Peter C. Agre, MD
Molecular Microbiology and Immunology
School of Medicine (Primary)
Center & Institute Affiliation(s):
615 N. Wolfe Street
Baltimore , Maryland 21205
MD , Johns Hopkins School of Medicine , 1974
Aquaglyceroporins in malaria During the rapid growth of malarial parasites within red blood cells, glycerol is taken up by the parasites and incorporated into lipids for membrane biosynthesis. In order for the parasite to have access to glycerol, it must cross the red blood cell plasma membrane and the parasitic plasma membrane. We have shown that aquaglyceroporins are expressed in both membranes in mice. Aquaporin 9 (AQP9) is expressed in the red blood cell plasma membrane and Plasmodium berghei aquaglyceroporin (PbAQP) is expressed in the parasite plasma membrane. We have recently shown that PbAQP null malarial parasites grow more slowly in mice. As a result, mice infected with PbAQP null parasites survive longer than mice infected with wild type parasites. In addition, mice that are deficient in AQP9 survive longer during the initial portion of malarial infection compared to wild type mice. This suggests that aquaglyceroporins are important during malarial infection. Further studies will examine the role of aquaglyceroporins in other stages of the malarial parasite life cycle and their role in the human malarial parasite, Plasmodium falciparum.
Honors and Awards
2000 National Academy of Sciences 2003 Nobel Prize in Chemistry
- water channels
Liu Y, Promeneur D, Rojek A, Kumar N, Frokiaer J, Nielsen S, King LS, Agre P, and Carbrey JM. 2007. Aquaglyceroporin AQP9: The major pathway for glycerol uptake by mouse erythrocytes with implications for malarial virulence. Proc Natl Acad Sci USA 104:12560-4.
Promeneur D, Liu Y, Maciel J, Agre, King LS, and Kumar N. 2007. Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei. Proc Natl Acad Sci USA 104: 2211-16.
Rojek A, Skowronski MT, Fuchtbauer EM, Fuchtbauer AC, Fenton RA, Agre P, Frokiaer J, and Nielsen S. 2007. Defective glycerol metabolism in aquaporin 9 (AQP9) knockout mice. Proc Natl Acad Sci USA 104: 3609-14.
Huang CG, Lamitina T, Agre P, and Strange K. 2007. Functional analysis of the aquaporin gene family in C. elegans. Am J Physiol Cell Physiol 292: C1867-73.
Saparov SM, Liu K, Agre P, and Pohl. 2006. Fast and selective ammonia transport by aquaporin-8. J Biol Chem 282: 5296-5301.