glycotope sharing between snail hemolymph and larval schistosomes larval transformation products alter shared glycan patterns of plasma proteinsglycotope蜗牛血淋巴和幼虫血吸虫幼虫转换产品之间共享改变血浆蛋白聚糖模式共享.pdfVIP

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glycotope sharing between snail hemolymph and larval schistosomes larval transformation products alter shared glycan patterns of plasma proteinsglycotope蜗牛血淋巴和幼虫血吸虫幼虫转换产品之间共享改变血浆蛋白聚糖模式共享.pdf

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glycotope sharing between snail hemolymph and larval schistosomes larval transformation products alter shared glycan patterns of plasma proteinsglycotope蜗牛血淋巴和幼虫血吸虫幼虫转换产品之间共享改变血浆蛋白聚糖模式共享

Glycotope Sharing between Snail Hemolymph and Larval Schistosomes: Larval Transformation Products Alter Shared Glycan Patterns of Plasma Proteins 1 1 1 1 ´ 2 Timothy P. Yoshino *, Xiao-Jun Wu , Hongdi Liu , Laura A. Gonzalez , Andre M. Deelder , Cornelis H. Hokke2 1 Department of Pathobiological Sciences, University of Wisconsin School of Veterinary Medicine, Madison, Wisconsin, United States of America, 2 Department of Parasitology, Center for Infectious Diseases, Leiden University Medical Center, Leiden, The Netherlands Abstract Recent evidence supports the involvement of inducible, highly diverse lectin-like recognition molecules in snail hemocyte- mediated responses to larval Schistosoma mansoni. Because host lectins likely are involved in initial parasite recognition, we sought to identify specific carbohydrate structures (glycans) shared between larval S. mansoni and its host Biomphalaria glabrata to address possible mechanisms of immune avoidance through mimicry of elements associated with the host immunoreactivity. A panel of monoclonal antibodies (mABs) to specific S. mansoni glycans was used to identify the distribution and abundance of shared glycan epitopes (glycotopes) on plasma glycoproteins from B. glabrata strains that differ in their susceptibilities to infection by S. mansoni. In addition, a major aim of this study was to determine if larval transformation products (LTPs) could bind to plasma proteins, and thereby alter the glycotopes exposed on plasma proteins in a snail strain-specific fashion. Plasma fractions (,100 kDa/.100 kDa) from susceptible (NMRI) and resistant (BS-90) snail strains were subjected to SDSand immunoblot analyses using mAB to LacdiNAc (LDN),