کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5741080 | 1616986 | 2017 | 6 صفحه PDF | دانلود رایگان |
- 3â²nucleotidase/nuclease (3â²NT/NU) is a member of the class I nuclease family.
- 3â²NT/NU hydrolyzes both 3â²-monophosphorylated nucleotides and nucleic acids.
- 3â²NT/NU is involved in purine salvage pathway of protozoan parasites.
- 3â²nucleotidase activity increases the association index of parasites and macrophages.
- 3â²NT/NU plays a role in parasite escape from neutrophil extracellular traps.
3â²-nucleotidase/nuclease (3â²NT/NU) is a bi-functional enzyme that is able to hydrolyze 3â²-monophosphorylated nucleotides and nucleic acids. This review summarizes the major molecular and biochemical properties of this enzyme in different trypanosomatid species. Sequence analysis of the gene encoding 3â²NT/NU in Leishmania and Crithidia species showed that the protein possesses five highly conserved regions that are characteristic of members of the class I nuclease family. 3â²NT/NU presents a molecular weight of approximately 40Â kDa, which is conserved among the studied species. Throughout the review, we discuss inhibitors and substrate specificity, relating them to the putative structure of the enzyme. Finally, we present the major biological roles performed by 3â²NT/NU. The involvement of 3â²NT/NU in the purine salvage pathway was confirmed by the increase of activity and expression of the enzyme when the parasites were submitted to purine starvation. The generation of extracellular adenosine is also important to the modulation of the host immune response. Interaction assays involving Leishmania parasites and macrophages indicated that 3â²-nucleotidase activity increases the association index between them. Recently, it was shown that 3â²NT/NU plays a role in parasite escape from neutrophil extracellular traps, one of the first mechanisms of the host immune system for preventing infection.
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Journal: Experimental Parasitology - Volume 179, August 2017, Pages 1-6