Molecular cloning and characterization of a cytosolic heat shock protein 70 from Naegleria fowleri

A gene encoding a cytosolic heat shock protein 70 from pathogenic Naegleria fowleri (Nf-cHSP70) was identified. The Nf-cHSP70 was 2,062 bp in length with an open reading frame of 1,980 bp encoding 659 amino acid residues. The deduced amino acid sequence of the gene shared high sequence identities wi...

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Bibliographic Details
Published in:Parasitology research (1987) 2007-04, Vol.100 (5), p.1083-1089
Main Authors: SONG, Kyoung-Ju, SONG, Kyung-Hui, NA, Byoung-Kuk, KIM, Jong-Hyun, KWON, Daeho, PARK, Sun, PAK, Jhang-Ho, IM, Kyung-Il, SHIN, Ho-Joon
Format: Article
Language:English
Subjects:
Amino Acid Motifs - genetics
Amino Acid Sequence
Animals
Biological and medical sciences
Cloning, Molecular
Conserved Sequence
Cytosol - chemistry
DNA, Protozoan - chemistry
DNA, Protozoan - genetics
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
General aspects
General aspects and techniques. Study of several systematic groups. Models
HSP70 Heat-Shock Proteins - genetics
Invertebrates
Microscopy, Fluorescence
Molecular Sequence Data
Naegleria fowleri - genetics
Open Reading Frames
Protein Structure, Tertiary - genetics
Protozoan Proteins - genetics
Reverse Transcriptase Polymerase Chain Reaction
RNA, Messenger - biosynthesis
RNA, Messenger - genetics
RNA, Protozoan - biosynthesis
RNA, Protozoan - genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Temperature
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Summary:A gene encoding a cytosolic heat shock protein 70 from pathogenic Naegleria fowleri (Nf-cHSP70) was identified. The Nf-cHSP70 was 2,062 bp in length with an open reading frame of 1,980 bp encoding 659 amino acid residues. The deduced amino acid sequence of the gene shared high sequence identities with HSP70s from other parasitic organisms and mammals. The characteristic domains, including N-terminal ATPase domain, calmodulin-binding domain, and EE(D)VD motif, found in HSP70s were also well conserved in this gene. The recombinant Nf-cHSP70 protein showed strong antigenicity against the sera from mice experimentally infected with N. fowleri. Immunofluorescence assay showed that Nf-cHSP70 localized in cytosol of the parasite. The results from semi-quantitative RT-PCR and Western blot analyses demonstrated the expression levels of gene transcripts, and its products were significantly increased at high temperature (42 degrees C). The definitive biological roles of Nf-cHSP70 are not clear, but it may protect the parasite under environmental changes especially high temperature.
ISSN:0932-0113
1432-1955
DOI:10.1007/s00436-006-0404-8