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- Title
Identification of a perchloric acid-soluble protein (PSP)-like ribonuclease from Trichomonas vaginalis.
- Authors
Villalobos-Osnaya, Alma; Garza-Ramos, Georgina; Serratos, Iris N.; Millán-Pacheco, César; González-Robles, Arturo; Arroyo, Rossana; Quintas-Granados, Laura Itzel; Alvarez-Sanchez, María Elizbeth
- Abstract
A perchloric acid-soluble protein (PSP), named here tv-psp1, was identified in Trichomonas vaginalis. It is expressed under normal culture conditions according to expressed sequence tag (EST) analysis. On the other hand, Tv-PSP1 protein was identified by mass spectrometry with a 40% of identity to human PSP (p14.1). Polyclonal antibodies against recombinant Tv-PSP1 (rTv-PSP1) recognized a single band at 13.5 kDa in total protein parasite extract by SDS-PAGE and a high molecular weight band analyzed by native PAGE. Structural analysis of Tv-PSP1, using dynamic light scattering, size exclusion chromatography, and circular dichroism spectroscopy, showed a trimeric structure stable at 7 M urea with 38% α-helix and 14% β-sheet in solution and a molecular weight of 40.5 kD. Tv-PSP1 models were used to perform dynamic simulations over 100 ns suggesting a stable homotrimeric structure. Tv-PSP1 was located in the nucleus, cytoplasm, and hydrogenosomes of T. vaginalis, and the in silico analysis by Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) showed interactions with RNA binding proteins. The preliminary results of RNA degradation analysis with the recombinant Tv-PSP1 showed RNA partial deterioration suggesting a possible putative ribonuclease function.
- Subjects
PERCHLORIC acid; RIBONUCLEASE genetics; TRICHOMONAS vaginalis; EXPRESSED sequence tag (Genetics); MASS spectrometry; CIRCULAR dichroism; HYDROGENOSOMES
- Publication
Parasitology Research, 2018, Vol 117, Issue 11, p3639
- ISSN
0932-0113
- Publication type
Article
- DOI
10.1007/s00436-018-6065-6