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. 2023 Feb 2;12(2):237.
doi: 10.3390/pathogens12020237.

Comparative Degradome Analysis of the Bovine Piroplasmid Pathogens Babesia bovis and Theileria annulata

Tomás Javier Poklepovich  1   2 , Maria Mesplet  1   2 , Romina Gallenti  1   2 , Monica Florin-Christensen  1   2 , Leonhard Schnittger  1   2
Affiliations

Comparative Degradome Analysis of the Bovine Piroplasmid Pathogens Babesia bovis and Theileria annulata

Tomás Javier Poklepovich et al. Pathogens. .

Abstract

Babesia bovis and Theileria annulata are tick-borne hemoprotozoans that impact bovine health and are responsible for considerable fatalities in tropical and subtropical regions around the world. Both pathogens infect the same vertebrate host, are closely related, and contain similar-sized genomes; however, they differ in invertebrate host specificity, absence vs. presence of a schizont stage, erythrocyte invasion mechanism, and transovarial vs. transstadial transmission. Phylogenetic analysis and bidirectional best hit (BBH) identified a similar number of aspartic, metallo, and threonine proteinases and nonproteinase homologs. In contrast, a considerably increased number of S54 serine rhomboid proteinases and S9 nonproteinase homologs were identified in B. bovis, whereas C1A cysteine proteinases and A1 aspartic nonproteinase homologs were found to be expanded in T. annulata. Furthermore, a single proteinase of families S8 (subtilisin-like protein) and C12 (ubiquitin carboxyl-terminal hydrolase), as well as four nonproteinase homologs, one with dual domains M23-M23 and three with S9-S9, were exclusively present in B. bovis. Finally, a pronounced difference in species-specific ancillary domains was observed between both species. We hypothesize that the observed degradome differences represent functional correlates of the dissimilar life history features of B. bovis and T. annulata. The presented improved classification of piroplasmid proteinases will facilitate an informed choice for future in-depth functional studies.

Keywords: Babesia bovis; Theileria annulata; bovine babesiosis; comparative degradomics; degradome; peptidases; proteinase repertoire; tropical theileriosis.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Global phylogenetic proteinase wheel of proteinase and nonproteinase homolog domains of B. bovis and T. annulata. The global tree was generated using the protease domain from one member of each catalytic type, and individual family trees were added at the corresponding positions. Colors indicate proteinases of different catalytic types: blue, aspartic type; light yellow, cysteine type; light violet, metallo type; green, serine type, and light brown, threonine type. Species-specific functional proteinases (circles) or nonproteinase homologs (triangles) of B. bovis (red) and T. annulata (green) are designated with their corresponding gene ID. Underlined gene IDs refer to nonproteinase homologs. Clockwise, roman numerals I to VI indicate species-specific paralog families of proteinases and nonproteinase homologs. Remaining designations indicate single species-specific proteinases or nonproteinase homologs. The designation of the proteinase family (MEROPS) is given before the gene ID of B. bovis and T. annulata proteinases and nonproteinase homologs.
Figure 2
Figure 2
Ancillary domains present in proteinases and nonproteinase homologs of B. bovis (right circle) and T. annulata (left circle). Each proteinase sequence was analyzed by Pfam (InterPro) for the presence of nonproteinase domains. Ancillary domains are displayed with their short name according to Pfam.
Figure 3
Figure 3
Bioinformatic pipeline used to identify active proteinases and nonproteinase homologs.
See this image and copyright information in PMC

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