TY - JOUR
T1 - A single amino acid substitution on the surface of a natural hevein isoform (Hev b 6.0202), confers different IgE recognition
AU - Reyes-López, César A.
AU - Pedraza-Escalona, Martha
AU - Mendoza, Guillermo
AU - Hernández-Santoyo, Alejandra
AU - Rodríguez-Romero, Adela
N1 - Funding Information:
We are grateful to Dr. Michael K. Gilson from CARB-UMBI, USA for helpful discussion and Dr. Socorro Orozco and José Huerta from the Instituto Nacional de Pediatria, México City for providing the adult and children sera (The ethics committee of the Institution approved this study). X-ray data were collected at the L.U.E.P, U.N.A.M. This research was supported in part by the Dirección General de Asuntos del Personal Académico UNAM (IN209506-3).
PY - 2006/5/1
Y1 - 2006/5/1
N2 - Decreased immune reactivity of isoforms of major allergens has been reported. However, such claims have always been based on experiments with recombinant proteins. This work describes the molecular and physicochemical characterization of a hevein (Hev b 6.0201) natural isoform (Hev b 6.0202), which is present in rubber latex from Hevea brasiliensis. The isoallergen has a single substitution Asn14Asp, which gives rise to local differences in the surface potential, as observed from the crystal structure presented here. Besides, ELISA inhibition using serum pools of adult and pediatric patients showed reduced IgE-binding capacity (∼27%) with the isoallergen. Overall, these results are relevant to delineate crucial residues involved in this dominant discontinuous epitope.
AB - Decreased immune reactivity of isoforms of major allergens has been reported. However, such claims have always been based on experiments with recombinant proteins. This work describes the molecular and physicochemical characterization of a hevein (Hev b 6.0201) natural isoform (Hev b 6.0202), which is present in rubber latex from Hevea brasiliensis. The isoallergen has a single substitution Asn14Asp, which gives rise to local differences in the surface potential, as observed from the crystal structure presented here. Besides, ELISA inhibition using serum pools of adult and pediatric patients showed reduced IgE-binding capacity (∼27%) with the isoallergen. Overall, these results are relevant to delineate crucial residues involved in this dominant discontinuous epitope.
KW - Crystal structure
KW - Hev b 6.0201
KW - Hevein
KW - IgE-epitope
KW - Isoallergens
UR - http://www.scopus.com/inward/record.url?scp=33646914467&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2006.03.085
DO - 10.1016/j.febslet.2006.03.085
M3 - Artículo
C2 - 16638575
SN - 0014-5793
VL - 580
SP - 2483
EP - 2487
JO - FEBS Letters
JF - FEBS Letters
IS - 10
ER -