Affinity purification of latex antigens

Slater, Jay E.; Trybul, Diane E.

doi:10.1016/s0091-6749(94)70076-1

Cited by 26 publications

(16 citation statements)

References 8 publications

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“…In our earlier work using NAL, monoclonal antibodies detected peptides of several sizes by Western blot analysis and affinity purification techniques (31), an observation confirmed by other investigators (32). One possible explanation of this result is that many of the peptide bands observed in NAL were cleavage products of larger, parent proteins; other explanations are that several proteins contain the epitopes recognized by the monoclonals or that latex proteins aggregate under conditions of standard electrophoretic analysis.…”

supporting

confidence: 72%

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Identification, Cloning, and Sequence of a Major Allergen (Hev b 5) from Natural Rubber Latex (Hevea brasiliensis)

Slater

Vedvick

Arthur-Smith

et al. 1996

Journal of Biological Chemistry

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128

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Natural rubber latex in medical devices and consumer products has been implicated in over 1100 anaphylactic reactions that resulted in at least 15 deaths between 1988 and 1992 (1, 2). These reactions are caused by proteins that elute from the surfaces of certain latex products, especially gloves, barium enema catheters, balloons, and condoms. The proteins bind to antigen-specific IgE on tissue mast cells and trigger an anaphylactic response. While the production of IgE to latex proteins can occur in any individual, some individuals with uniquely high exposure to latex products appear to be at significantly greater risk for the production of these antibodies than the general population. These include health care workers and children with spina bifida (3-5). Interestingly, there appears to be significant clinical and immunochemical cross-reactivity between some latex proteins and allergens in certain fruits and vegetables, such as banana, kiwi, avocado, and potato, and patients with fruit and vegetable allergy may be at increased risk for reacting to latex proteins (6 -10).Latex allergy can be a devastating disease, with serious and occasionally fatal outcomes. The only treatment is avoidance (11,12), and health care workers with severe latex allergy may be required to change careers or leave health care entirely to avoid potentially dangerous exposure. Since anaphylactic episodes have occurred following skin testing with crude latex extracts (13-16), immunotherapy is not possible with currently available crude preparations. The identification and isolation of pure antigens, and the analysis of the B-and T-cell epitopes of these antigens, will facilitate the design and testing of safer regimens of immunotherapy.The proteins in natural rubber latex are derived from the commercial rubber tree, Hevea brasiliensis. Latex is produced in laticifers, which are specialized structures that consist of anastamosed latex-producing cells. Harvested Hevea latex is a complete cytosol with a high protein content (17, 18). Hevea latex is typically ammoniated when tapped to prevent premature coagulation and bacterial growth. Ammoniated latex is the source material for most of the products that elicit allergic reactions; thus, it clearly contains immunogenic material. However, immunochemical studies with ammoniated latex have failed to reveal the wealth of IgE-binding proteins found in non-ammoniated latex (NAL) 1 (19), which is collected into a liquid nitrogen-cooled container.From the first observations that products made from Hevea latex can elicit catastrophic allergic reactions in susceptible individuals, the component allergens have eluded conclusive identification. In part, this has been due to the complexity and instability of the proteins of Hevea latex. In addition, many investigators have been unable to obtain quantities of fresh material for examination and have been limited to the use of finished products or ammoniated latex (19) for their studies. In spite of these difficulties, several potential allergens have been i...

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confidence: 72%

“…Production of Mouse Hybridomas-Hybridoma lines were produced from a BALB/c mouse immunized with rHev b 5/MBP in Freund's adjuvant, as described previously (31). Cell lines were tested for production of antibody to rHev b 5/MBP, MBP, and NAL.…”

Section: Methodsmentioning

confidence: 99%

Identification, Cloning, and Sequence of a Major Allergen (Hev b 5) from Natural Rubber Latex (Hevea brasiliensis)

Slater

Vedvick

Arthur-Smith

et al. 1996

Journal of Biological Chemistry

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128

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“…Slater and Trybul [16] have recently shown by immunoblotting binding of IgE from latex-allergic children with spina bifida to 14.3-and 27.5-kD NRL proteins. They also reported that a monoclonal antibody raised against ammoniated NRL detected 26-and 27-kD proteins and also sever al other polypeptides in NRL.…”

Section: Discussionmentioning

confidence: 99%

Purification and Partial Amino Acid Sequencing of a 27-kD Natural Rubber Allergen Recognized by Latex-Allergic Children with Spina Bifida

Alenius

Kalkkinen

Lukka

et al. 1995

Int Arch Allergy Immunol

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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.

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“…Turjanmaa (31), Fuchs and Wahl (32), Slater et al (33)(34)(35), and others (36)(37)(38) have studied extracts of natural rubber latex, latex gloves, condoms, and balloons to identify the relevant allergenic proteins. By using Western blot analyses to identify human IgE bound to electrophoresis proteins, well over 50 allergenic bands have been reported, with major bands occurring in the 14 and 30 kDa regions (39).…”

Section: Resultsmentioning

confidence: 99%