Search PubMed⌕ Search

Biomedical subjects

H Alenius

Publications and source records attributed to H Alenius.

At least 37 records · Page 2Linked to original sources
PubMed1999

Identification of patatin as a novel allergen for children with positive skin prick test responses to raw potato.

BACKGROUND: Peeling of raw potatoes may cause allergic symptoms, such as sneezing, wheezing, and contact urticaria, for adults. For children, potatoes as food may cause various allergic reactions. However, the identity and molecular structure of the putative allergens in potato have remained unknown. OBJECTIVE: The aim of our study was to identify possible major allergens in potato by using sera of atopic children suspected of having food allergy and having positive skin prick test responses to raw potato. METHODS: Potato proteins were purified by standard methods of protein chemistry and characterized with amino-terminal sequencing and mass spectrometry. The IgE-binding ability of the purified proteins was verified by immunoblotting and ELISA with IgE antibodies from the sera of atopic children having positive skin prick test responses to raw potato. RESULTS: Immunoblotting showed strong IgE binding to a 43-kd protein, identified as patatin, the main storage protein of potato tubers. In ELISA, 20 of 27 (74%) children with positive skin prick test responses to potato and none of the control subjects showed specific binding of IgE antibodies to purified patatin. A positive wheal-and-flare reaction was seen in 8 of 14 children prick tested with purified patatin. CONCLUSION: These results show that patatin in potatoes is a significant, previously unrecognized,IgE-binding protein for children with a positive skin prick test response to raw potato. Further studies are needed to confirm the clinical importance of potatoes, and especially patatin, as a food allergen.

Allergens↗
PubMed1998

IgE antibodies to prohevein, hevein, and rubber elongation factor in children with latex allergy.

BACKGROUND: Prohevein (Hev b 6.01) and hevein (Hev b 6.02) have been shown to be major IgE-binding allergens in health care workers and other adult patients allergic to natural rubber latex (NRL). Rubber elongation factor (REF; Hev b 1) and the 23/27 kd NRL allergen (Hev b 3) are characteristic of children with latex allergy who have spina bifida and other children requiring multiple operations at an early age. In addition, there are children with latex allergy and no history of multiple operations in whom sensitizing allergens are not known. OBJECTIVES: We studied IgE antibodies to NRL allergens in children with latex allergy who had not undergone surgery and compared the findings with those in children with latex allergy and a history of multiple operations. METHODS: Sera from 30 children with latex allergy who had not undergone surgery, 12 children with latex allergy with a history of multiple operations, and 19 control children without evidence of NRL allergy were examined. Immunoblotting was used to study IgE binding to NRL proteins, and purified prohevein, hevein, and REF were used in ELISA to measure specific IgE antibodies. RESULTS: In immunoblotting, sera from 21 (70%) children who had not undergone surgery and from 4 (33%) children with a history of multiple operations showed IgE binding to a 20-kd protein band (known to contain prohevein), and 9 (30%) and 8 (67%) sera, respectively, to a 14-kd protein band (known to contain REF). In ELISA, sera from 26 (86%) children who had not undergone surgery and from 7 (58%) children with a history of multiple operations had IgE antibodies to prohevein and 19 (63%) and 7 (58%) sera, respectively, to hevein. Eight (27%) sera from the children who had not undergone surgery had IgE antibodies to REF in contrast to 8 (67%) sera from children with a history of multiple operations. CONCLUSIONS: The IgE antibody pattern differs between children with latex allergy who had not undergone surgery and those with a history of multiple operations. The major allergens in children with no history of surgery appear to be prohevein and hevein and not REF, a finding that agrees well with that reported for health care workers with allergy to latex.

Adolescent↗
PubMed1998

Hevein-like protein domains as a possible cause for allergen cross-reactivity between latex and banana.

BACKGROUND: Patients allergic to natural rubber latex (NRL) frequently exhibit immediate hypersensitivity reactions to banana, but the molecular basis of these putative cross-reactions is unknown. OBJECTIVE: We wanted to examine whether proteins resembling hevein, a major NRL allergen, exist in banana and whether coexisting allergy to NRL and banana can be explained by IgE cross-reactivity to these proteins. METHODS: Allergens in banana cross-reacting with hevein were identified by IgE immunoblot inhibition. The cross-reacting proteins were purified by reversed-phase chromatography and characterized by amino acid sequencing. Allergen cross-reactivity was further assessed by IgE ELISA, IgE ELISA inhibition, and skin prick testing. RESULTS: In immunoblotting, 9 of 15 sera from patients allergic to NRL with IgE to hevein showed IgE binding to 32- and 33-kd banana proteins. These 2 protein bands were also targets to IgG from a hevein-immunized rabbit. IgE binding to both 32- and 33-kd protein bands was totally inhibited by hevein (10 ng/mL) in all 5 sera from patients allergic to NRL sera studied. N-terminal sequencing of the purified 32- and 33-kd proteins revealed 80% identity to the N-terminus of hevein. An internal peptide (19 amino acids) of the 33-kd protein gave over 90% identity to endochitinases of several plants. In ELISA all 15 sera from patients allergic to NRL had IgE to the purified 32-kd banana protein. In ELISA inhibition hevein (10 ng/mL) inhibited approximately 50% of IgE binding to the solid-phase 32-kd banana protein in a pool of sera from patients allergic to NRL. CONCLUSION: These results suggest that the commonly occurring hypersensitivity to banana in patients allergic to NRL could be explained by cross-reacting IgE antibodies binding to epitopes in hevein and in a hevein-like domain of a previously undescribed endochitinase in banana.

Adult↗
PubMed1998

Measurement of natural rubber latex allergen levels in medical gloves by allergen-specific IgE-ELISA inhibition, RAST inhibition, and skin prick test.

Exposure to natural rubber latex (NRL) medical gloves poses risks to patients sensitized to NRL and to users of protective gloves. Previous studies have shown that extractable allergen levels of the gloves vary widely. Since most of the available laboratory methods of NRL allergen measurement lack adequate validation, we wanted to evaluate the performance of a recently developed competitive IgE-ELISA-inhibition method in relation to the skin prick test (SPT) and RAST inhibition, as well as to extractable protein quantification and an immunochemical latex antigen assay (LEAP). Twenty samples of surgical (n = 14) and examination gloves (n = 6), covering > 90% of medical gloves marketed in Finland in 1994-5, were collected by the Finnish National Research and Development Centre for Welfare and Health, coded, extracted, and analyzed by the five methods. The IgE-ELISA inhibition correlated highly significantly with SPT (r = 0.94) and RAST inhibition (r = 0.96). Likewise, ELISA inhibition and RAST inhibition showed highly significant correlation (P = 0.96, P < 0.0001 in all three instances). Protein quantification by a modified Lowry method also correlated highly significantly with SPT (r = 0.80), RAST inhibition (r = 0.82), and ELISA inhibition (r = 0.81, P < 0.0001 in all three instances). Clearly weaker correlation, though statistically significant (r = 0.48, P = 0.03), was found between SPT and the LEAP assay. An NRL standard preparation was assigned an arbitrary content of 100,000 allergen units (AU) per ml. In relation to this standard, the NRL allergen level was considered low (< 10 AU/ml) in 11, moderate (10-100 AU/ml) in two, and high (> 100 AU/ml) in seven of the 20 glove brands analyzed. In conclusion, the results of a novel IgE-ELISA-inhibition method of measuring NRL allergen levels in medical gloves correlated highly significantly with those of SPT. The ELISA method was found to be sensitive, reproducible, technically easy, inexpensive, and suitable for the analysis of large numbers of NRL products. The results of extensive market surveys in 1994 and 1995, communicated to the medical community in Finland, appear to have had a clear effect in moving glove purchasing policies toward the use of low-allergen gloves.

Adolescent↗
PubMed1998

Purification of filaggrin from human epidermis and measurement of antifilaggrin autoantibodies in sera from patients with rheumatoid arthritis by an enzyme-linked immunosorbent assay.

BACKGROUND: The so-called antikeratin antibody (AKA) and the antiperinuclear factor (APF) that recognize proteins related to human epidermal filaggrin belong to the most specific serological markers of rheumatoid arthritis (RA). However, assays for the detection of AKA and APF are currently based on immunofluorescence, a method that is subject to arbitrary interpretation and inadequate standardization of the substrates. METHODS: Proteins extracted from human epidermis were separated by reversed-phase high-performance liquid chromatography (HPLC). Filaggrin-containing fractions, identified in immunoblotting by monoclonal antifilaggrin antibodies, were then subjected to gel filtration HPLC and, finally, to a second reversed-phase HPLC step. Tryptic digestion, amino acid sequencing and mass spectrometry were used to confirm the identity of the purified protein. Filaggrin was used as antigen in enzyme-linked immunosorbent assay (ELISA) to measure IgG class antifilaggrin antibodies. RESULTS: The filaggrin preparation obtained gave a single band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, binding monoclonal antifilaggrin antibody in immunoblotting. Amino acid sequences of all 10 tryptic peptides analyzed were shown to originate from human filaggrin. Antifilaggrin antibody levels exceeded the 99th percentile level of 100 middle-aged blood donors in 26/55 (47%) RA sera. At a similar cutoff level 28/55 (51%) of the RA sera were positive in the AKA test. Of the 26 antifilaggrin-positive sera, 21 were also AKA-positive. CONCLUSION: Human filaggrin can be purified by standard biochemical techniques, despite the heterogeneity of the protein, and used in ELISA for testing autoantibodies to filaggrin. The sensitivity of the assay equals that of the AKA test.

Adult↗
PubMed1997

Latex allergy diagnosis: in vivo and in vitro standardization of a natural rubber latex extract.

For the diagnosis of IgE-mediated (immediate) hypersensitivity to natural rubber latex (NRL), skin prick testing with extracts of latex gloves has been widely used, but such extracts are difficult to standardize. The present study aimed to produce on an industrial scale an NRL extract from freshly collected NRL and to evaluate, calibrate, and standardize the extract by both in vivo and in vitro testing. The source material, latex of the rubber tree, Hevea brasiliensis (clone RRIM 600), was frozen immediately after collection in Malaysia and shipped in dry ice to Stallergènes SA, France. Protein and allergen profiles were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), immunoblotting, isoelectric focusing (IEF), crossed immunoelectrophoresis (CIE), and crossed radioimmunoelectrophoresis (CRIE). Allergen quantification was effected by RAST inhibition. The capacity of the preparation to elicit immediate hypersensitivity reactions in vivo was measured by skin prick testing in 46 latex-allergic patients and 76 nonallergic control subjects. SDS-PAGE and immunoblot profiles of the extract and an NRL standard (E8) provided by the US Food and Drug Administration were almost identical, disclosing several distinct IgE-binding proteins with apparent molecular weights of 14, 20, 27, 30, and 45 kDa, conforming to reported molecular weights of several significant NRL allergens. An arbitrary index of reactivity (IR) of 100 was assigned to the extract at 1:200 dilution (w/v), having a protein content of 22 micrograms/ml. Skin prick testing of latex-allergic patients and controls using the extract at 100 IR revealed 93% sensitivity, 100% specificity, 100% negative predictive value, and 96% positive predictive value. In conclusion, a skin prick test reagent for diagnosis of type I NRL allergy was successfully standardized. The reagent was demonstrated to contain most, if not all, of the currently known clinically significant NRL allergens, and it showed high sensitivity and specificity.

Adolescent↗
PubMed1996

The main IgE-binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein.

Polypeptides of natural rubber latex (NRL) that elute from surgeon's gloves and other manufactured rubber products can sensitize exposed individuals and elicit severe hypersensitivity reactions. Previously, we showed that prohevein is a major allergen in NRL, the source material for rubber manufacturing. To analyze which region of the molecule carries the main IgE-binding epitope(s), we purified prohevein and its C-domain from NRL by gel filtration, reverse phase chromatography, and electroelution. In immunoblotting, prohevein bound IgE from 15 of 20 (75%), and the prohevein C-domain from 3 of 20 (15%) latex-allergic patient sera. In ELISA, 36 of 52 (69%) patient sera showed IgE binding to prohevein, whereas 11 of 52 (21%) sera had IgE to prohevein C-domain. We then purified from a brand of highly allergenic surgeon's gloves six hydrophilic peptides that revealed in amino-terminal sequencing 100% identity to the N-terminus of prohevein. In mass spectrometry, all purified peptides gave a molecular mass of 4719 +/- 1.9 daltons, which corresponds to the molecular mass of hevein (4719.1 daltons), a 43-amino acid N-terminal fragment of prohevein. Purified hevein inhibited 72% of IgE binding from pooled sera of NRL-allergic patients to solid phase glove extract and 45% of IgE binding to solid phase NRL. Of the 43 NRL-allergic patient sera tested, 56% showed IgE Abs to purified hevein in ELISA. In skin prick testing, purified hevein elicited positive reactions in three-quarters of the latex-allergic patients tested. These results indicate that the majority of prohevein's IgE-binding ability resides in its N-terminal fragment, known as hevein. In one highly allergenic latex glove examined, the majority of IgE-binding ability was attributable to hevein molecules, suggesting that these peptides can be significant sensitizers in NRL allergy.

Adult↗
PubMed1996

A two-dimensional electrophoretic analysis of latex peptides reacting with IgE and IgG antibodies from patients with latex allergy.

Latex proteins from nonammoniated natural rubber latex were investigated for their reactivity with antibodies in the sera of patients with spina bifida and health care workers with allergy to latex. Immunoblots of two-dimensional electrophoresis were used to compare the reactivity of various polypeptides against IgE, IgG, and subclasses of IgG. A total of 79 polypeptides showed reactivity with IgG and IgE antibodies from different patients. IgG showed reactivity with all the 79 polypeptides, while IgE reacted with 56 allergens. IgG2 reacted with the least number of proteins, while IgG4 reacted with the largest number of polypeptides. Several antigens were identified as significant due to their reactivity with antibodies in latex-allergic patients. Four proteins reacted with IgE, IgG1, IgG3 and IgG4 of only spina bifida patients with latex allergy, while one other protein reacted only with health care workers. Thus, these relevant latex peptides may be isolated, purified, and used in various assays for more reliable diagnosis of latex allergy.

Adolescent↗
PubMed1996

Significance of rubber elongation factor as a latex allergen.

IgE-mediated hypersensitivity to proteins eluting from surgical gloves and other natural rubber products is a well-recognized allergic condition with special impact to health care workers and sensitized patients. Since rubber elongation factor (REF) has been suggested to be the major latex allergen (Hev b 1) we purified REF from rubber particles using electrophoresis and electroelution and reevaluated the occurrence of IgE antibodies to purified REF. The purified protein was subjected to tryptic digestion, peptide separation and amino acid sequencing. Amino acid sequences of 9 tryptic peptides from the purified 14-kD protein gave 100% homology to REF. In immunoblotting, sera from 4 of 6 latex-allergic children with spina bifida or other congenital anomalies exhibited IgE antibodies against REF whereas only 1 serum from the 30 other latex-allergic patients had similar antibodies. In IgE ELISA 8/45 (18%) latex-allergic patients had IgE antibodies to purified REF, whereas 30 (67%) of the same patients had IgE antibodies to purified prohevein, another rubber protein, recently shown to be a major natural rubber latex allergen. The observed overall low frequency of IgE antibodies to purified REF, as measured by two specific IgE assays, indicates that REF is one but not the most significant allergen among the natural rubber latex proteins.

Adolescent↗
PubMed1996

Crossreactivity between allergens in natural rubber latex and banana studied by immunoblot inhibition.

BACKGROUND: An association between allergic reactions to natural rubber latex and to banana has been reported but the immunochemical properties of the putative cross-reacting allergens remain unknown. OBJECTIVE: To study extracts of banana and natural rubber latex and sera from latex-allergic patients for possible crossreacting allergens and IgE antibodies. METHODS: Sera from 22 latex-allergic patients and 22 control subjects with no evidence of allergy to latex or to banana were studied. All patients had positive and controls negative reactions in skin-prick testing using an eluate of latex gloves. IgE antibodies to natural rubber latex and to banana were evaluated by immunoblotting and by radioallergosorbent test (RAST) and crossreactivity between allergens in banana and natural rubber latex by immunoblot inhibition. Skin-prick testing was used to examine in vivo reactivity to banana. RESULTS: Ten of the 22 (45%) latex-allergic patients sera recognized altogether 14 allergens in banana by immunoblotting. The most frequently identified banana allergens were 23, 32, 36, 39 and 47 kDa proteins. The banana skin-prick test was positive in 14 of 18 (78%) latex-allergic patients studied and banana RAST in 12 of 14 patient sera tested. Fourteen of 21 interviewed patients reported symptoms from eating or handling bananas. In immunoblot inhibition studies a dose-dependent inhibition of IgE binding to banana extract with natural rubber latex proteins was observed in all five patient sera tested and, likewise, the binding of IgE to natural rubber latex extract was inhibited with banana proteins in four of the five patient sera. CONCLUSIONS: The present results confirm the existence of crossreacting allergens in natural rubber latex and banana and provide new information on the immunochemical nature and heterogeneity of these allergens.

Adult↗
PubMed1995

Cross-reacting allergens in natural rubber latex and avocado.

BACKGROUND: An association between allergy to latex and avocado has been reported but the responsible cross-reacting allergens have not been identified or characterized. METHODS: Immunoblotting, immunoblot inhibition, and RAST inhibition methods were used to study cross-reactive proteins between natural rubber latex (NRL) and avocado. Sera from 18 patients with previously verified latex allergy were used as the source of IgE antibodies, and 11 of the patients underwent skin prick testing with fresh avocado. RESULTS: Fourteen of the 18 sera (78%) had IgE antibodies that bound to a total of 17 avocado proteins with apparent molecular weights ranging from 16 to 91 kd. Ten most strongly reacting sera were used for immunoblot inhibition studies. When NRL proteins were used as soluble inhibitors, binding of IgE antibodies to solid-phase avocado proteins was inhibited in a dose-dependent manner: 100 micrograms of NRL proteins inhibited IgE binding to 15 of the 17 avocado proteins, and 10 micrograms caused inhibition to 13 protein bands. Comparably, soluble avocado proteins were able to inhibit IgE binding to solid-phase NRL. Corresponding RAST inhibitions were performed with two patient sera; in both, avocado inhibited IgE binding to NRL and in one NRL proteins inhibited IgE binding to avocado. Skin prick test responses to fresh avocado were positive in seven of the 11 patients with latex allergy who were tested. CONCLUSIONS: The large number of inhibitable proteins in immunoblot experiments and clinical observations from skin prick tests suggest considerable immunologic cross-reactivity between NRL and avocado. The observed cross-reacting protein components may be responsible for the recently reported type I hypersensitivity reactions to NRL and avocado in patients with a preexisting allergy to either allergen.

Adolescent↗
PubMed1995

Prohevein from the rubber tree (Hevea brasiliensis) is a major latex allergen.

BACKGROUND: There is general agreement that proteins eluting from different natural rubber latex products can cause immediate type hypersensitivity reactions in latex-allergic patients. However, there is as yet no consensus as to what are the most important allergens in natural rubber latex. OBJECTIVE: We wanted to purify and characterize at the primary structure level three natural latex proteins, suggested to represent significant allergens. METHODS: Proteins were purified from ultracentrifuged bottom fraction of natural rubber latex using high performance liquid chromatography gel filtration and reversed phase chromatography. Purified proteins were subjected to tryptic cleavage, peptide separation and amino acid sequencing. Immunoblotting was used to demonstrate IgE antibodies to the purified proteins in sera from latex-allergic patients. RESULTS: A 20 kDa protein was identified by amino acid sequencing as prohevein, a major protein in the rubber tree Hevea brasiliensis, and a 30 kDa natural rubber latex protein as hevamine, another essential rubber tree protein. A third, previously undescribed natural rubber latex protein, showed high homology to several plant endo-1,3-beta-glucosidases. In immunoblotting, the purified prohevein bound IgE antibodies from 24/29 (83%) sera of latex-allergic patients including positive results in 4/6 latex-allergic children with spina bifida or other congenital anomalies. The purified prohevein elicited positive skin-prick test reactions in all six latex-allergic patients showing IgE to prohevein. The purified 36 kDa protein bound IgE from 6/29 (21%) latex-allergic sera, and the purified hevamine from only 1/29 patient sera. CONCLUSION: The observed high frequency of IgE antibodies to prohevein suggests that this protein is a major natural rubber latex allergen.

Adolescent↗
PubMed1995

Purification and partial amino acid sequencing of a 27-kD natural rubber allergen recognized by latex-allergic children with spina bifida.

We purified from natural rubber latex (NRL) by means of high-performance liquid chromatography a 27-kD protein, recognized characteristically by IgE in sera from latex-allergic children with spina bifida or other congenital anomalies and histories of multiple surgeries. N-terminal sequence analysis of the purified 27-kD protein was unsuccessful suggesting that its N-terminus is blocked. To obtain internal sequence information from the protein it was digested with trypsin and the purified tryptic peptides were subjected to sequence analysis. Thirteen of the 14 sequenced peptides revealed no significant homology to any of the published protein sequences indicating that the 27-kD protein is previously undescribed at the primary structure level. However, one of the 14 sequenced peptides showed significant homology to the rubber elongation factor, a 14.6-kD NRL protein. For the time being, the 27-kD NRL protein is the first molecularly characterized NRL allergen associated with defined clinical manifestations of latex allergy.

Adolescent↗
PubMed1994

IgE immune response to rubber proteins in adult patients with latex allergy.

In the present immunoblot study we examined IgE immune responses to natural rubber latex proteins in sera from 27 adult patients with latex allergy. We demonstrated at least 30 proteins in the rubber tree sap, of which 19 bound IgE antibodies in a heterogeneous manner in patient sera. Twenty-two of the 27 patient sera (81%) showed positive immunoblot test results. IgE antibodies in the patient sera bound most frequently to a 20 kd allergen, which was recognized by 17 of the 22 (77%) patient sera with positive immunoblot test results. These results suggest that a 20 kd rubber protein could be a major allergen in adult patients with latex allergy. Immunoblotting with a representative set of allergens as antigen would offer a sensitive, confirmatory in vitro test to demonstrate hypersensitivity to latex.

Adult↗
PubMed1994

Allergen and protein content of latex gloves.

BACKGROUND: Proteins eluting from surgical gloves and other medical rubber products elicit immediate local and systemic hypersensitivity reactions in latex-allergic subjects but detailed knowledge about the amount and allergenic potential of these proteins is scanty. OBJECTIVE: To protect latex-allergic people and to diminish the risk of sensitization, adequate methods are needed to measure and monitor the allergen content of surgical latex gloves. METHODS: Extracts of six surgical and one household latex glove brand were studied. Bradford and Lowry methods were used for total protein measurements. Sera from 17 latex-allergic patients were used as a source of latex IgE antibodies. Allergen content of extracts was studied in vitro by immunoblot, crossed radioimmunoelectrophoresis and immunospot methods, and in vivo by skin prick testing in 35 latex-allergic patients. RESULTS: The total protein concentration of the glove extracts varied from 3 to 337 micrograms/g glove. The Bradford method gave lower values than the Lowry method. Immunoblotting showed allergenic rubber proteins in four of the seven glove brands. Ten proteins in two surgical and six proteins in one household glove brand bound latex IgE antibodies in a heterogeneous manner. The results from crossed radioimmunoelectrophoresis and immunospot assays were mostly in line with immunoblotting findings. Extracts from five of the seven glove brands elicited positive prick tests; in all five also the presence of allergens could be shown by in vitro tests. Prick test reactivity and total protein concentration were not directly correlated. CONCLUSIONS: In vitro assays showed considerable variation in the total protein and allergen contents of different latex glove brands. The amount of protein eluting from the gloves did not always correlate with their allergenicity in skin prick tests indicating that total protein measurement is not a sufficient method to monitor the allergenic properties of latex gloves.

Allergens↗
PubMed1994

Latex allergy: frequent occurrence of IgE antibodies to a cluster of 11 latex proteins in patients with spina bifida and histories of anaphylaxis.

Proteins and allergens in natural rubber latex were characterized by a two-dimensional immunoblot method with serum samples from 17 patients with latex allergy of whom 10 had spina bifida and 7 were health care workers. We demonstrated in rubber tree sap approximately 240 polypeptides of which 57 bound immunoglobulin E (IgE) in patient serum samples. Forty-six of the 57 allergens were identified by patients with spina bifida, 19 of 57 allergens by health care workers, and 8 of 57 allergens by both patient groups. IgE antibodies from all 5 patients with spina bifida with histories of anaphylaxis bound three allergens with molecular weights of 27 kd and isoelectric points ranging from pH 4.6 to pH 4.8. Four of these 5 patients also identified a complex of eight other allergens with molecular weights ranging from 13 kd to 27 kd and isoelectric points from pH 4.4 to pH 5.6. This cluster of 11 allergens was identified by none of the 7 health care workers and by only 1 of 5 patients with spina bifida without demonstrable anaphylaxis. These preliminary findings indicate that patients with spina bifida in whom latex hypersensitivity has developed exhibit a strong anti-latex IgE immune response, which seems to differ markedly from the immune response of health care workers with latex allergy. The characteristic anti-latex IgE profile in patients with spina bifida and with a history of an anaphylactic reaction may be valuable in the evaluation of pathogenetic processes in latex allergy.

Adolescent↗
PubMed1993

Immunoglobulin E reactivity to latex antigens in the sera of patients from Finland and the United States.

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.

Adult↗