{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T23:21:36Z","timestamp":1788045696380,"version":"build-2784847793"},"reference-count":79,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,5,16]],"date-time":"2022-05-16T00:00:00Z","timestamp":1652659200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cell Dev. Biol."],"abstract":"<jats:p><jats:italic>Plasmodium falciparum<\/jats:italic> is a unicellular protozoan parasite and causative agent of the most severe form of malaria in humans. The malaria parasite has had to develop sophisticated mechanisms to preserve its proteome under the changing stressful conditions it confronts, particularly when it invades host erythrocytes. Heat shock proteins, especially those that function as molecular chaperones, play a key role in protein homeostasis (proteostasis) of <jats:italic>P. falciparum<\/jats:italic>. Soon after invading erythrocytes, the malaria parasite exports a large number of proteins including chaperones, which are responsible for remodeling the infected erythrocyte to enable its survival and pathogenesis. The infected host cell has parasite-resident and erythrocyte-resident chaperones, which appear to play a vital role in the folding and functioning of <jats:italic>P. falciparum<\/jats:italic> proteins and potentially host proteins. This review critiques the current understanding of how the major chaperones, particularly the Hsp70 and Hsp40 (or J domain proteins, JDPs) families, contribute to proteostasis of the malaria parasite-infected erythrocytes.<\/jats:p>","DOI":"10.3389\/fcell.2022.921739","type":"journal-article","created":{"date-parts":[[2022,5,16]],"date-time":"2022-05-16T08:52:00Z","timestamp":1652691120000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":16,"title":["Plasmodium falciparum Molecular Chaperones: Guardians of the Malaria Parasite Proteome and Renovators of the Host Proteome"],"prefix":"10.3389","volume":"10","author":[{"given":"Gregory L.","family":"Blatch","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,5,16]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"e44605","DOI":"10.1371\/journal.pone.0044605","article-title":"An Exported Heat Shock Protein 40 Associates with Pathogenesis-Related Knobs in Plasmodium falciparum Infected Erythrocytes","volume":"7","author":"Acharya","year":"2012","journal-title":"PloS One"},{"key":"B2","doi-asserted-by":"publisher","first-page":"e1600177","DOI":"10.1002\/prca.201600177","article-title":"Proteome and Structural Organization of the Knob Complex on the Surface of the Plasmodium Infected Red Blood Cell","volume":"12","author":"Alampalli","year":"2018","journal-title":"Proteomics Clin. 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