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A growing interest in asparagine (Asn) metabolism has currently been observed in cancer and infection fields. Asparagine synthetase (AS) is responsible for the conversion of aspartate into Asn in an ATP-dependent manner, using ammonia or glutamine as a nitrogen source. There are two structurally distinct AS: the strictly ammonia dependent, type A, and the type B, which preferably uses glutamine. Absent in humans and present in trypanosomatids, AS-A was worthy of exploring as a potential drug target candidate. Appealingly, it was reported that AS-A was essential in  Leishmania donovani , making it a promising drug target. In the work herein we demonstrate that  Leishmania infantum  AS-A, similarly to  Trypanosoma  spp. and  L .  donovani , is able to use both ammonia and glutamine as nitrogen donors. Moreover, we have successfully generated  LiASA  null mutants by targeted gene replacement in  L .  infantum , and these parasites do not display any significant growth or infectivity defect. Indeed, a severe impairment of  in vitro  growth was only observed when null mutants were cultured in asparagine limiting conditions. Altogether our results demonstrate that despite being important under asparagine limitation,  Li AS-A is not essential for parasite survival, growth or infectivity in normal  in vitro  and  in vivo  conditions. Therefore we exclude AS-A as a suitable drug target against  L .  infantum  parasites.

Leishmania infantum Asparagine Synthetase A Is Dispensable for Parasites Survival and Infectivity