ArticleParasitology international2009
Enzymatic characterization of the Plasmodium vivax chitinase, a potential malaria transmission-blocking target.
Article in Parasitology international, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- The chemistry and biology of natural ribomimetics and related compounds.RSC chemical biology · 2022Review
- Evolutionary Insights into the Microneme-Secreted, Chitinase-Containing High-Molecular-Weight Protein Complexes Involved inInfection and immunity · 2022Article
- Plasmodium chitinases: revisiting a target of transmission-blockade against malaria.Protein science : a publication of the Protein Society · 2021Review
- A Hetero-Multimeric Chitinase-ContainingFrontiers in cellular and infection microbiology · 2020Article
- Expression of functional Plasmodium falciparum enzymes using a wheat germ cell-free system.Eukaryotic cell · 2013Article
- Novel biological activities of allosamidins.Molecules (Basel, Switzerland) · 2013Review
- Limited sequence polymorphisms of four transmission-blocking vaccine candidate antigens in Plasmodium vivax Korean isolates.Malaria journal · 2013Article
- Platform for Plasmodium vivax vaccine discovery and development.Memorias do Instituto Oswaldo Cruz · 2011Review
- Production of chitooligosaccharides and their potential applications in medicine.Marine drugs · 2010Review
- Contributions of Francisella tularensis subsp. novicida chitinases and Sec secretion system to biofilm formation on chitin.Applied and environmental microbiology · 2010Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The chitinase (EC 3.2.1.14) of the human malaria parasite Plasmodium falciparum, PfCHT1, has been validated as a malaria transmission-blocking vaccine (TBV). The present study aimed to delineate functional characteristics of the P. vivax chitinase PvCHT1, whose primary structure differs from that of PfCHT1 by having proenzyme and chitin-binding domains. The recombinant protein rPvCHT1 expressed with a wheat germ cell-free system hydrolyzed 4-methylumbelliferone (4MU) derivatives of chitin oligosaccharides (beta-1,4-poly-N-acetyl glucosamine (GlcNAc)). An anti-rPvCHT1 polyclonal antiserum reacted with in vitro-obtained P. vivax ookinetes in anterior cytoplasm, showing uneven patchy distribution. Enzymatic activity of rPvCHT1 shared the exclusive endochitinase property with parallelly expressed rPfCHT1 as demonstrated by a marked substrate preference for 4MU-GlcNAc(3) compared to shorter GlcNAc substrates. While rPvCHT1 was found to be sensitive to the general family-18 chitinase inhibitor, allosamidin, its pH (maximal in neutral environment) and temperature (max. at approximately 25 degrees C) activity profiles and sensitivity to allosamidin (IC50=6 microM) were different from rPfCHT1. The results in this first report of functional rPvCHT1 synthesis indicate that the P. vivax chitinase is enzymatically close to long form Plasmodium chitinases represented by P. gallinaceum PgCHT1.
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Registered trials
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