Show simple item record

dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorRathore, Dharmendar
dc.contributor.authorHrstka, Sybil C.L.
dc.contributor.authorSacci, John B.
dc.contributor.authorDe la Vega, Patricia
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorKumar, Sanjai
dc.contributor.authorMcCutchan, Thomas F.
dc.identifier.citationMolecular Mechanism of Host Specificity in Plasmodium Falciparum Infection: Role of Circumsporozoite Protein, D. Rathore, S. C. L. Hrstka, J. B. Sacci, P. de la Vega, R.J. Linhardt, S. Kumar, T.F. McCutchan, Journal of Biological Chemistry, 278, 40905 – 40910, 2003.
dc.descriptionJournal of Biological Chemistry, 278, 40905–40910
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractPlasmodium falciparum sporozoites invade liver cells in humans and set the stage for malaria infection. Circumsporozoite protein (CSP), a predominant surface antigen on sporozoite surface, has been associated with the binding and invasion of liver cells by the sporozoites. Although CSP across the Plasmodium genus has homology and conserved structural organization, infection of a non-natural host by a species is rare. We investigated the role of CSP in providing the host specificity in P. falciparum infection. CSP from P. falciparum, P. gallinaceum, P. knowlesi, and P. yoelii species representing human, avian, simian, and rodent malaria species were recombinantly expressed, and the proteins were purified to homogeneity. The recombinant proteins were evaluated for their capacity to bind to human liver cell line HepG2 and to prevent P. falciparum sporozoites from invading these cells. The proteins showed significant differences in the binding and sporozoite invasion inhibition activity. Differences among proteins directly correlate with changes in the binding affinity to the sporozoite receptor on liver cells. P. knowlesi CSP (PkCSP) and P. yoelii CSP (PyCSP) had 4,790- and 17,800-fold lower affinity for heparin in comparison to P. falciparum CSP (PfCSP). We suggest that a difference in the binding affinity for the liver cell receptor is a mechanism involved in maintaining the host specificity by the malaria parasite.
dc.description.sponsorshipNational Institute of Allergy and Infectious Diseases
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Biological Chemistry
dc.rightsAttribution 3.0 United States*
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleMolecular Mechanism of Host Specificity in Plasmodium Falciparum Infection: Role of Circumsporozoite Proteinen_US
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.accessRightsOpen Access
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)

Files in this item


This item appears in the following Collection(s)

Show simple item record

CC BY — Creative Commons Attribution
Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution