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NAD(P) transhydrogenase has vital non-mitochondrial functions in malaria parasite transmission.
EMBO Rep 2020; :e47832ER

Abstract

Nicotinamide adenine dinucleotide (NAD) and its phosphorylated form (NADP) are vital for cell function in all organisms and form cofactors to a host of enzymes in catabolic and anabolic processes. NAD(P) transhydrogenases (NTHs) catalyse hydride ion transfer between NAD(H) and NADP(H). Membrane-bound NTH isoforms reside in the cytoplasmic membrane of bacteria, and the inner membrane of mitochondria in metazoans, where they generate NADPH. Here, we show that malaria parasites encode a single membrane-bound NTH that localises to the crystalloid, an organelle required for sporozoite transmission from mosquitos to vertebrates. We demonstrate that NTH has an essential structural role in crystalloid biogenesis, whilst its enzymatic activity is required for sporozoite development. This pinpoints an essential function in sporogony to the activity of a single crystalloid protein. Its additional presence in the apicoplast of sporozoites identifies NTH as a likely supplier of NADPH for this organelle during liver infection. Our findings reveal that Plasmodium species have co-opted NTH to a variety of non-mitochondrial organelles to provide a critical source of NADPH reducing power.

Authors+Show Affiliations

Department of Infection Biology, Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, London, UK.Department of Infection Biology, Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, London, UK.School of Biomedical Sciences, University of Plymouth, Plymouth, UK.School of Biomedical Sciences, University of Plymouth, Plymouth, UK.Department of Infection Biology, Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, London, UK.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31951090

Citation

Saeed, Sadia, et al. "NAD(P) Transhydrogenase Has Vital Non-mitochondrial Functions in Malaria Parasite Transmission." EMBO Reports, 2020, pp. e47832.
Saeed S, Tremp AZ, Sharma V, et al. NAD(P) transhydrogenase has vital non-mitochondrial functions in malaria parasite transmission. EMBO Rep. 2020.
Saeed, S., Tremp, A. Z., Sharma, V., Lasonder, E., & Dessens, J. T. (2020). NAD(P) transhydrogenase has vital non-mitochondrial functions in malaria parasite transmission. EMBO Reports, pp. e47832. doi:10.15252/embr.201947832.
Saeed S, et al. NAD(P) Transhydrogenase Has Vital Non-mitochondrial Functions in Malaria Parasite Transmission. EMBO Rep. 2020 Jan 17;e47832. PubMed PMID: 31951090.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - NAD(P) transhydrogenase has vital non-mitochondrial functions in malaria parasite transmission. AU - Saeed,Sadia, AU - Tremp,Annie Z, AU - Sharma,Vikram, AU - Lasonder,Edwin, AU - Dessens,Johannes T, Y1 - 2020/01/17/ PY - 2019/01/30/received PY - 2019/12/11/revised PY - 2019/12/17/accepted PY - 2020/1/18/entrez KW - malaria KW - oocyst KW - ookinete KW - sporozoite KW - transhydrogenase KW - transmission SP - e47832 EP - e47832 JF - EMBO reports JO - EMBO Rep. N2 - Nicotinamide adenine dinucleotide (NAD) and its phosphorylated form (NADP) are vital for cell function in all organisms and form cofactors to a host of enzymes in catabolic and anabolic processes. NAD(P) transhydrogenases (NTHs) catalyse hydride ion transfer between NAD(H) and NADP(H). Membrane-bound NTH isoforms reside in the cytoplasmic membrane of bacteria, and the inner membrane of mitochondria in metazoans, where they generate NADPH. Here, we show that malaria parasites encode a single membrane-bound NTH that localises to the crystalloid, an organelle required for sporozoite transmission from mosquitos to vertebrates. We demonstrate that NTH has an essential structural role in crystalloid biogenesis, whilst its enzymatic activity is required for sporozoite development. This pinpoints an essential function in sporogony to the activity of a single crystalloid protein. Its additional presence in the apicoplast of sporozoites identifies NTH as a likely supplier of NADPH for this organelle during liver infection. Our findings reveal that Plasmodium species have co-opted NTH to a variety of non-mitochondrial organelles to provide a critical source of NADPH reducing power. SN - 1469-3178 UR - https://www.unboundmedicine.com/medline/citation/31951090/NAD(P)_transhydrogenase_has_vital_non-mitochondrial_functions_in_malaria_parasite_transmission L2 - https://doi.org/10.15252/embr.201947832 DB - PRIME DP - Unbound Medicine ER -
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