LISP1 is important for the egress of Plasmodium berghei parasites from liver cells.
Most Apicomplexa are obligatory intracellular parasites that multiply inside a so-called parasitophorous vacuole (PV) formed upon parasite entry into the host cell. Plasmodium, the agent of malaria and the Apicomplexa most deadly to humans, multiplies in both hepatocytes and erythrocytes in the mammalian host. Although much has been learned on how Apicomplexa parasites invade host cells inside a PV, little is known of how they rupture the PV membrane and egress host cells. Here, we characterize a Plasmodium protein, called LISP1 (liver-specific protein 1), which is specifically involved in parasite egress from hepatocytes. LISP1 is expressed late during parasite development inside hepatocytes and locates at the PV membrane. Intracellular parasites deficient in LISP1 develop into hepatic merozoites, which display normal infectivity to erythrocytes. However, LISP1-deficient liver-stage parasites do not rupture the membrane of the PV and remain trapped inside hepatocytes. LISP1 is the first Plasmodium protein shown by gene targeting to be involved in the lysis of the PV membrane.
Institut Pasteur, Biologie et Génétique du Paludisme, 75724 Paris cedex 15, France.
Tomoko
T
Ishino
Bertrand
B
Boisson
Yuki
Y
Orito
Céline
C
Lacroix
Emmanuel
E
Bischoff
Céline
C
Loussert
Chris
C
Janse
Robert
R
Ménard
Masao
M
Yuda
Patricia
P
Baldacci
D000818:Animals; D017353:Gene Deletion; D020869:Gene Expression Profiling; D018390:Gene Targeting; D008099:Liver / Q000469:parasitology*; D008969:Molecular Sequence Data; D010962:Plasmodium berghei / Q000235:genetics / Q000502:physiology*; D015800:Protozoan Proteins / Q000235:genetics / Q000502:physiology*; D014617:Vacuoles / Q000469:parasitology*
D015800:Protozoan Proteins