PV1 Protein from <i>Plasmodium falciparum</i> Exhibits Chaperone-Like Functions and Cooperates with Hsp100s

• Main Authors: Kazuaki Hakamada, Manami Nakamura, Rio Midorikawa, Kyosuke Shinohara, Keiichi Noguchi, Hikaru Nagaoka, Eizo Takashima, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Akihiro Kawamoto, Masafumi Yohda
• Format: Article
• Language: English
• Published: MDPI AG 2020-11-01
• Series: International Journal of Molecular Sciences
• Subjects: malaria; <i>Plasmodium falciparum</i>; translocon; chaperone unfolding; transport
• Online Access: https://www.mdpi.com/1422-0067/21/22/8616

<i>Plasmodium falciparum</i> 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 <i>Plasmodium</i> 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.