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A Plasmodium berghei putative serine-threonine kinase 2 (PBANKA_0311400) is required for late liver stage development and timely initiation of blood stage infection.

ABSTRACT: In Plasmodium, protein kinases govern key biological processes of the parasite life cycle involved in the establishment of infection, dissemination and sexual reproduction. The rodent malaria model P lasmodium berghei encodes for 66 putative eukaryotic protein kinases (ePKs) as identified through modelling domain signatures and are highly conserved in Plasmodium falciparum We report here the functional characterisation of a putative serine-threonine kinase P BANKA_0311400 identified in this kinome analysis and designate it as Pbstk2 To elucidate its role, we knocked out Pbstk2 locus and performed a detailed phenotypic analysis at different life cycle stages. The Pbstk2 knockout (KO) was not compromised in asexual blood stage propagation, transmission and development in the mosquito vector. The Pbstk2 KO produced viable salivary gland sporozoites that successfully transformed into exo-erythrocytic forms (EEFs) and were morphologically indistinguishable from wild-type GFP (WT GFP) with regard to size and shape until 48?h. An intravenous dose of 1×103 Pbstk2 KO sporozoites in C57BL/6 mice failed to establish blood stage infection and a higher dose of 5X103 showed a 2-3?day delay in prepatency as compared to WT GFP parasites. Consistent with such an observation, analysis of in vitro EEF development at 62?h revealed that the hepatic merozoite numbers were reduced to nearly 40% as compared to WT GFP and showed meagre expression of MSP1. Our studies provide evidence for the role of PbSTK2 in late liver stage development and for the successful establishment of a timely blood stage infection.

SUBMITTER: Jillapalli R

PROVIDER: S-EPMC6737972 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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A Plasmodium berghei putative serine-threonine kinase 2 (PBANKA_0311400) is required for late liver stage development and timely initiation of blood stage infection.

Jillapalli Ravi R Narwal Sunil Kumar SK Kolli Surendra Kumar SK Mastan Babu S BS Segireddy Rameswara Reddy RR Dey Sandeep S Srivastava Pratik Narain PN Mishra Satish S Kumar Kota Arun KA

Biology open 20190823 8

In Plasmodium, protein kinases govern key biological processes of the parasite life cycle involved in the establishment of infection, dissemination and sexual reproduction. The rodent malaria model P lasmodium berghei encodes for 66 putative eukaryotic protein kinases (ePKs) as identified through modelling domain signatures and are highly conserved in Plasmodium falciparum We report here the functional characterisation of a putative serine-threonine kinase P <i ...[more]

PMID: 31444161

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Project description:BACKGROUND: Serine/threonine kinases (STKs) have been found in an increasing number of prokaryotes, showing important roles in signal transduction that supplement the well known role of two-component system. Cyanobacteria are photoautotrophic prokaryotes able to grow in a wide range of ecological environments, and their signal transduction systems are important in adaptation to the environment. Sequence information from several cyanobacterial genomes offers a unique opportunity to conduct a comprehensive comparative analysis of this kinase family. In this study, we extracted information regarding Ser/Thr kinases from 21 species of sequenced cyanobacteria and investigated their diversity, conservation, domain structure, and evolution. RESULTS: 286 putative STK homologues were identified. STKs are absent in four Prochlorococcus strains and one marine Synechococcus strain and abundant in filamentous nitrogen-fixing cyanobacteria. Motifs and invariant amino acids typical in eukaryotic STKs were conserved well in these proteins, and six more cyanobacteria- or bacteria-specific conserved residues were found. These STK proteins were classified into three major families according to their domain structures. Fourteen types and a total of 131 additional domains were identified, some of which are reported to participate in the recognition of signals or substrates. Cyanobacterial STKs show rather complicated phylogenetic relationships that correspond poorly with phylogenies based on 16S rRNA and those based on additional domains. CONCLUSION: The number of STK genes in different cyanobacteria is the result of the genome size, ecophysiology, and physiological properties of the organism. Similar conserved motifs and amino acids indicate that cyanobacterial STKs make use of a similar catalytic mechanism as eukaryotic STKs. Gene gain-and-loss is significant during STK evolution, along with domain shuffling and insertion. This study has established an overall framework of sequence-structure-function interactions for the STK gene family, which may facilitate further studies of the role of STKs in various organisms.

Dataset Information

A Plasmodium berghei putative serine-threonine kinase 2 (PBANKA_0311400) is required for late liver stage development and timely initiation of blood stage infection.

Publications

A <i>Plasmodium berghei</i> putative serine-threonine kinase 2 (<i>PBANKA_0311400</i>) is required for late liver stage development and timely initiation of blood stage infection.

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