Open AccessLISP1 is important for the egress of Plasmodium berghei parasites from liver cells
Author(s) -
Ishino Tomoko,
Boisson Bertrand,
Orito Yuki,
Lacroix Céline,
Bischoff Emmanuel,
Loussert Céline,
Janse Chris,
Ménard Robert,
Yuda Masao,
Baldacci Patricia
Publication year - 2009
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/j.1462-5822.2009.01333.x
Subject(s) - biology , plasmodium berghei , apicomplexa , plasmodium (life cycle) , infectivity , intracellular , parasite hosting , intracellular parasite , microbiology and biotechnology , vacuole , virology , malaria , plasmodium falciparum , immunology , cytoplasm , virus , world wide web , computer science
Summary 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 ( li ver‐ s pecific p rotein 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.