Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/1165
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dc.contributor.authorSingh, Agam P-
dc.contributor.authorPandey, Kailash C.-
dc.contributor.authorPande, Veena-
dc.contributor.authorSaxena, Ajay K.-
dc.contributor.authorAbid, Mohammad-
dc.contributor.authorKumar, Bhumika-
dc.contributor.authorVerma, Sonia-
dc.contributor.authorKashif, Mohammad-
dc.contributor.authorSharma, Ruby-
dc.contributor.authorAtul-
dc.contributor.authorDixit, Rajnikant-
dc.date.accessioned2021-03-03T09:08:59Z-
dc.date.available2021-03-03T09:08:59Z-
dc.date.issued2019-10-
dc.identifier.urihttp://hdl.handle.net/123456789/1165-
dc.description.abstractMetacaspases are clan CD cysteine peptidases found in plants, fungi and protozoa that possess a conserved Peptidase_C14 domain, homologous to the human caspases and a catalytic His/Cys dyad. Earlier reports have indicated the role of metacaspases in cell death; however, metacaspases of human malaria parasite remains poorly understood. In this study, we aimed to functionally characterize a novel malarial protease, P. falciparum metacaspase-3 (PfMCA3). Unlike other clan CD peptidases, PfMCA3 has an atypical active site serine (Ser1865) residue in place of canonical cysteine and it phylogenetically forms a distinct branch across the species. To investigate whether this domain retains catalytic activity, we expressed, purified and refolded the Peptidase_C14 domain of PfMCA3 which was found to express in all asexual stages. PfMCA3 exhibited trypsin-like serine protease activity with ser1865 acting as catalytic residue to cleave trypsin oligopeptide substrate. PfMCA3 is inhibited by trypsin-like serine protease inhibitors. Our study found that PfMCA3 enzymatic activity was abrogated when catalytic serine1865 (S1865A) was mutated. Moreover, PfMCA3 was found to be inactive against caspase substrate. Overall, our study characterizes a novel metacaspase of P. falciparum, different from human caspases and not responsible for the caspase-like activity, therefore, could be considered as a potential chemotherapeutic target.en_US
dc.language.isoenen_US
dc.publisherElsevier B.V.en_US
dc.subjectCaspase; Chemotherapeutic; Cysteine peptidase; Metacaspase-3; Peptidase_C14; Serine proteaseen_US
dc.titleMetacaspase-3 of Plasmodium falciparum: An atypical trypsin-like serine proteaseen_US
dc.typeArticleen_US
dc.journalInt J Biol Macromolen_US
dc.volumeno138en_US
dc.pages309-320en_US
Appears in Collections:Infectious Disease, Publications

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