有哪些信誉好的足球投注网站a structural model for binding of the serine-rich repeat adhesin gspb to host carbohydrate receptors结构模型绑定的serine-rich重复adhesin gspb碳水化合物受体.pdfVIP
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a structural model for binding of the serine-rich repeat adhesin gspb to host carbohydrate receptors结构模型绑定的serine-rich重复adhesin gspb碳水化合物受体
A Structural Model for Binding of the Serine-Rich Repeat
Adhesin GspB to Host Carbohydrate Receptors
Tasia M. Pyburn1,2, Barbara A. Bensing3, Yan Q. Xiong4, Bruce J. Melancon2,5¤a, Thomas M.
Tomasiak1,2¤b, Nicholas J. Ward1, Victoria Yankovskaya6, Kevin M. Oliver2,5, Gary Cecchini6,7, Gary A.
Sulikowski2,5, Matthew J. Tyska8, Paul M. Sullam3, T. M. Iverson 1,2,9*
1 Department of Pharmacology, Vanderbilt University Medical Center, Nashville, Tennessee, United States of America, 2 Vanderbilt Institute of Chemical Biology, Nashville,
Tennessee, United States of America, 3 Department of Medicine, Veterans Affairs Medical Center and the University of California, San Francisco, California, United States of
America, 4 Department of Medicine, Harbor-UCLA Medical Center, Torrance, California, United States of America, 5 Department of Chemistry, Vanderbilt University,
Nashville, Tennessee, United States of America, 6 Molecular Biology Division, Veterans Affairs Medical Center, San Francisco, California, United States of America,
7 Department of Biochemistry Biophysics University of California, San Francisco, California, United States of America, 8 Department of Cell and Developmental Biology,
Vanderbilt University Medical Center, Nashville, Tennessee, United States of America, 9 Department of Biochemistry, Vanderbilt University Medical Center, Nashville,
Tennessee, United States of America
Abstract
GspB is a serine-rich repeat (SRR) adhesin of Streptococcus gordonii that mediates binding of this organism to human
platelets via its interaction with sialyl-T antigen on the receptor GPIba. This interaction appears to be a major virulence
determinant in the pathogenesis of infective endocarditis. To address the mechanism by which GspB recognizes
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