Molecular and biochemical characterization of methionine aminopeptidase of Babesia bovis as a potent drug target

Munkhjargal, Tserendorj; Ishizaki, Takahiro; Guswanto, Azirwan; Takemae, Hitoshi; Yokoyama, Naoki; Igarashi, Ikuo

doi:10.1016/j.vetpar.2016.02.024

Cited by 9 publications

(12 citation statements)

References 43 publications

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“…The SignalP 4.1 server showed that BmMetAP1 had no signal peptide. The secondary structure of BmMetAP1 is similar to those of other known enzymes (Vedro and Chang 2002;Chen et al 2006;Kang et al 2012Kang et al , 2015Munkhjargal et al 2016a), consisting of an MYND-like zinc finger at a less-conserved N-teriminal domain, the signature of the MetAP1 and APP_MetAP subfamily at the highly conserved catalytic C-terminal domain, and a metallopeptidase family M24 domain but no transmembrane structure or signal peptide (Fig. 1a).…”

Section: Resultsmentioning

confidence: 66%

“…BmMetAP1 shared similar biochemical properties with MetAPs of other organisms (Kang et al 2012(Kang et al , 2015, including Babesia (Munkhjargal et al 2016a). BmMetAP1 was found to be catalytically active, as seen by hydrolysis of Met-MCA, the substrate used for the fluorometric determination of methionine aminopeptidases.…”

Section: Enzymatic Profiles Of Rbmmetap1mentioning

confidence: 76%

“…The aminopeptidase activity of BmMetAP1 was assayed fluorometrically based on the hydrolysis of L-methionine 4-methyl-coumaryl-7-amide (Met-MCA; Peptides International, Louisville, KY, USA) in a 96-well microplate format, as described previously (Munkhjargal et al 2016a). Enzyme activity was assayed in buffers with various pHs, ranging from pH 5.0 to 9.0.…”

Section: Enzyme Assaymentioning

confidence: 99%

“…Recombinant MetAP enzymes expressed in E. coli are known to be suitable for the characterization of MetAPs of parasitic pathogens (Narayanan et al 2008;Marschner and Klein 2015;Kang et al 2012Kang et al , 2015Munkhjargal et al 2016a). In the present study, we have successfully expressed rBmMetAP1 protein with a molecular mass of approximately 66.8 kDa in E. coli as a GST-fusion protein (Fig.…”

Section: Characterization Of Metap1 From B Microtimentioning

confidence: 99%

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Recombinant methionine aminopeptidase protein of Babesia microti: immunobiochemical characterization as a vaccine candidate against human babesiosis

2016

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Human babesiosis is the most important zoonotic protozoan infection in the world. This is the first report of the cloning, expression, purification, and immunobiochemical characterization of a methionine aminopeptidase 1 (MetAP1) protein from Babesia microti (B. microti). The gene encodes a MetAP1 protein of B. microti (BmMetAP1) of approximately 66.8 kDa that includes glutathione S-transferase (GST) tag and shows MetAP activity. BmMetAP1 was detected in a lysate of B. microti and further localized in cytoplasm of the B. microti merozoite. rBmMetAP1 was found to be immunogenic, eliciting a high antibody titer in mice. Moreover, rBmMetAP1 stimulated the production of IFN-γ and IL-12 but not IL-4. Finally, rBmMetAP1 was able to provide considerable protection to mice against a B. microti challenge infection based on a reduction in peak parasitemia levels and earlier clearance of the parasite as compared with control mice. Taken together, these results suggest that rBmMetAP1 confers significant protection against experimental B. microti infection and might be considered a potential vaccine target against human babesiosis.

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Section: Resultsmentioning

confidence: 66%

Section: Enzymatic Profiles Of Rbmmetap1mentioning

confidence: 76%

Section: Enzyme Assaymentioning

confidence: 99%

Section: Characterization Of Metap1 From B Microtimentioning

confidence: 99%

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Recombinant methionine aminopeptidase protein of Babesia microti: immunobiochemical characterization as a vaccine candidate against human babesiosis

2016

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“…Some molecules have been investigated because of their physiological importance in microorganisms. Aminopeptidases have been used as therapeutic and prophylactic targets in many parasitic infections and other diseases [32]. In B. bovis, a member of the methionine aminopeptidase (MAP) family was characterized and expressed in E. coli.…”

Section: Pathogenicity Islands (Pais)mentioning

confidence: 99%

Pathogenomics and Molecular Advances in Pathogen Identification

Quiroz-Castañeda¹

2018

Farm Animals Diseases, Recent Omic Trends and New Strategies of Treatment

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Today exists a spread spectrum of tools to be used in pathogen identification. Traditional staining and microscopic methods as well as modern molecular methods are presented in this chapter. Pathogen identification is only the beginning to obtain information related to pathogenicity of the microorganism in the near future. Once the pathogen is identified, genome-sequencing methods will provide a significant amount of information that can be elucidated only through bioinformatics methods. In this point, pathogenomics is a powerful tool to identify potential virulence factors, pathogenicity islands, and many other genes that could be used as therapeutic targets or in vaccine development. In this chapter, we present an update of the molecular advances used to identify pathogens and to obtain information of their diversity. We also review the most recent studies on pathogenomics with a special attention on pathogens of veterinary importance.

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