MyMedR

Displaying publications 1 - 20 of 129 in total

Abstract:

Sort:

Fulltext Allergies in asthma

Zulkifli A, Ng WH, Chelvam P

Family Practitioner, 1979;3(5):32-34.

148 patients, 79 males and 60 females were seen in 1978 at Medical Unit Universiti Kebangsaan Kuala Lumpur. For majority of the patients the attacks of asthma begin at an early age. History of allergies were found in majority of the patients. Family history of asthma was noted in about 50%. Of the allergens that triggers of an attack of asthma, household dusts, rhinitis and pollen tops the list. Of the food the common allergens were shrimps, eggs and crabs. Most of the above allergens can be avoided or counteracted.
Study site: Medical Unit, Hospital Kuala Lumpur (UKM unit), Malaysia

Matched MeSH terms: Allergens
Experience with skin reactions to various allergens in bronchial asthma

Zulkifli A, Weng CK

Med J Malaysia, 1979 Dec;34(2):153-5.
PMID: 548718
Matched MeSH terms: Allergens*
Fulltext Malaysian cockle (Anadara granosa) allergy: Identification of IgE-binding proteins and effects of different cooking methods

Zailatul HM, Rosmilah M, Faizal B, Noormalin A, Shahnaz M

Trop Biomed, 2015 Jun;32(2):323-34.
PMID: 26691261 MyJurnal

The purpose of this study was to evaluate the effect of different cooking methods on the allergenicity of cockle and to identify proteins most frequently bound by IgE antibodies using a proteomics approach. Raw, boiled, fried and roasted extracts of the cockle were prepared. The protein profiles of the extracts were obtained by separation using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and 2-dimensional gel electrophoresis (2-DE). IgE-immunoblotting was then performed with the use of individual sera from patients with cockle allergy and the major IgE-binding proteins were analyzed by mass-spectrometry. SDS-PAGE of raw extract showed 13 protein bands. Smaller numbers of protein bands were detected in the boiled, fried and roasted extracts. The 2-DE gel profile of the raw extract further separated the protein bands to ~50 protein spots with molecular masses between 13 to 180 kDa and isoelectric point (pI) values ranging from 3 to 10. Immunoblotting of raw extract exhibited 11 IgE-binding proteins with two proteins of 36 and 40 kDa as the major IgE-binding proteins, while the boiled extract revealed 3 IgE-binding proteins. Fried and roasted extracts only showed a single IgE-binding protein at 36 kDa. 2-DE immunoblotting of raw extract demonstrated 5 to 20 IgE reactive spots. Mass spectrometry analysis led to identification of 2 important allergens, tropomyosin (36 kDa) and arginine kinase (40 kDa). Heated extracts showed a reduction in the number of IgE-reactive bands compared with raw extract, which suggest that thermal treatment can be used as a tool in attempting to reduce cockle allergenicity. The degree of allergenicity of cockle was demonstrated in the order raw > boiled > fried ≈ roasted. Two important allergens reacting with more than 50% of patients' sera identified using mass spectrometric approaches were tropomyosin and arginine kinase. Thus, allergens found in this study would help in component based diagnosis, management of cockle allergic patients and to the standardisation of allergenic test products as tools in molecular allergology.

Matched MeSH terms: Allergens/analysis*; Allergens/chemistry
The manufacture of gloves from natural rubber latex

Yip E, Cacioli P

J Allergy Clin Immunol, 2002 Aug;110(2 Suppl):S3-14.
PMID: 12170237 DOI: 10.1067/mai.2002.124499

Gloves that will provide a barrier of protection from infectious organisms are an essential feature of medical practice for the protection of both patients and medical personnel. Natural rubber latex has consistently been the most satisfactory raw material for the manufacture of gloves. Certain latex proteins, carried over into the finished product by inadequate manufacturing processes, may pose a risk of provoking allergic reactions in some patients and medical workers. As with any allergy, the risk depends on the route of exposure and dose. Hence, the method of manufacture, including the means used to coat gloves to make donning easy, can influence the eventual exposure of sensitive people to latex allergens. In this article, we describe the several processes in use and their effects on latex protein content.

Matched MeSH terms: Allergens/immunology; Allergens/isolation & purification
Fulltext Insight into different environmental niches adaptation and allergenicity from the Cladosporium sphaerospermum genome, a common human allergy-eliciting Dothideomycetes

Yew SM, Chan CL, Ngeow YF, Toh YF, Na SL, Lee KW, et al.

Sci Rep, 2016 05 31;6:27008.
PMID: 27243961 DOI: 10.1038/srep27008

Cladosporium sphaerospermum, a dematiaceous saprophytic fungus commonly found in diverse environments, has been reported to cause allergy and other occasional diseases in humans. However, its basic biology and genetic information are largely unexplored. A clinical isolate C. sphaerospermum genome, UM 843, was re-sequenced and combined with previously generated sequences to form a model 26.89 Mb genome containing 9,652 predicted genes. Functional annotation on predicted genes suggests the ability of this fungus to degrade carbohydrate and protein complexes. Several putative peptidases responsible for lung tissue hydrolysis were identified. These genes shared high similarity with the Aspergillus peptidases. The UM 843 genome encodes a wide array of proteins involved in the biosynthesis of melanin, siderophores, cladosins and survival in high salinity environment. In addition, a total of 28 genes were predicted to be associated with allergy. Orthologous gene analysis together with 22 other Dothideomycetes showed genes uniquely present in UM 843 that encode four class 1 hydrophobins which may be allergens specific to Cladosporium. The mRNA of these hydrophobins were detected by RT-PCR. The genomic analysis of UM 843 contributes to the understanding of the biology and allergenicity of this widely-prevalent species.

Matched MeSH terms: Allergens/genetics*; Allergens/immunology
Fulltext Exotic food anaphylaxis and the broken heart: sago worm and takotsubo cardiomyopathy

Yew KL, Kok VS

Med J Malaysia, 2012 Oct;67(5):540-1.
PMID: 23770880 MyJurnal

There is increasing consumption of exotic food in Malaysia. Animals such as insects, worms and wild life animals also form part of the staple food of the local population. This practice may lead to more incidence of food allergy and anaphylaxis. We report a non-indigenous man who developed food anaphylaxis after consuming fried sago worms and consequently Takotsubo cardiomyopathy. We postulate that certain food allergy and anaphylaxis could be another causative trigger for Takotsubo cardiomyopathy.

Matched MeSH terms: Allergens
Sensitization profiles of Malaysian and Singaporean subjects to allergens from Dermatophagoides pteronyssinus and Blomia tropicalis

Yeoh SM, Kuo IC, Wang DY, Liam CK, Sam CK, De Bruyne JA, et al.

Int Arch Allergy Immunol, 2003 Nov;132(3):215-20.
PMID: 14646382 DOI: 10.1159/000074302

BACKGROUND: The house dust mites Dermatophagoides pteronyssinus (Der p) and Blomia tropicalis (Blo t) are the most common house dust mite species in Southeast Asia. To date, there have only been a few studies on the sensitization profile of the general populations in Southeast Asia to house dust mites. The aim of this study was to determine the profiles of Der p and Blo t sensitization among Singaporean and Malaysian subjects.

METHODS: Enzyme-linked immunosorbent assay was used to detect specific IgE to Der p and Blo t mite crude extracts as well as purified Der p 1, Der p 2 and Blo t 5 allergens. Sera used were from 229 Singaporean subjects (124 with rhinitis, 105 without rhinitis) and 143 Malaysian subjects (94 adults and 49 children with asthma).

RESULTS: The sensitization profile of rhinitis subjects to the dust mite allergens used in this study was as follows: Blo t extract positive: 91/124 (73%); Blo t 5 positive: 62/124 (50%); Der p extract positive: 61/124 (49%); Der p 1 positive: 53/124 (43%); Der p 2 positive: 45/124 (36%). The nonrhinitis subjects' sensitization profile was as follows: Blo t extract positive: 60/105 (57%); Blo t 5 positive: 24/105 (23%); Der p extract positive: 38/105 (36%); Der p 1 positive: 14/105 (13%); Der p 2 positive: 17/105 (16%). The study of Malaysian asthmatic adults showed that 39% of them were sensitized to Der p 1, 32% to Der p 2 and 37% to Blo t 5. Among the asthmatic children, sensitization to Blo t 5, Der p 1 and Der p 2 was 90, 57 and 39%, respectively.

CONCLUSION: This study clearly revealed that dual sensitization to B. tropicalis and D. pteronyssinus is common in the general populations of Singapore and Malaysia. Sensitization to Blo t 5 is more prevalent than to Der p 1 and Der p 2.

Matched MeSH terms: Allergens/immunology*
Hev b 5 and Hev b 13 as allergen markers to estimate the allergenic potency of latex gloves

Yeang HY, Arif SA, Raulf-Heimsoth M, Loke YH, Sander I, Sulong SH, et al.

J Allergy Clin Immunol, 2004 Sep;114(3):593-8.
PMID: 15356563 DOI: 10.1016/j.jaci.2004.05.039

BACKGROUND:
Sensitization to natural rubber latex has been linked to proteins from medical latex gloves. Various assays to estimate the amount of residual allergenic proteins extractable from latex gloves to assess their potential exposure hazard have inherent weaknesses.

OBJECTIVE:
This investigation was aimed at developing 2-site immunoenzymetric assays and identifying appropriate protein markers to assess the allergenic potential of latex gloves.

METHODS:
The presence of 6 latex allergens--Hev b 1, 2, 3, 5, 6, and 13--was measured in a cross-section of commercial latex medical gloves by using monoclonal and polyclonal antibody-based 2-site immunoenzymetric assays. The overall allergenic potential of these gloves was assessed by IgE-inhibition assay. Stepwise multiple regression analyses were performed to identify marker allergens that best explained the variation in latex glove allergenicity.

RESULTS:
All 6 latex allergens were detected in at least some of the glove samples. Hev b 5 and Hev b 13 were identified as the marker allergens that combined best to explain the variation in the glove allergenicity. The significant multiple correlation (R=0.855) between these 2 markers and glove allergenic potency forms the basis of an assay to gauge latex glove allergenicity.

CONCLUSION:
The overall allergenic potential of latex gloves can be estimated by using Hev b 5 and Hev b 13 as indicator allergens. The correlation between glove allergenicity and the level of these allergens was maintained for low-protein gloves (<200 microg/g). This estimation of glove allergenicity was superior to that obtained by using total protein readings.

Matched MeSH terms: Allergens/adverse effects; Allergens/analysis*
Appraisal of latex glove proteins in the induction of sensitivity to multiple latex allergens

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: Allergens/adverse effects*; Allergens/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: Allergens/immunology
Amino acid sequence similarity of Hev b 3 to two previously reported 27- and 23-kDa latex proteins allergenic to spina bifida patients

Yeang HY, Ward MA, Zamri AS, Dennis MS, Light DR

Allergy, 1998 May;53(5):513-9.
PMID: 9636811

Separate studies have reported spina bifida patients to be especially allergic to proteins of 27 and 23 kDa found in the serum of centrifuged natural rubber latex. An insoluble latex protein located on the surface of small rubber particles, Hev b 3, has similarly been found to be allergenic to spina bifida patients. In this study, internal amino acid sequences of Hev b 3 showed similarity to the published sequences for the 27- and 23-kDa latex proteins. The latter allergens are hence identified as Hev b 3. Determination of the molecular weight of Hev b 3 revealed various species of 22-23 kDa. The consistent gaps of about 266 Da observed between various forms of the intact protein suggest that the protein undergoes post-translational modification. To determine whether Hev b 3 also occurs in a soluble form in the latex serum, its presence in molecular-filtered serum was checked by ELISA and Western blot. The results showed Hev b 3 to be largely absent in the C-serum from fresh latex. The protein is therefore insoluble in its native state. However, a small amount of the solubilized protein was detected in ammonia-stabilized latex (commonly used in the manufacture of latex products).

Matched MeSH terms: Allergens/genetics*; Allergens/immunology*; Allergens/chemistry
The 14.6 kd rubber elongation factor (Hev b 1) and 24 kd (Hev b 3) rubber particle proteins are recognized by IgE from patients with spina bifida and latex allergy

Yeang HY, Cheong KF, Sunderasan E, Hamzah S, Chew NP, Hamid S, et al.

J Allergy Clin Immunol, 1996 Sep;98(3):628-39.
PMID: 8828541 DOI: 10.1016/s0091-6749(96)70097-0

Two major water-insoluble proteins are located on the surface of rubber particles in Hevea brasiliensis latex. A 14.6 kd protein (Hev b 1), found mainly on large rubber particles (> 350 mm in diameter), and a 24 kd protein (Hev b 3), found mainly on small rubber particles (average diameter, 70 nm), are recognized by IgE from patients with spina bifida and latex allergy. Although Hev b 1 (also called the rubber elongation factor [REF]) has previously been reported as a major latex allergen, this conclusion has been disputed on the basis of results from other studies. The allergenicity of Hev b 1 is verified in this study by testing the recombinant protein generated from its gene. Because allergenicity is confined to patients with spina bifida and not observed in adults sensitive to latex, it is not a major latex allergen. The identification of Hev b 3 as another allergen originating from rubber particles is confirmed by immunogold labeling and electron microscopy. Observations with the monoclonal antibody USM/RC2 developed against Hev b 3 show that the protein has a tendency to fragment into several polypeptides of lower molecular weight (from 24 kd to about 5 kd) when stored at -20 degrees C. There is also indication of protein aggregation from the appearance of proteins with molecular weights greater than 24 kd. Fragmentation of Hev b 3 is induced immediately on he addition of latex B-serum, which is normally compartmentalized in the lutoids in fresh latex. In the preparation of ammoniated latex (used for the manufacture of latex products), the lutoids are ruptured, and the released B-serum reacts with Hev b 3 on the rubber particles to give rise to an array of low molecular weight polypeptides that are allergenic to patients with spina bifida.

Matched MeSH terms: Allergens/immunology*; Allergens/metabolism; Allergens/chemistry
Natural rubber latex allergens: new developments

Yeang HY

Curr Opin Allergy Clin Immunol, 2004 Apr;4(2):99-104.
PMID: 15021061

PURPOSE OF REVIEW:
New allergenic latex proteins have been identified, whereas further information on known latex allergens has emerged in recent years. Although prevalence figures for sensitization to the various latex allergens have been published in several studies in the past, the data have not been collated to facilitate cross-comparison.

RECENT FINDINGS:
Salient characteristics of the three most recently identified latex allergens, Hev b 11, 12 and 13 are described, whereas new findings on some of the previously recognized allergens are examined. Hev b 2 is viewed from the standpoint of allergenicity and protein glycosylation, Hev b 4 in relation to its biochemical identity and molecular cloning, Hev b 5 with respect to its recombinant form, and Hev b 6 in connection with conformational IgE epitopes. Reports on sensitization or allergic reaction to purified latex allergens from recent and past work are summarized. The use of latex allergens in latex allergy diagnostics is reviewed and discussed.

SUMMARY:
Thirteen latex allergens have been recognized by the International Union of Immunological Societies. Based on the results of published studies, native Hev b 2, recombinant Hev b 5, native or recombinant Hev b 6, native Hev b 13, and possibly native Hev b 4 are the major allergens relevant to latex-sensitized adults. Although there is an increasing tendency to identify and characterize latex allergens largely on the basis of their recombinant forms, not all such recombinant proteins have been fully validated against their native counterparts with respect to clinical significance.

Matched MeSH terms: Allergens/adverse effects*; Allergens/classification
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: Allergens/analysis*; Allergens/genetics; Allergens/immunology
The pattern of allergic contact hand dermatitis at a tertiary skin clinic in Sarawak, Malaysia

Yap FBB

Dermatitis, 2010 May-Jun;21(3):179-81.
PMID: 20487668
Matched MeSH terms: Allergens/classification*; Allergens/immunology
Identification of tropomyosin as major allergen of white squid (Loligo edulis) by two-dimensional immunoblotting and mass spectrometry

Yadzir ZH, Misnan R, Murad S

Southeast Asian J. Trop. Med. Public Health, 2012 Jan;43(1):185-91.
PMID: 23082569

IgE-mediated allergic reaction to squid is one of the most frequent molluscan shellfish allergies. Previously, we have detected a 36 kDa protein as the major allergen of Loligo edulis (white squid) by immunoblotting using sera from patients with squid allergy. The aim of this present study was to further identify this major allergen using a proteomics approach. The major allergen was identified by a combination of two-dimensional electrophoresis (2-DE), immunoblotting, mass spectrometry and bioinformatics tools. The 2-DE gel fractionated the cooked white squid proteins to more than 50 different protein spots between 10 to 38 kDa and isoelectric point (pI) from 3.0 to 10.0. A highly reactive protein spot of a molecular mass of 36 kDa and pI of 4.55 was observed in all of the patients' serum samples tested. Mass spectrometry analysis led to identification of this allergen as tropomyosin. This finding can contribute to advancement in component-based diagnosis, management of squid allergic patients, to the development of immunotherapy and to the standardization of allergenic test products as tools in molecular allergology.

Matched MeSH terms: Allergens/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: Allergens/adverse effects; Allergens/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: Allergens/blood; Allergens/isolation & purification*
Fulltext Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn)

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

Asian Pac J Trop Biomed, 2012 Jan;2(1):50-4.
PMID: 23569834 DOI: 10.1016/S2221-1691(11)60189-5

OBJECTIVE: To characterize the major allergens of Macrobrachium rosenbergii (giant freshwater prawn).
METHODS: Raw and cooked extracts of the giant freshwater prawn were prepared. The IgE reactivity pattern was identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting technique with the sera of 20 skin prick test (SPT) positive patients. The major allergen identified was then characterized using the proteomics approach involving a combination of two-dimensional (2-DE) electrophoresis, mass spectrometry and bioinformatics tools.
RESULTS: SDS-PAGE of the raw extract showed 23 protein bands (15-250 kDa) but those ranging from 40 to 100 kDa were not found in the cooked extract. From immunoblotting experiments, raw and cooked extracts demonstrated 11 and 5 IgE-binding proteins, respectively, with a molecular mass ranging from 15 to 155 kDa. A heat-resistant 36 kDa protein was identified as the major allergen of both extracts. In addition, a 42 kDa heat-sensitive protein was shown to be a major allergen of the raw extract. The 2-DE gel fractionated the prawn proteins to more than 50 different protein spots. Of these, 10 spots showed specific IgE reactivity with patients' sera. Matrix assisted laser desorption/ionization-time of flight (MALDI-TOF) analysis led to identification of 2 important allergens, tropomyosin and arginine kinase.
CONCLUSIONS: It can be concluded that the availability of such allergens would help in component-based diagnosis and therapy of prawn allergies.

Matched MeSH terms: Allergens/isolation & purification*
Childhood rhinitis is predominantly associated with mite allergens

Yadav, M., Harnam, S.

Malaysian Journal of Child Health, 1998;10(1):19-27.
MyJurnal

The total and allergen-specific IgE response of patients with rhinitis, rhinoconjunctivities, rhinitis with asthma and rhinitis with dermatitis was analyzed to a panel of twelve high risk airborne and food allergens. It has been found that this panel will detect 96 percent of the allergen-causing diseases in children. It was found that 26 (76%) of the 34 young patients had a family history for atopy suggesting a high frequency of inheritance of allergic disorders. Elevated total IgE was found in most patients with allergic disease. Positive IgE antibody response to two species of Dermatophagoides mite-allergens was found in 7/12 (58%) patients with rhinitis, 11/11 (100%) patients with rhinoconjunctivitis, 7/9 (78%) cases ofrhinitis with asthma and 3/3 (100%) cases of rhinitis with dermatitis. Some of the patients also responded to food allergens. Food allergy was noted in 4/12 (33%) cases of rhinitis, 11/11 (100%) cases of rhinoconjunctivitis, 4/9 (44%) cases of rhinitis with asthma and 1/3 (33%) cases of rhinitis with dermatitis. Patients with rhinoconjunctivitis who tested positive at high titres for mites invariably had enhanced response for cockroaches, shrimps and crabs suggesting invertebrate antigen cross-reactivity. A few patients however, did not show this type of cross-reactivity although they had high titres of anti-mite IgE antibodies indicating that they responded to non cross-reacting allergen epitopes. Response to multiple allergens appears to be a common feature of most patients with respiratory or skin allergic diseases. The prevalence of multiple target-organ allergy to wide variety offood and environmental allergens complicates the long term management ofpatients with such allergic disorders.

Matched MeSH terms: Allergens

Filters

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links