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A de novo peptide from a high throughput peptide library blocks myosin a-mtip complex formation in plasmodium falciparum
Anam Z.E., Joshi N., Gupta S., Yadav P., Chaurasiya A., Kahlon A.K., Kaushik S., Munde M., Ranganathan A., Singh S.
Published in MDPI AG
PMID: 32859024
Volume: 21
Issue: 17
Pages: 1 - 17
Apicomplexan parasites, through their motor machinery, produce the required propulsive force critical for host cell-entry. The conserved components of this so-called glideosome machinery are myosin A and myosin A Tail Interacting Protein (MTIP). MTIP tethers myosin A to the inner membrane complex of the parasite through 20 amino acid-long C-terminal end of myosin A that makes direct contacts with MTIP, allowing the invasion of Plasmodium falciparum in erythrocytes. Here, we discovered through screening a peptide library, a de-novo peptide ZA1 that binds the myosin A tail domain. We demonstrated that ZA1 bound strongly to myosin A tail and was able to disrupt the native myosin A tail MTIP complex both in vitro and in vivo. We then showed that a shortened peptide derived from ZA1, named ZA1S, was able to bind myosin A and block parasite invasion. Overall, our study identified a novel anti-malarial peptide that could be used in combination with other antimalarials for blocking the invasion of Plasmodium falciparum. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
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Published in MDPI AG
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