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oai:repisalud.isciii.es:20.500.12105/151822024-09-27T21:51:12Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Solana, Jose C. author Bernardo, Lorena author Moreno, Javier author Aguado, Begoña author Requena, Jose M author 2022-04-23 Abrupt environmental changes are faced by Leishmania parasites during transmission from a poikilothermic insect vector to a warm-blooded host. Adaptation to harsh environmental conditions, such as nutrient deprivation, hypoxia, oxidative stress and heat shock needs to be accomplished by rapid reconfiguration of gene expression and remodeling of protein interaction networks. Chaperones play a central role in the maintenance of cellular homeostasis, and they are responsible for crucial tasks such as correct folding of nascent proteins, protein translocation across different subcellular compartments, avoiding protein aggregates and elimination of damaged proteins. Nearly one percent of the gene content in the Leishmania genome corresponds to members of the HSP40 family, a group of proteins that assist HSP70s in a variety of cellular functions. Despite their expected relevance in the parasite biology and infectivity, little is known about their functions or partnership with the different Leishmania HSP70s. Here, we summarize the structural features of the 72 HSP40 proteins encoded in the Leishmania infantum genome and their classification into four categories. A review of proteomic data, together with orthology analyses, allow us to postulate cellular locations and possible functional roles for some of them. A detailed study of the members of this family would provide valuable information and opportunities for drug discovery and improvement of current treatments against leishmaniasis. Genes (Basel). 2022 Apr 23;13(5):742. 10.3390/genes13050742 2073-4425 Genes 35627127 http://hdl.handle.net/20.500.12105/15182 Leishmania HSP40 J-domain protein (JDP) Molecular chaperones The Astonishing Large Family of HSP40/DnaJ Proteins Existing in Leishmania