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Plasmepsin-like Aspartyl Proteases in Babesia

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903725" target="_blank" >RIV/60076658:12310/21:43903725 - isvavai.cz</a>

  • Alternative codes found

    RIV/60077344:_____/21:00555034

  • Result on the web

    <a href="https://www.mdpi.com/2076-0817/10/10/1241" target="_blank" >https://www.mdpi.com/2076-0817/10/10/1241</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/pathogens10101241" target="_blank" >10.3390/pathogens10101241</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Plasmepsin-like Aspartyl Proteases in Babesia

  • Original language description

    Apicomplexan genomes encode multiple pepsin-family aspartyl proteases (APs) that phylogenetically cluster to six independent clades (A to F). Such diversification has been powered by the function-driven evolution of the ancestral apicomplexan AP gene and is associated with the adaptation of various apicomplexan species to different strategies of host infection and transmission through various invertebrate vectors. To estimate the potential roles of Babesia APs, we performed qRT-PCR-based expressional profiling of Babesia microti APs (BmASP2, 3, 5, 6), which revealed the dynamically changing mRNA levels and indicated the specific roles of individual BmASP isoenzymes throughout the life cycle of this parasite. To expand on the current knowledge on piroplasmid APs, we searched the EuPathDB and NCBI GenBank databases to identify and phylogenetically analyse the complete sets of APs encoded by the genomes of selected Babesia and Theileria species. Our results clearly determine the potential roles of identified APs by their phylogenetic relation to their homologues of known function-Plasmodium falciparum plasmepsins (PfPM I-X) and Toxoplasma gondii aspartyl proteases (TgASP1-7). Due to the analogies with plasmodial plasmepsins, piroplasmid APs represent valuable enzymatic targets that are druggable by small molecule inhibitors-candidate molecules for the yet-missing specific therapy for babesiosis.&lt;/p&gt;

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Pathogens

  • ISSN

    2076-0817

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    17

  • Pages from-to

  • UT code for WoS article

    000712318700001

  • EID of the result in the Scopus database

    2-s2.0-85116033411