Critical role for heat shock protein 20 (HSP20) in migration of malarial sporozoites

GEORGINA N. MONTAGNA; CARLOS A BUSCAGLIA; SILVIA MÜNTER; CHRISTIAN GOOSMANN; FRIEDRICH FRISCHKNECHT1; VOLKER BRINKMANN; KAI MATUSCHEWSKI

JOURNAL OF BIOLOGICAL CHEMISTRY

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Lugar: Bethesda, Maryland; Año: 2012

0021-9258

Plasmodium sporozoites, single cell eukaryotic pathogens,use their own actin/myosin-based motor machinery for lifecycle progression, which includes forward locomotion, penetrationof cellular barriers, and invasion of target cells. To displayfast gliding motility, the parasite uses a high turnover of actinpolymerization and adhesion sites. Paradoxically, only a fewclassic actin regulatory proteins appear to be encoded in thePlasmodium genome. Small heat shock proteins have been associatedwith cytoskeleton modulation in various biological processes.In this study, we identify HSP20 as a novel player in Plasmodiummotility and provide molecular genetics evidence for acritical role of a small heat shock protein in cell traction andmotility. We demonstrate that HSP20 ablation profoundlyaffects sporozoite-substrate adhesion, which translates intoaberrant speed and directionality in vitro. Loss of HSP20 functionimpairs migration in the host, an important sporozoite traitrequired to find a blood vessel and reach the liver after beingdeposited in the skin by the mosquito. Our study also shows thatfast locomotion of sporozoites is crucial during natural malariatransmission.