The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pearce, E. J.
Right arrow Articles by Sher, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pearce, E. J.
Right arrow Articles by Sher, A.

The Journal of Immunology, Vol 144, Issue 7 2751-2756, Copyright © 1990 by American Association of Immunologists

ARTICLES

Host-specific evasion of the alternative complement pathway by schistosomes correlates with the presence of a phospholipase C- sensitive surface molecule resembling human decay accelerating factor

EJ Pearce, BF Hall and A Sher
Immunology and Cell Biology Section, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.

Schistosoma mansoni parasites recovered from the blood stream were found to be nonactivators of the alternative complement pathway (ACP) when exposed to sera of homologous but not heterologous host species. Schistosomes could be converted into activators of the homologous ACP by treatment with phospholipase C. Antibodies to either human or guinea pig decay accelerating factor (DAF), a 70-kDa glycosylphosphatidylinositol anchored membrane glycoprotein which controls ACP activation on the mammalian cell plasma membrane, bound to the surface of immature schistosomes and immunoprecipitated a molecule of similar molecular mass from detergent extracts of surface iodinated parasites. Phospholipase C treatment drastically reduced the reactivity of the worms with the anti-DAF antibodies. These data suggest that schistosomes evade the ACP by inserting functional host DAF into their surfaces, possibly through adsorption of the molecule's lipophilic diacyglycerol membrane anchor moiety into the outer lipid bilayer of the parasite.


This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
S. Braschi and R. A. Wilson
Proteins Exposed at the Adult Schistosome Surface Revealed by Biotinylation
Mol. Cell. Proteomics, February 1, 2006; 5(2): 347 - 356.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
E. M. Sloand, J. P. Maciejewski, D. Dunn, J. Moss, B. Brewer, M. Kirby, and N. S. Young
Correction of the PNH Defect by GPI-Anchored Protein Transfer
Blood, December 1, 1998; 92(11): 4439 - 4445.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
G. Civenni, S. T. Test, U. Brodbeck, and P. Butikofer
In Vitro Incorporation of GPI-Anchored Proteins Into Human Erythrocytes and Their Fate in the Membrane
Blood, March 1, 1998; 91(5): 1784 - 1792.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
D. Kooyman, G. Byrne, S McClellan, D Nielsen, M Tone, H Waldmann, T. Coffman, K. McCurry, J. Platt, and J. Logan
In vivo transfer of GPI-linked complement restriction factors from erythrocytes to the endothelium
Science, July 7, 1995; 269(5220): 89 - 92.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
S. T. Furlong, K. S. Thibault, and R. A. Rogers
Fluorescent phospholipids preferentially accumulate in sub-tegumental cells of schistosomula of Schistosoma mansoni
J. Cell Sci., November 1, 1992; 103(3): 823 - 830.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.