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Cell Stress and Chaperones

, Volume 24, Issue 1, pp 125–148 | Cite as

The Hsp70/J-protein machinery of the African trypanosome, Trypanosoma brucei

  • Stephen John Bentley
  • Miebaka Jamabo
  • Aileen BoshoffEmail author
Original Paper
  • 111 Downloads

Abstract

The etiological agent of the neglected tropical disease African trypanosomiasis, Trypanosoma brucei, possesses an expanded and diverse repertoire of heat shock proteins, which have been implicated in cytoprotection, differentiation, as well as progression and transmission of the disease. Hsp70 plays a crucial role in proteostasis, and inhibition of its interactions with co-chaperones is emerging as a potential therapeutic target for numerous diseases. In light of genome annotations and the release of the genome sequence of the human infective subspecies, an updated and current in silico overview of the Hsp70/J-protein machinery in both T. brucei brucei and T. brucei gambiense was conducted. Functional, structural, and evolutionary analyses of the T. brucei Hsp70 and J-protein families were performed. The Hsp70 and J-proteins from humans and selected kinetoplastid parasites were used to assist in identifying proteins from T. brucei, as well as the prediction of potential Hsp70–J-protein partnerships. The Hsp70 and J-proteins were mined from numerous genome-wide proteomics studies, which included different lifecycle stages and subcellular localisations. In this study, 12 putative Hsp70 proteins and 67 putative J-proteins were identified to be encoded on the genomes of both T. brucei subspecies. Interestingly there are 6 type III J-proteins that possess tetratricopeptide repeat-containing (TPR) motifs. Overall, it is envisioned that the results of this study will provide a future context for studying the biology of the African trypanosome and evaluating Hsp70 and J-protein interactions as potential drug targets.

Keywords

African trypanosomiasis Trypanosoma brucei Hsp70 J-protein Hsp110 

Notes

Funding information

This work was funded by a grant from the National Research Foundation (NRF), grant number 87663. S.J.B. is the recipient of an NRF Doctoral Innovation Scholarship. M.J. is the recipient of an NRF DAAD Fellowship.

Supplementary material

12192_2018_950_MOESM1_ESM.docx (221 kb)
Fig. S1 Alignment of the Hsp70 superfamily from T. brucei in relation to human and other selected kinetoplastids. Multiple sequence alignment of the full-length amino acid sequences was performed using the in-built ClustalW program (Larkin et al. 2007) with default parameters in the MEGA7 software (Kumar et al. 2016). Degree of amino acid conservation is symbolized by the following: (*) all fully conserved residues; (:) one of the residues is fully conserved and (.) residues are weakly conserved. Accession numbers for the J-protein amino acid sequences used in this study are provided in Table 1 and Table S1. (DOCX 220 kb)
12192_2018_950_Fig4_ESM.png (274 kb)
Fig. S2

Schematic representation of the domain architecture of the HSPA/Hsp70 proteins in T. brucei. Each protein sequence for the T. brucei HSPA/Hsp70 family is represented by an open bar with the number of amino acids indicated on either side of the protein bar with the various protein domains and other associated features that were identified using Prosite (Sigrist et al. 2009) and SMART (Letunic et al. 2012). These domains and associated features include the N-terminal nucleotide binding domain (NBD; blue), substrate binding domain (SBD I; light green), C-terminal region (SBD II; yellow) and targeting signal peptides (S; pink). The molecular weight (MW), and isoelectric point (pI) for each T. brucei Hsp70 protein was calculated using the compute pI/Mw tool from ExPASy (https://web.expasy.org/compute_pi/; Gasteiger et al. 2005). Data on the phenotypic knockdown screen, using RNAi conducted by Alsford et al. (2011), for HSPA/Hsp70 protein member is provided: ALL-All lifecycle stages; BSF- Bloodstream; DIFF- Differentiation; NE- Non-essential; ND-Not determined. (PNG 273 kb)

12192_2018_950_MOESM2_ESM.tif (607 kb)
High resolution image (TIF 607 kb)
12192_2018_950_Fig5_ESM.png (199 kb)
Fig. S3

Schematic representation of the domain architecture of the HSPH/Hsp110 proteins in T. brucei. Each protein sequence for the T. brucei HSPH/Hsp110 family is represented by an open bar with the number of amino acids indicated on either side of the protein bar with the various protein domains and other associated features that were identified using Prosite (Sigrist et al. 2009) and SMART (Letunic et al. 2012). These domains and associated features include the N-terminal nucleotide binding domain (NBD; blue), substrate binding domain (SBD I; dark green), C-terminal region (SBD II; yellow) and targeting signal peptides (S; pink). The molecular weight (MW), and isoelectric point (pI) for each T. brucei Hsp110 protein was calculated using the compute pI/Mw tool from ExPASy (https://web.expasy.org/compute_pi/; Gasteiger et al. 2005). Data on the phenotypic knockdown screen, using RNAi conducted by Alsford et al. (2011), for HSPH/Hsp110 protein member is provided: ALL-All lifecycle stages; BSF- Bloodstream; DIFF- Differentiation. (PNG 199 kb)

12192_2018_950_MOESM3_ESM.tif (509 kb)
High resolution image (TIF 508 kb)
12192_2018_950_MOESM4_ESM.docx (105 kb)
Fig. S4 Alignment of the Type I, II and IV J-protein subfamilies from T. brucei in relation to human and other selected kinetoplastids. Multiple sequence alignment of the full-length amino acid sequences was performed using the in-built ClustalW program (Larkin et al. 2007) with default parameters in the MEGA7 software (Kumar et al. 2016). Degree of amino acid conservation is symbolized by the following: (*) all fully conserved residues; (:) one of the residues is fully conserved and (.) residues are weakly conserved. Accession numbers for the J-protein amino acid sequences used in this study are provided in Table 2 and Table S2. (DOCX 104 kb)
12192_2018_950_MOESM5_ESM.docx (28 kb)
Table S1 Accession numbers for HSPA/Hsp70 and HSPH/Hsp110 amino acid sequences used in this study. (DOCX 27 kb)
12192_2018_950_MOESM6_ESM.docx (24 kb)
Table S2 Accession numbers for J-protein amino acid sequences used in this study. (DOCX 23 kb)

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© Cell Stress Society International 2018

Authors and Affiliations

  1. 1.Biotechnology Innovation CentreRhodes UniversityGrahamstownSouth Africa

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