PV1 Protein from Plasmodium falciparum Exhibits Chaperone-Like Functions and Cooperates with Hsp100s

parasitophorous vacuolar protein 1 (PfPV1), a protein unique to malaria parasites, is localized in the parasitophorous vacuolar (PV) and is essential for parasite growth. Previous studies suggested that PfPV1 cooperates with the translocon of exported proteins (PTEX) complex to export various protei...

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Bibliographic Details
Published in:International journal of molecular sciences 2020-11, Vol.21 (22), p.8616
Main Authors: Hakamada, Kazuaki, Nakamura, Manami, Midorikawa, Rio, Shinohara, Kyosuke, Noguchi, Keiichi, Nagaoka, Hikaru, Takashima, Eizo, Morishima, Ken, Inoue, Rintaro, Sugiyama, Masaaki, Kawamoto, Akihiro, Yohda, Masafumi
Format: Article
Language:English
Subjects:
chaperone unfolding
Chaperones
Chromatography
Disaggregation
Heat-Shock Proteins - chemistry
Humans
Insulin
Malaria
Parasites
Plasmodium falciparum
Plasmodium falciparum - chemistry
Proteins
Protozoan Proteins - chemistry
Structure-function relationships
translocon
transport
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Summary:parasitophorous vacuolar protein 1 (PfPV1), a protein unique to malaria parasites, is localized in the parasitophorous vacuolar (PV) and is essential for parasite growth. Previous studies suggested that PfPV1 cooperates with the translocon of exported proteins (PTEX) complex to export various proteins from the PV. However, the structure and function of PfPV1 have not been determined in detail. In this study, we undertook the expression, purification, and characterization of PfPV1. The tetramer appears to be the structural unit of PfPV1. The activity of PfPV1 appears to be similar to that of molecular chaperones, and it may interact with various proteins. PfPV1 could substitute CtHsp40 in the CtHsp104, CtHsp70, and CtHsp40 protein disaggregation systems. Based on these results, we propose a model in which PfPV1 captures various PV proteins and delivers them to PTEX through a specific interaction with HSP101.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms21228616