Leishmania tarentolae: Taxonomic classification and its application as a promising biotechnological expression host

PLoS Negl Trop Dis. 2019 Jul 25;13(7):e0007424. doi: 10.1371/journal.pntd.0007424. eCollection 2019 Jul.

Abstract

In this review, we summarize the current knowledge concerning the eukaryotic protozoan parasite Leishmania tarentolae, with a main focus on its potential for biotechnological applications. We will also discuss the genus, subgenus, and species-level classification of this parasite, its life cycle and geographical distribution, and similarities and differences to human-pathogenic species, as these aspects are relevant for the evaluation of biosafety aspects of L. tarentolae as host for recombinant DNA/protein applications. Studies indicate that strain LEM-125 but not strain TARII/UC of L. tarentolae might also be capable of infecting mammals, at least transiently. This could raise the question of whether the current biosafety level of this strain should be reevaluated. In addition, we will summarize the current state of biotechnological research involving L. tarentolae and explain why this eukaryotic parasite is an advantageous and promising human recombinant protein expression host. This summary includes overall biotechnological applications, insights into its protein expression machinery (especially on glycoprotein and antibody fragment expression), available expression vectors, cell culture conditions, and its potential as an immunotherapy agent for human leishmaniasis treatment. Furthermore, we will highlight useful online tools and, finally, discuss possible future applications such as the humanization of the glycosylation profile of L. tarentolae or the expression of mammalian recombinant proteins in amastigote-like cells of this species or in amastigotes of avirulent human-pathogenic Leishmania species.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biotechnology / methods*
  • Glycosylation
  • Humans
  • Leishmania / classification*
  • Leishmania / pathogenicity
  • Leishmaniasis
  • Protein Processing, Post-Translational
  • Recombinant Proteins / biosynthesis*

Substances

  • Recombinant Proteins

Grants and funding

The authors (SK and ZK) acknowledge support by the German Federal Ministry for Education and Research (BMBF) through grant no. 0315941B. Additionally, ZK acknowledges financial support through the German Federal Ministry of Economic Affairs and Energy (ZIM Program, grant no. 16KN041839). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.