Literature DB >> 32244008

Relevance and proteomics challenge of functional posttranslational modifications in Kinetoplastid parasites.

R Manzano-Román1, M Fuentes2.   

Abstract

Protozoan parasitic infections are health, social and economic issues impacting both humans and animals, with significant morbidity and mortality worldwide. Protozoan parasites have complicated life cycles with both intracellular and extracellular forms. As a consequence, protozoan adapt to changing environments in part through a dynamic enzyme-catalyzed process leading to reversible posttranslational modifications (PTMs). The characterization by proteomics approaches reveals the critical role of the PTMs of the proteins involved in host-pathogen interaction. The complexity of PTMs characterization is increased by the high diversity, stoichiometry, dynamic and also co-existence of several PTMs in the same moieties which crosstalk between them. Here, we review how to understand the complexity and the essential role of PTMs crosstalk in order to provide a new hallmark for vaccines developments, immunotherapies and personalized medicine. In addition, the importance of these motifs in the biology and biological cycle of kinetoplastid parasites is highlighted with key examples showing the potential to act as targets against protozoan diseases.
Copyright © 2020 Elsevier B.V. All rights reserved.

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Keywords:  Crosstalk; Posttranslational modifications; Protein function; Protozoan parasites; Signaling

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Year:  2020        PMID: 32244008     DOI: 10.1016/j.jprot.2020.103762

Source DB:  PubMed          Journal:  J Proteomics        ISSN: 1874-3919            Impact factor:   4.044


  1 in total

1.  The Experimental Proteome of Leishmania infantum Promastigote and Its Usefulness for Improving Gene Annotations.

Authors:  África Sanchiz; Esperanza Morato; Alberto Rastrojo; Esther Camacho; Sandra González-de la González-de la Fuente; Anabel Marina; Begoña Aguado; Jose M Requena
Journal:  Genes (Basel)       Date:  2020-09-02       Impact factor: 4.096

  1 in total

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