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INFECTION AND IMMUNITY, July 2010, p. 29272936 Vol. 78, No. 7 0019-9567/10/$12.00 doi:10.1128/IAI.00077-10

Summary: INFECTION AND IMMUNITY, July 2010, p. 29272936 Vol. 78, No. 7
0019-9567/10/$12.00 doi:10.1128/IAI.00077-10
Copyright 2010, American Society for Microbiology. All Rights Reserved.
Cholangiocyte Myosin IIB Is Required for Localized Aggregation of
Sodium Glucose Cotransporter 1 to Sites of Cryptosporidium parvum
Cellular Invasion and Facilitates Parasite Internalization
Steven P. O'Hara,* Gabriella B. Gajdos, Christy E. Trussoni,
Patrick L. Splinter, and Nicholas F. LaRusso
Miles and Shirley Fiterman Center for Digestive Diseases, Division of Gastroenterology and Hepatology, and
Mayo Clinic Center for Cell Signaling, Mayo Clinic, Rochester, Minnesota 55905
Received 22 January 2010/Returned for modification 1 March 2010/Accepted 30 April 2010
Internalization of the obligate intracellular apicomplexan parasite, Cryptosporidium parvum, results in the
formation of a unique intramembranous yet extracytoplasmic niche on the apical surfaces of host epithelial
cells, a process that depends on host cell membrane extension. We previously demonstrated that efficient C.
parvum invasion of biliary epithelial cells (cholangiocytes) requires host cell actin polymerization and localized
membrane translocation/insertion of Na /glucose cotransporter 1 (SGLT1) and of aquaporin 1 (Aqp1), a water
channel, at the attachment site. The resultant localized water influx facilitates parasite cellular invasion by
promoting host-cell membrane protrusion. However, the molecular mechanisms by which C. parvum induces
membrane translocation/insertion of SGLT1/Aqp1 are obscure. We report here that cultured human cholan-
giocytes express several nonmuscle myosins, including myosins IIA and IIB. Moreover, C. parvum infection of


Source: Arnold, Jonathan - Nanoscale Science and Engineering Center & Department of Genetics, University of Georgia


Collections: Biotechnology