Identification of a perchloric acid-soluble protein (PSP)-like ribonuclease from Trichomonas vaginalis

被引：1

作者：

Villalobos-Osnaya, Alma ^{[1
]}

Garza-Ramos, Georgina ^{[2
]}

Serratos, Iris N. ^{[3
]}

Millan-Pacheco, Cesar ^{[4
]}

Gonzalez-Robles, Arturo ^{[5
]}

Arroyo, Rossana ^{[5
]}

Itzel Quintas-Granados, Laura ^{[6
]}

Elizbeth Alvarez-Sanchez, Maria ^{[1
]}

机构：

[1] UACM, Posgrado Ciencias Genom, San Lorenzo 290, Mexico City 03100, DF, Mexico

[2] Univ Nacl Autonoma Mexico, Fac Med, Dept Bioquim, Univ 3000, Mexico City 04510, DF, Mexico

[3] Univ Autonoma Metropolitana, Dept Quim, Apartado Postal 55-534, Mexico City 09340, DF, Mexico

[4] Univ Autonoma Estado Morelos, Fac Farm, Cuernavaca 62209, Morelos, Mexico

[5] Ctr Invest & Estudios Avanzados, CINVESTAV, IPN, Dept Infect & Patogenesis Mol, Av IPN 2508, Mexico City 07360, DF, Mexico

[6] Univ Mexiquense Bicentenario, Unidad Estudios Super Tultitlan, Av Ex Hacienda Portales S-N, Tultitlan 54910, Estado De Mexic, Mexico

来源：

PARASITOLOGY RESEARCH | 2018年 / 117卷 / 11期

关键词：

Trichomonas vaginalis; Perchloric acid-soluble proteins; Molecular dynamic; Cellular localization; Homotrimeric structure; Size exclusion chromatographic; CALPAIN ACTIVATOR PROTEIN; CRYSTAL-STRUCTURE; CIRCULAR-DICHROISM; FAMILY PROTEIN; MEMBER; UK114; YJGF; MAINTENANCE; INTERFACE; BINDING;

D O I：

10.1007/s00436-018-6065-6

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

A perchloric acid-soluble protein (PSP), named here dv-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% alpha-helix and 14% beta-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.

引用

页码：3639 / 3652

页数：14

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