Cryptosporidium spp. are waterborne apicomplexan parasites responsible for outbreaks of diarrheal disease worldwide. Antigens involved in zoite invasion into host cells have been the focus of many investigations as these may prove to be good vaccine candidates. gp40/15 is a zoite antigen synthesized as a precursor protein and proteolytically cleaved into the mature glycoproteins, gp40 and gp15. gp15 is anchored in the sporozoite membrane by a glycosylphosphatidyl inositol moiety, while gp40 is predicted to be soluble. However, gp40 bears epitopes that recognize a host cell receptor. If this interaction is important for zoite invasion, then gp40 must have some mechanism of associating with the parasite membrane. In these studies we demonstrate that gp40 and gp15 co-localize to the surface membrane of sporozoites and merozoites, and co-immunoprecipitate, suggesting that these antigens associate after proteolytic cleavage to generate a protein complex capable of linking zoite and host cell surfaces.
|Original language||English (US)|
|Number of pages||4|
|Journal||Molecular and Biochemical Parasitology|
|State||Published - Nov 2007|
Bibliographical noteFunding Information:
This work was supported by NIH grants K01DK062816 (R.M.O.), RO1 AI05786 (H. D.W.) and the GRASP Digestive Diseases Center at Tufts-New England Medical Center (P30 DK34928-18). We would like to thank Delynn Moss and Michael Arrowood for Cryptosporidium antigen preparation. Use of trade names is for identification only and does not imply endorsement by the Public Health Service or by the U.S. Department of Health and Human Services. The findings and conclusions in this report are those of the author(s) and do not necessarily represent the views of the Centers for Disease Control and Prevention.