Korean J Parasitol.  2017 Apr;55(2):121-128. 10.3347/kjp.2017.55.2.121.

Differential Protein Expressions in Virus-Infected and Uninfected Trichomonas vaginalis

• He D
• Pengtao G
• Ju Y
• Jianhua L
• He L
• Guocai Z
• Xichen Z

• KMID: 2379413
• DOI: http://doi.org/10.3347/kjp.2017.55.2.121

Abstract

Protozoan viruses may influence the function and pathogenicity of the protozoa. Trichomonas vaginalis is a parasitic protozoan that could contain a double stranded RNA (dsRNA) virus, T. vaginalis virus (TVV). However, there are few reports on the properties of the virus. To further determine variations in protein expression of T. vaginalis, we detected 2 strains of T. vaginalis; the virus-infected (V⁺) and uninfected (V⁻) isolates to examine differentially expressed proteins upon TVV infection. Using a stable isotope N-terminal labeling strategy (iTRAQ) on soluble fractions to analyze proteomes, we identified 293 proteins, of which 50 were altered in V⁺ compared with V⁻ isolates. The results showed that the expression of 29 proteins was increased, and 21 proteins decreased in V⁺ isolates. These differentially expressed proteins can be classified into 4 categories: ribosomal proteins, metabolic enzymes, heat shock proteins, and putative uncharacterized proteins. Quantitative PCR was used to detect 4 metabolic processes proteins: glycogen phosphorylase, malate dehydrogenase, triosephosphate isomerase, and glucose-6-phosphate isomerase, which were differentially expressed in V⁺ and V⁻ isolates. Our findings suggest that mRNA levels of these genes were consistent with protein expression levels. This study was the first which analyzed protein expression variations upon TVV infection. These observations will provide a basis for future studies concerning the possible roles of these proteins in host-parasite interactions.

Keyword

Trichomonas vaginalis; Trichomonas vaginalis virus; iTRAQ; quantitative PCR; protein expression

MeSH Terms

Glucose-6-Phosphate Isomerase
Glycogen Phosphorylase
Heat-Shock Proteins
Host-Parasite Interactions
Malate Dehydrogenase
Metabolism
Polymerase Chain Reaction
Proteome
Reticuloendotheliosis virus
Ribosomal Proteins
RNA, Double-Stranded
RNA, Messenger
Trichomonas vaginalis*
Trichomonas*
Triose-Phosphate Isomerase
Virulence
Glucose-6-Phosphate Isomerase
Glycogen Phosphorylase
Heat-Shock Proteins
Malate Dehydrogenase
Proteome
RNA, Double-Stranded
RNA, Messenger
Ribosomal Proteins
Triose-Phosphate Isomerase