Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 20, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1074/mcp.RA120.002375
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Funding
- National Natural Science Foundation of China [82030060, 81772219]
- Distinguished Scientist grant from Shenyang Agricultural University and Liaoning Province [8804-880416076]
- CAMS Innovation Fund for Medical Sciences (CIFMS) [2019-I2M-5-042]
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Extensive and dynamic posttranslational modifications of proteins in Plasmodium falciparum and infected red blood cells play a crucial role in understanding parasite biology and malaria pathogenesis.
These modifications critically modulate virulence factors, host-parasite interaction, and disease mechanisms in malaria.
Furthermore, the study provides a valuable resource for mining new antimalarial targets.
Malaria elimination is still pending on the development of novel tools that rely on a deep understanding of parasite biology. Proteins of all living cells undergo myriad posttranslational modifications (PTMs) that are critical to multifarious life processes. An extensive proteome-wide dissection revealed a fine PTM map of most proteins in both Plasmodium falciparum, the causative agent of severe malaria, and the infected red blood cells. More than two-thirds of proteins of the parasite and its host cell underwent extensive and dynamic modification throughout the erythrocytic developmental stage. PTMs critically modulate the virulence factors involved in the host-parasite interaction and pathogenesis. Furthermore, P. falciparum stabilized the supporting proteins of erythrocyte origin by selective demodification. Collectively, our multiple omic analyses, apart from having furthered a deep understanding of the systems biology of P. falciparum and malaria pathogenesis, provide a valuable resource for mining new antimalarial targets.
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