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Review
. 2014 Apr 29:5:153.
doi: 10.3389/fpls.2014.00153. eCollection 2014.

Transport proteins of parasitic protists and their role in nutrient salvage

Affiliations
Review

Transport proteins of parasitic protists and their role in nutrient salvage

Paul Dean et al. Front Plant Sci. .

Abstract

The loss of key biosynthetic pathways is a common feature of important parasitic protists, making them heavily dependent on scavenging nutrients from their hosts. This is often mediated by specialized transporter proteins that ensure the nutritional requirements of the parasite are met. Over the past decade, the completion of several parasite genome projects has facilitated the identification of parasite transporter proteins. This has been complemented by functional characterization of individual transporters along with investigations into their importance for parasite survival. In this review, we summarize the current knowledge on transporters from parasitic protists and highlight commonalities and differences in the transporter repertoires of different parasitic species, with particular focus on characterized transporters that act at the host-pathogen interface.

Keywords: amino acid; hexose; parasite; protist; protozoa; purine; transport; transporter.

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Figures

Figure 1
Figure 1
Schematic representation of the diversity of experimentally-verified transport proteins located on the surface membrane of parasitic protists based upon published data. All transporters shown are given and discussed in the main text. Three transporters located in mitochondria derived organelles are also indicated. See main text for all abbreviations used for species and transporters.
Figure 2
Figure 2
Transport protein repertoires of parasitic protists. Prediction of transporters was taken from the literature where indicated or obtained from the TransportDB database (Ren et al., 2007). Nomenclature of transporters is consistent with that given in TransportDB. Transporter proteins shown are those only found in the selected parasites, as those having no hits in any parasite were omitted. Most transporters are not experimentally verified and their subcellular location has not been determined (see Table 1). Key: *Expanded protein families from the analysis of 9 species of microsporidia. The 24 additional yeast transporters can be found in the TransportDB database and comprise 10 transporter families. (a) Data for microsporidian transporters were taken from (Heinz et al., 2012). (b) Includes proteins that possess an ABC transporter domain (PFAM:PF00005, e-value cutoff < 1e-5) using InterProScan. 4.8. Values taken from (c) (Kay et al., 2012), (d) (Sauvage et al., 2009), (e) (Beitz, 2005), and (f) (Heinz et al., 2012). Cp, Cryptosporidium parvum; Eh, Entamoeba histolytica; Lm, Leishmania major; Pf, Plasmodium falciparum; Tg, Toxoplasma gondii; Tv, Trichomonas vaginalis; Tb, Trypanosoma brucei; Th, Trachipleistophora hominis; Ec, Encephalitozoon cuniculi. Sc, Saccharomyces cerevisiae.

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References

    1. Acimovic Y., Coe I. R. (2002). Molecular evolution of the equilibrative nucleoside transporter family: identification of novel family members in prokaryotes and eukaryotes. Mol. Biol. Evol. 19, 2199–2210 10.1093/oxfordjournals.molbev.a004044 - DOI - PubMed
    1. Ali V., Shigeta Y., Tokumoto U., Takahashi Y., Nozaki T. (2004). An intestinal parasitic protist, Entamoeba histolytica, possesses a non-redundant nitrogen fixation-like system for iron-sulfur cluster assembly under anaerobic conditions. J. Biol. Chem. 279, 16863–16874 10.1074/jbc.M313314200 - DOI - PubMed
    1. Arastu-Kapur S., Arendt C. S., Purnat T., Carter N. S., Ullman B. (2005). Second-site suppression of a nonfunctional mutation within the Leishmania donovani inosine-guanosine transporter. J. Biol. Chem. 280, 2213–2219 10.1074/jbc.M408224200 - DOI - PubMed
    1. Arastu-Kapur S., Ford E., Ullman B., Carter N. S. (2003). Functional analysis of an inosine-guanosine transporter from Leishmania donovani. The role of conserved residues, aspartate 389 and arginine 393. J. Biol. Chem. 278, 33327–33333 10.1074/jbc.M305141200 - DOI - PubMed
    1. Audia J. P., Winkler H. H. (2006). Study of the five Rickettsia prowazekii proteins annotated as ATP/ADP translocases (Tlc): only Tlc1 transports ATP/ADP, while Tlc4 and Tlc5 transport other ribonucleotides. J. Bacteriol. 188, 6261–6268 10.1128/JB.00371-06 - DOI - PMC - PubMed

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