Mosquito and porcine liver heparan sulfate proteoglycans: Structural and functional comparison, and their roles in malaria

CARB 106

Jin Xie, xiej@rpi.edu, Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, 110, 8th Street, Troy, NY 12180, Melissa Kemp, kempm@rpi.edu, Department of Biology, Rensselaer Polytechnic Institute, 110, 8th Street, Troy, NY 12180, Photini Sinnis, Photini.Sinnis@med.nyu.edu, Department of Infectious Diseases, New York University, New York City, NY 10010, Toshihiko Toida, Faculty of Pharmaceutical Sciences, Chiba University, 1-33, Yayoi, Inage-ku, Chiba, 263-8522, Japan, and Robert J Linhardt, linhar@rpi.edu, Departments of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Center for Biotechnology and Interdisciplinary Studies, 110 8th Street, Troy, NY 12180.
Plasmodium sporozoite is known to be the causative agents of malaria. It has been shown that the heparan sulfate found in human liver is responsible for binding to the major surface protein of sporozoite, the circumsporozoite protein (CSP). But less is known about the role of the heparan sulfate in host mosquito. In this work, heparan sulfate is successfully extracted from female Anopheles stephensi mosquitoes and is compared, structurally and functionally, with porcine liver heparan sulfate as both represent receptors for the malaria parasite CSP by using HPLC and surface plasmon resonance. An understanding of the structural and functional similarities and differences of these receptors may result in novel therapeutic approaches for developing anti-malaria vaccines.
 

General Contributed Papers: Synthesis
9:00 AM-11:00 AM, Thursday, 14 September 2006 Hilton San Francisco -- Yosemite C, Oral

Division of Carbohydrate Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006