H.Y. Yeang

Allergenic proteins of natural rubber latex

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.

Allergen concentration in natural rubber latex

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.

Percutaneous reactivity to natural rubber latex proteins persists in health‐care workers following avoidance of natural rubber latex

Background Long‐term avoidance of natural rubber latex [Hevea brasiliensis (Hev b)] is currently recommended for health‐care workers (HCWs) with established natural rubber latex (NRL) allergy. Percutaneous sensitivity to eight Hev b NRL allergens was evaluated in HCWs in 2000. To date, no studies have evaluated the longitudinal effects of NRL avoidance on percutaneous sensitivity to NRL allergens.

Molecular cloning and immunoglobulin E reactivity of a natural rubber latex lecithinase homologue, the major allergenic component of Hev b 4

Background Hev b 4 is an allergenic natural rubber latex (NRL) protein complex that is reactive in skin prick tests and in vitro immunoassays. On SDS‐polyacrylamide gel electrophoresis (SDS‐PAGE), Hev b 4 is discerned predominantly at 53–55 kDa together with a 57 kDa minor component previously identified as a cyanogenic glucosidase. Of the 13 NRL allergens recognized by the International Union of Immunological Societies, the 53–55 kDa Hev b 4 major protein is the only candidate that lacks complete cDNA and protein sequence information.

Erratum: Allergen concentration in natural rubber latex (Clinical and Experimental Allergy (2006) 36 (1078-86))

Allergen concentration in natural rubber latex H.-Y. Yeang, R. G. Hamilton, D. I. Bernstein, S. A. M. Arif, K. -S. Chow, Y. -H. Loke, M. Raulf-Heimsoth, S. Wagner, H. Breiteneder and R. E. Biagini Biotechnology and Strategic Research Unit, Rubber Research Institute of Malaysia, Malaysian Rubber Board, Malaysia, Johns Hopkins Asthma and Allergy Center, Johns Hopkins University School of Medicine, Baltimore, MD, USA, Division of Allergy/Immunology, University of Cincinnati College of Medicine, Cincinnati, OH, USA, Allergy/Immunology Division, Institute of Occupational Medicine, Bochum, Germany, Department of Pathophysiology, Medical University of Vienna, Austria and Biomonitoring and Health Assessment Branch, National Institute for Occupational Safety and Health, Cincinnati, OH, USA