the function and three-dimensional structure of a thromboxane a2cysteinyl leukotriene-binding protein from the saliva of a mosquito vector of the malaria parasite功能和三维结构的凝血恶烷a2cysteinyl leukotriene-binding唾液的蛋白质疟原虫的蚊子.pdf

The Function and Three-Dimensional Structure of a Thromboxane A2/Cysteinyl Leukotriene-Binding Protein from the Saliva of a Mosquito Vector of the Malaria Parasite 1,2 1 1 ´ 1,3 ´ 1 Patricia H. Alvarenga , Ivo M. B. Francischetti , Eric Calvo , Anderson Sa-Nunes , Jose M. C. Ribeiro , John F. Andersen1* 1 Laboratory of Malaria and Vector Research, National Institutes of Health, National Institute of Allergy and Infectious Diseases, Rockville, Maryland, United States of ´ ´ ´ ´ ´ America, 2 Laboratorio de Bioquımica e Fisiologia de Artropodes, Departamento de Quımica, Universidade Federal Rural do Rio de Janeiro, Seropedica, Brazil, ´ ˆ ´ ˜ ˜ 3 Laboratorio de Imunologia Experimental, Departamento de Imunologia, Instituto de Ciencias Biomedicas, Universidade de Sao Paulo, Sao Paulo, Brazil Abstract The highly expressed D7 protein family of mosquito saliva has previously been shown to act as an anti-inflammatory mediator by binding host biogenic amines and cysteinyl leukotrienes (CysLTs). In this study we demonstrate that AnSt-D7L1, a two-domain member of this group from Anopheles stephensi, retains the CysLT binding function seen in the homolog AeD7 from Aedes aegypti but has lost the ability to bind biogenic amines. Unlike any previously characterized members of the D7 family, AnSt-D7L1 has