Identification and characterization of a surface-associated, subtilisin-like serine protease in Trichomonas vaginalis

Trichomonas vaginalis is a protozoan parasite causing trichomonosis, a sexually transmitted infection in humans. This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and character...

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Veröffentlicht in:Parasitology 2010-09, Vol.137 (11), p.1621-1635
Hauptverfasser: HERNÁNDEZ-ROMANO, PABLO, HERNÁNDEZ, ROBERTO, ARROYO, ROSSANA, ALDERETE, JOHN F., LÓPEZ-VILLASEÑOR, IMELDA
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container_issue 11
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container_title Parasitology
container_volume 137
creator HERNÁNDEZ-ROMANO, PABLO
HERNÁNDEZ, ROBERTO
ARROYO, ROSSANA
ALDERETE, JOHN F.
LÓPEZ-VILLASEÑOR, IMELDA
description Trichomonas vaginalis is a protozoan parasite causing trichomonosis, a sexually transmitted infection in humans. This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and characterize a putative subtilisin-like serine protease (SUB1). The sub1 gene encodes a 101-kDa protein. In silico analyses predict signal and pro-peptides at the N-terminus, and a transmembrane helix at the carboxy-terminal region. The sub1 gene was found as single copy by Southern analysis, albeit additional serine protease related genes are annotated in the T. vaginalis genome. The expression of sub1 could only be detected by RT-PCR and Ribonuclease Protection Assays, suggesting a low abundant mRNA. The sub1 gene transcription start site was correctly assigned by RPA. The transcript abundance was found to be modulated by the availability of iron in the growth medium. Antibodies raised to a specific SUB1 peptide recognized a single protein band (~82 kDa) in Western blots, possibly representing the mature form of the protein. Immunofluorescence showed SUB1 on the trichomonad surface, and in dispersed vesicles throughout the cytoplasm. A bioinformatic analysis of genes annotated as serine proteases in the T. vaginalis genome is also presented. To our knowledge this is the first putative serine protease experimentally described for T. vaginalis.
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This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and characterize a putative subtilisin-like serine protease (SUB1). The sub1 gene encodes a 101-kDa protein. In silico analyses predict signal and pro-peptides at the N-terminus, and a transmembrane helix at the carboxy-terminal region. The sub1 gene was found as single copy by Southern analysis, albeit additional serine protease related genes are annotated in the T. vaginalis genome. The expression of sub1 could only be detected by RT-PCR and Ribonuclease Protection Assays, suggesting a low abundant mRNA. The sub1 gene transcription start site was correctly assigned by RPA. The transcript abundance was found to be modulated by the availability of iron in the growth medium. 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This parasite has numerous proteases, most of which are cysteine proteases that appear to be involved in adherence and cytotoxicity of host cells. In this report we identify and characterize a putative subtilisin-like serine protease (SUB1). The sub1 gene encodes a 101-kDa protein. In silico analyses predict signal and pro-peptides at the N-terminus, and a transmembrane helix at the carboxy-terminal region. The sub1 gene was found as single copy by Southern analysis, albeit additional serine protease related genes are annotated in the T. vaginalis genome. The expression of sub1 could only be detected by RT-PCR and Ribonuclease Protection Assays, suggesting a low abundant mRNA. The sub1 gene transcription start site was correctly assigned by RPA. The transcript abundance was found to be modulated by the availability of iron in the growth medium. Antibodies raised to a specific SUB1 peptide recognized a single protein band (~82 kDa) in Western blots, possibly representing the mature form of the protein. Immunofluorescence showed SUB1 on the trichomonad surface, and in dispersed vesicles throughout the cytoplasm. A bioinformatic analysis of genes annotated as serine proteases in the T. vaginalis genome is also presented. To our knowledge this is the first putative serine protease experimentally described for T. vaginalis.</abstract><cop>Cambridge, UK</cop><pub>Cambridge University Press</pub><pmid>20602853</pmid><doi>10.1017/S003118201000051X</doi><tpages>15</tpages></addata></record>
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subjects Amino Acid Sequence
Animals
Antigens, Protozoan - chemistry
Antigens, Protozoan - genetics
Antigens, Protozoan - immunology
Antigens, Protozoan - metabolism
Base Sequence
Biological and medical sciences
cellular localization
Cytotoxicity
Female
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
General aspects
General aspects and techniques. Study of several systematic groups. Models
Humans
Invertebrates
Iron - metabolism
Mice
Models, Molecular
Molecular Sequence Data
Parasites
Peptides
Protozoan Proteins - chemistry
Protozoan Proteins - genetics
Protozoan Proteins - immunology
Protozoan Proteins - metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sequence Analysis, DNA
serine protease
Serine Proteases - chemistry
Serine Proteases - genetics
Serine Proteases - immunology
Serine Proteases - metabolism
Sexually transmitted diseases
STD
subtilisin
Subtilisin - chemistry
Subtilisin - genetics
Subtilisin - immunology
Subtilisin - metabolism
surface protein
Trichomonas vaginalis
Trichomonas vaginalis - enzymology
Trichomonas vaginalis - genetics
Trichomonas vaginalis - metabolism
title Identification and characterization of a surface-associated, subtilisin-like serine protease in Trichomonas vaginalis
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