chronic obstructive pulmonary disease, and cystic fibrosis; however, its presence, frequency, and clinical significance in non-cystic fibrosis bronchiectasis remain unclear.
OBJECTIVES: To determine the frequency and geographic variability that exists in a sensitization pattern to common and specific allergens, including house dust mite and fungi, and to correlate such patterns to airway immune-inflammatory status and clinical outcomes in bronchiectasis.
METHODS: Patients with bronchiectasis were recruited in Asia (Singapore and Malaysia) and the United Kingdom (Scotland) (n = 238), forming the Cohort of Asian and Matched European Bronchiectasis, which matched recruited patients on age, sex, and bronchiectasis severity. Specific IgE response against a range of common allergens was determined, combined with airway immune-inflammatory status and correlated to clinical outcomes. Clinically relevant patient clusters, based on sensitization pattern and airway immune profiles ("immunoallertypes"), were determined.
MEASUREMENTS AND MAIN RESULTS: A high frequency of sensitization to multiple allergens was detected in bronchiectasis, exceeding that in a comparator cohort with allergic rhinitis (n = 149). Sensitization was associated with poor clinical outcomes, including decreased pulmonary function and more severe disease. "Sensitized bronchiectasis" was classified into two immunoallertypes: one fungal driven and proinflammatory, the other house dust mite driven and chemokine dominant, with the former demonstrating poorer clinical outcome.
CONCLUSIONS: Allergic sensitization occurs at high frequency in patients with bronchiectasis recruited from different global centers. Improving endophenotyping of sensitized bronchiectasis, a clinically significant state, and a "treatable trait" permits therapeutic intervention in appropriate patients, and may allow improved stratification in future bronchiectasis research and clinical trials.

Matched MeSH terms: Hypersensitivity/immunology
Effect of histamine on lecithin content in broncho-alveolar lavage fluid of rat

Janardhana Rao G

Asian Pac J Allergy Immunol, 1997 Jun;15(2):77-80.
PMID: 9346270

Deficiency of surfactant in alveoli leads to increased resistance to breathing. Histamine is a mediator in allergic respiratory diseases. Though the bronchoconstrictor effect of histamine is well recognised, histamine may have additional actions that contribute to pathogenesis in these diseases. The present study aimed to observe the effect of histamine on lecithin, a major component of alveolar surfactant. Lecithin content in broncho-alveolar lavage (BAL) fluid of healthy adult male rats was estimated by enzymatic method using Boehringer-Mannheim kits. Lecithin content in these control animals was compared with that in three groups of healthy adult male rats following subcutaneous administration of 0.06 mg of histamine diphosphate at 10 minutes, 30 minutes and 60 minutes intervals, respectively. A significant reduction in lecithin levels in BAL fluid was observed up to one hour after administration of histamine. The results indicate a possible additional action of histamine in the pathogenesis of allergic respiratory diseases.

Matched MeSH terms: Respiratory Hypersensitivity/immunology
Evaluation of the MAST CLA allergy system for diagnosis of allergies to house dust mites and cats

Ho TM, DeBruynne J, Ahamad M, Darussamin H

Asian Pac J Allergy Immunol, 1997 Sep;15(3):123-6.
PMID: 9438543

The MAST CLA system was evaluated against skin prick test (SPT) for diagnosis of allergies to house dust mites (Dermatophagoides pteronyssinus, Dermatophagoides farinae) and cats. Forty three asthmatic children were examined by SPT and MAST CLA. Chi-square analysis indicated significant association between SPT and MAST CLA results for the house dust mites but not for cats. The sensitivities of MAST CLA for house dust mites and cats were 100 and 25% respectively; specificities were all less than 50%. The efficiency of MAST CLA for detection of allergy to the house dust mites was 88% and 44% for cats. A significant linear correlation was found between SPT wheal size and MAST CLA grade for D. farinae but not for D. pteronyssinus and cats. It is concluded that the MAST CLA allergy system can be used to supplement SPT for diagnosis of allergies to house dust mites but not to cats.

Matched MeSH terms: Hypersensitivity/immunology
Expression of a codon-optimised recombinant Ara h 2.02 peanut allergen in Escherichia coli

Lew MH, Lim RL

Appl Microbiol Biotechnol, 2016 Jan;100(2):661-71.
PMID: 26411458 DOI: 10.1007/s00253-015-6953-y

Current diagnostic tools for peanut allergy using crude peanut extract showed low predictive value and reduced specificity for detection of peanut allergen-specific immunoglobulin E (IgE). The Ara h 2.02, an isoform of the major peanut allergen Ara h 2, contains three IgE epitope recognition sequence of 'DPYSPS' and may be a better reagent for component resolve diagnosis. This research aimed to generate a codon-optimised Ara h 2.02 gene for heterologous expression in Escherichia coli and allergenicity study of this recombinant protein. The codon-optimised gene was generated by PCR using overlapping primers and cloned into the pET-28a (+) expression vector. Moderate expression of a 22.5 kDa 6xhistidine-tagged recombinant Ara h 2.02 protein (6xHis-rAra h 2.02) in BL21 (DE3) host cells was observed upon induction with 1 mM isopropyl β-D-1-thiogalactopyranoside (IPTG). The insoluble recombinant protein was purified under denaturing condition using nickel-nitrilotriacetic acid (Ni-NTA) affinity chromatography and refolded by dialysis in decreasing urea concentration, amounting to a yield of 74 mg/l of expression culture. Matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) and immunoblot analysis confirmed the production of the recombinant 6xHis-rAra h 2.02. The refolded recombinant 6xHis-rAra h 2.02, with or without adjuvant, was able to elicit comparable level of allergen-specific IgE and IgG1 in sensitised Balb/c mice. In addition, the specific IgE antibodies raised against the recombinant protein were able to recognise the native Ara h 2 protein, demonstrating its allergenicity and potential as a reagent for diagnosis and therapeutic study.

Matched MeSH terms: Peanut Hypersensitivity/immunology
FeNO level and allergy status among school children in Terengganu, Malaysia

Ma'pol A, Hashim JH, Norbäck D, Weislander G, Hashim Z, Isa ZM

J Asthma, 2020 08;57(8):842-849.
PMID: 31155989 DOI: 10.1080/02770903.2019.1614614

Background: Almost one third of the world population suffers from allergic conditions. Respiratory symptoms are common in Malaysian children but there are few studies on fractional exhaled nitric oxide (FeNO), inclusive of field clinical test for asthma among children in Malaysia. The aim was to provide insight on factors related to level of FeNO among students in Terengganu, Malaysia.Methods: In total, 487 randomly selected students from eight secondary schools participated (13-14 years old). A Standardized questionnaire was used to obtained information on doctors' diagnosed asthma, current asthma and respiratory symptoms. FeNO measurement and skin prick test (SPT to common allergen) were conducted.Results: The geometric mean FeNO was 16.7 ppb. Totally, 38.4% of students had elevated FeNO level (>20 ppb) and 40.3% had had positive SPT to house dust mites allergens (HDM), Dermatophagoides pteronyssinus (Der p 1), Dermatophagoides farinae (Der f 1) or Felis domisticus (cat). Male gender, height, parental history of allergy, self-reported allergy, and atopy were associated with FeNO. In particular, a combination of sensitization to HDM or cat and elevated FeNO were associated with doctor-diagnosed asthma and self-reported allergy to food, pollen and cat.Conclusion: Asthma, respiratory symptoms and sensitization to HDM and cat are common among students and presence of elevated FeNO levels indicate ongoing airway inflammation.

Matched MeSH terms: Hypersensitivity/immunology
First report on sensitization to allergens of a house dust mite, Suidasia pontifica (Acari: Saproglyphidae)

Mariana A, Ho TM, Gendeh BS, Iskandar H, Zainuldin-Taib M

Southeast Asian J. Trop. Med. Public Health, 2000 Dec;31(4):722-3.
PMID: 11414419

A species of house dust mite, Suidasia pontifica, was recently shown to produce allergens affecting man. The species may be as important as other allergen producing mite in sensitization and causing allergic symptoms in Malaysians. Surveys conducted demonstrated that 80% of the houses surveyed were positive for this mite with densities ranged from 2 to 50 mites per gram of dust. Colonies of the species has been successfully established and materials from those colonies have been used to produce extracts for studies on sensitization to the mites. A total of 85 suspected allergic rhinitis patients were tested and 74.1% demonstrated positive reactions. Extract of this mite should be considered for routine diagnostic testing and possible immunotherapy.

Matched MeSH terms: Hypersensitivity/immunology*
Histamine induced decrease of lecithin levels in broncho-alveolar lavage fluid of rats is mediated by H2 receptor

Rao GJ

Asian Pac J Allergy Immunol, 2000 Sep;18(3):169-71.
PMID: 11270474

Lecithin, a major surface active substance of the surfactant system of the lung, was estimated in broncho-alveolar lavage (BAL) fluid in four groups of healthy adult male albino rats. Rats from group I were not administered any drug and acted as controls. Group II were administered histamine diphosphate. Group III were given H1 blocker (pyrilamine maleate) followed by histamine diphosphate. Group IV received H2 blocker (ranitidine hydrochloride) followed by histamine diphosphate. Lecithin content of BAL fluid in the control group was compared with that in the other three groups. A significant decrease in lecithin content was observed in the rats that received either histamine diphosphate or H1 blocker followed by histamine diphosphate. However, compared to control rats no significant difference in lecithin content was seen in rats that received H2 blocker followed by histamine diphosphate. The results clearly indicate that the decrease in surface active lecithin content in BAL fluid following administration of histamine diphosphate was unaffected by prior administration of H1 blocker, but was blocked by prior administration of H2 blocker. It was concluded that histamine induced decrease in lecithin content of BAL fluid is mediated through H2 receptors. Since the predominant source of intra-alveolar lecithin are Type II cells of the alveolar epithelium, It is possible that Type II cells have H2 receptors, stimulation of which resulted in decreased intraalveolar lecithin.

Matched MeSH terms: Respiratory Hypersensitivity/immunology
Identification of Ige-binding proteins of raw and cooked extracts of Loligo edulis (white squid)

Yadzir ZH, Misnan R, Abdullah N, Bakhtiar F, Arip M, Murad S

Southeast Asian J. Trop. Med. Public Health, 2010 May;41(3):653-9.
PMID: 20578555

Allergy to different classes of mollusks, including squid, which are members of the class Cephalopods has been reported. Tropomyosin, a major muscle protein, is the only well-recognized allergen in squid. The aim of this study was to characterize IgE-binding proteins of local Loligo edulis (white squid) consumed in Malaysia. Protein profiles and IgE-binding proteins were detected by sodium dodecyl sulfate-polyacrylamide gel-electrophoresis (SDS-PAGE) and immunoblotting using sera from 23 patients with positive skin prick test to raw squid extract. SDS-PAGE of the raw extract exhibited 21 protein bands (10-170 kDa) but those ranging from 19 to 29 kDa and 41 to 94 kDa were not found in the cooked extract. Immunoblotting of raw extract demonstrated 16 IgE-binding bands, ranging from 13 to 170 kDa. A heat-resistant 36 kDa protein, corresponding to squid tropomyosin, was identified as the major allergen of both extracts. In addition, a 50 kDa heat-sensitive protein was shown to be a major allergen of the raw extract. Our findings indicate that the allergen extract used for diagnosis of squid allergy should contain both the 36 kDa and 50 kDa proteins.

Matched MeSH terms: Food Hypersensitivity/immunology*
Fulltext Identification of major allergens of two species of local snappers: Lutjanus argentimaculatus (merah/ red snapper) and Lutjanus johnii (jenahak/ golden snapper)

Rosmilah M, Shahnaz M, Masita A, Noormalin A, Jamaludin M

Trop Biomed, 2005 Dec;22(2):171-7.
PMID: 16883284 MyJurnal

Fish has been recognized as a source of potent allergens both in food and occupational allergy. Lutjanus argentimaculatus (red snapper) and Lutjanus johnii (golden snapper) locally known as merah and jenahak, respectively, are among the most commonly consumed fish in Malaysia. The objective of this study is to identify the IgE-binding proteins and major allergens of these species of fishes. Extracts of both fish species were prepared and fractionated by sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE). IgE binding patterns were then demonstrated by immunoblotting using sera from patients allergic to the fishes. The raw extracts of both fish produced 26 protein bands. Both species of fishes had similar protein profiles. In cooked extracts, several protein bands in the range of about 40 to 90 kD which were present in the uncooked extracts appeared to be denatured and formed high molecular weight complexes. The immunoblotting of golden snapper and red snapper revealed 16 and 15 various IgE-binding bands, in the range of 151 to 12-11 kD, respectively. A 51 kD protein was identified as a major allergen for both fishes. A 46 kD protein was also demonstrated as a major allergen in golden snapper and a 42 kD protein was also seen as a major allergen in red snapper. A heat-resistant protein of ~12 kD which is equivalent in size with fish parvalbumin was demonstrated only as minor allergen for both fishes.

Matched MeSH terms: Food Hypersensitivity/immunology
Identification of major allergens of wildflower honey

Yadzir ZH, Misnan R, Abdullah N, Arip M, Murad S

Southeast Asian J. Trop. Med. Public Health, 2011 Mar;42(2):370-5.
PMID: 21710860

The aim of this study was to identify the major allergens of wildflower honey in local patients with atopic disease. SDS-PAGE revealed ten protein bands of 25 to 110 kDa, with a heavy cluster in region of 40-75 kDa. Immunoblotting demonstrated seven IgE-binding bands of 39 to 110 kDa. The 60 kDa protein had the highest frequency of IgE-binding (100%) followed by 54 kDa protein (95%), thus identified as the major allergens of wildflowerhoney. Our findings indicate that the allergen extract used for diagnosis of honey allergy contains both the 54 kDa and 60 kDa proteins.

Matched MeSH terms: Food Hypersensitivity/immunology*
Fulltext Identification of parvalbumin and two new thermolabile major allergens of Thunnus tonggol using a proteomics approach

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: Food Hypersensitivity/immunology*

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