In:
International Journal of Molecular Sciences, MDPI AG, Vol. 21, No. 17 ( 2020-08-26), p. 6158-
Kurzfassung:
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.
Materialart:
Online-Ressource
ISSN:
1422-0067
DOI:
10.3390/ijms21176158
Sprache:
Englisch
Verlag:
MDPI AG
Publikationsdatum:
2020
ZDB Id:
2019364-6
SSG:
12