Trichomonas vaginalis vast BspA-like gene family: evidence for functional diversity from structural organisation and transcriptomics

BMC Genomics

Research Article

Petrus Tang¹  Thomas Sicheritz-Ponten²  Nicia Diaz³  Pier-Luigi Fiori³  Lucie Safarikova⁴  Jan Tachezy⁴  Christophe J Noël⁵  Robert P Hirt⁵ 

[1] Bioinformatics Center/Molecular Medicine Research Center, Chang Gung University, 333, Taoyuan, Taiwan;Center for Biological Sequence Analysis, Department of Systems Biology BioCentrum-DTU, Technical University of Denmark, DK-2800, Lyngby, Denmark;Department of Biomedical Sciences, Division of Experimental and Clinical Microbiology, University of Sassari, 07100, ItalySassari, Italy;Department of Parasitology, Charles University, Vinicna 7, 128 44, Prague 2, Czech Republic;Institute for Cell and Molecular Biosciences, Newcastle University, NE2 4HH, Newcastle upon Tyne, UK;

关键词: Sexually Transmitted Infection;    Lateral Gene Transfer;    Bovine Serum Albumine;    Microbial Eukaryote;    Trophozoite Form;   

DOI  :  10.1186/1471-2164-11-99

 received in 2009-10-02, accepted in 2010-02-08,  发布年份 2010

来源: Springer

【 摘 要 】

BackgroundTrichomonas vaginalis is the most common non-viral human sexually transmitted pathogen and importantly, contributes to facilitating the spread of HIV. Yet very little is known about its surface and secreted proteins mediating interactions with, and permitting the invasion and colonisation of, the host mucosa. Initial annotations of T. vaginalis genome identified a plethora of candidate extracellular proteins.ResultsData mining of the T. vaginalis genome identified 911 BspA-like entries (TvBspA) sharing TpLRR-like leucine-rich repeats, which represent the largest gene family encoding potential extracellular proteins for the pathogen. A broad range of microorganisms encoding BspA-like proteins was identified and these are mainly known to live on mucosal surfaces, among these T. vaginalis is endowed with the largest gene family. Over 190 TvBspA proteins with inferred transmembrane domains were characterised by a considerable structural diversity between their TpLRR and other types of repetitive sequences and two subfamilies possessed distinct classic sorting signal motifs for endocytosis. One TvBspA subfamily also shared a glycine-rich protein domain with proteins from Clostridium difficile pathogenic strains and C. difficile phages. Consistent with the hypothesis that TvBspA protein structural diversity implies diverse roles, we demonstrated for several TvBspA genes differential expression at the transcript level in different growth conditions. Identified variants of repetitive segments between several TvBspA paralogues and orthologues from two clinical isolates were also consistent with TpLRR and other repetitive sequences to be functionally important. For one TvBspA protein cell surface expression and antibody responses by both female and male T. vaginalis infected patients were also demonstrated.ConclusionsThe biased mucosal habitat for microbial species encoding BspA-like proteins, the characterisation of a vast structural diversity for the TvBspA proteins, differential expression of a subset of TvBspA genes and the cellular localisation and immunological data for one TvBspA; all point to the importance of the TvBspA proteins to various aspects of T. vaginalis pathobiology at the host-pathogen interface.

【 授权许可】

Unknown   
© Noël et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.