Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA

Shirai, Mutsunori; Hirakawa, Hideki; Kimoto, Mitsuaki; Tabuchi, Mitsuaki; Kishi, Fumio; Ouchi, Kazunobu; Shiba, Tadayoshi; Ishii, Kazuo; Hattori, Masahira; Kuhara, Satoru; Nakazawa, Takahiro

doi:10.1093/nar/28.12.2311

Cited by 168 publications

(109 citation statements)

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“…HEp-2 cells (ATCC CCL-23) were used as host cells for infection by C. pneumoniae J138, isolated in Japan in 1994 (Shirai et al, 2000). C. pneumoniae J138 EBs were purified by sucrose-gradient centrifugation and stored at 280 uC in SPG buffer (pH 7.2), which consists of 250 mM sucrose, 10 mM sodium phosphate and 5 mM glutamate.…”

Section: Methodsmentioning

confidence: 99%

“…Recently a small regulatory RNA gene was identified as a suppressor of the lethal phenotype of hctA overexpression in Escherichia coli and it was shown to negatively regulate Hc1 synthesis at an early stage of infection (Grieshaber et al, 2006 HEp-2 cells (ATCC CCL-23) were used as host cells for infection by C. pneumoniae J138, isolated in Japan in 1994 (Shirai et al, 2000). C. pneumoniae J138 EBs were purified by sucrose-gradient centrifugation and stored at 280 uC in SPG buffer (pH 7.2), which consists of 250 mM sucrose, 10 mM sodium phosphate and 5 mM glutamate.…”

Section: Introductionmentioning

confidence: 99%

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Chlamydial SET domain protein functions as a histone methyltransferase

et al. 2007

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SET domain genes have been identified in numbers of bacterial genomes based on similarity to SET domains of eukaryotic histone methyltransferases. Herein, a Chlamydophila pneumoniae SET domain gene was clarified to be coincidently expressed with hctA and hctB genes encoding chlamydial histone H1-like proteins, Hc1 and Hc2, respectively. The SET domain protein (cpnSET) is localized in chlamydial cells and interacts with Hc1 and Hc2 through the C-terminal SET domain. As expected from conservation of catalytic sites in cpnSET, it functions as a protein methyltransferase to murine histone H3 and Hc1. However, little is known about protein methylation in the molecular pathogenesis of chlamydial infection. cpnSET may play an important role in chlamydial cell maturation due to modification of chlamydial histone H1-like proteins. INTRODUCTIONChlamydophila pneumoniae is an obligatory intracellular eubacterium that causes acute respiratory diseases and may be involved in chronic inflammatory processes, such as atherosclerosis (Rosenfeld et al., 2000), asthma (Hahn et al., 1991) and Alzheimer's disease (Itzhaki et al., 2004). Persistence of chlamydial infection has been thought to be important for chronic diseases and has been characterized using model animals and activation stimuli such as cytokines and antibiotics (Beatty et al., 1993;Belland et al., 2003;Malinverni et al., 1995;Mehta et al., 1998). However, molecular-level relationships between chronic disease progression and persistent infection are not yet clear.Chlamydiae exhibit a unique life cycle in which they alternate morphologies between elementary bodies (EBs) and reticulate bodies (RBs). EBs are transcriptionally inactive electron-dense particles that are internalized into host cells by inducing phagocytosis. EB differentiation into RBs occurs with the development of phagosomes into inclusions. Transcriptionally active RBs multiply by binary fission with nutrients acquired from the host cell. At the end of the developmental cycle, RBs are converted into EBs and released from host cells for the next infection. Besides the developmental cycle, during persistent infection caused by exposure to interferon gamma (IFN-c) or antibiotics, RBs differentiate into aberrantly large and non-multiplying RBs (Belland et al., 2003). However, little is known about the switching mechanism whereby vegetative RBs convert into infectious EBs or aberrant RBs. Understanding this molecular system should be helpful for the prevention of persistent chlamydial infection.Two eukaryotic histone H1-like proteins of chlamydiae, Hc1 and Hc2, are present mainly in EBs, where those proteins bind DNA and promote genomic DNA condensation (Barry et al., 1992;Hackstadt et al., 1991;Perara et al., 1992;Tao et al., 1991). Recently a small regulatory RNA gene was identified as a suppressor of the lethal phenotype of hctA overexpression in Escherichia coli and it was shown to negatively regulate Hc1 synthesis at an early stage of infection (Grieshaber et al., 2006 HEp-2 cells (ATCC CCL-23) were used ...

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Chlamydial SET domain protein functions as a histone methyltransferase

et al. 2007

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“…Although, complete chromosomal sequences are available for several chlamydial species, which is a significant advance, [4,[11][12][13][14]; the elucidation of gene-structure function relationships has been slow, due to the absence of genetic methods, such as gene transfer and mutant isolation [15]. Thus studies of chlamydial bacteriophages are of great interest as these agents offer a potential natural means of transferring DNA between cells.…”

Section: Introductionmentioning

confidence: 99%

Isolation, Molecular Characterisation and Genome Sequence of a Bacteriophage (Chp3) from Chlamydophila pecorum

et al. 2004

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Abstract. Chlamydiae are obligate intracellular pathogens that have a unique developmental cycle. Thirty nine viable isolates representing all nine currently recognised chlamydial species were screened by immunofluorescence with a cross-reacting chlamydiaphage monoclonal antibody. A novel chlamydiaphage (Chp3) was detected in C. pecorum, a chlamydial species not previously known to carry bacteriophages. Chp3 belongs to the Microviridae, members of this virus family are characterised by circular, single-stranded DNA genomes and small T ¼ 1 icosahedral capsids. Double-stranded replicative form Chp3 DNA was purified from elementary bodies and used as a template to determine the complete genome sequence. The genome of Chp3 is 4,554 base pairs and encodes eight open reading frames organised in the same genome structure as other chlamydiaphages. An unrooted phylogenetic tree was constructed based on the major coat proteins of 11 members of the Microviridae and Chp3. This showed that the Microviridae are clearly divided into two discrete sub-families; those that infect the Enterobacteriaceae e.g. ØX174 and the bacteriophages that infect obligate intracellular bacteria or mollicutes including SpV4 (Spiroplasma melliferum), ØMH2K (Bdellovibrio bacteriovorus) and the chlamydiaphages. Comparative analyses demonstrate that the chlamydiaphages can be further subdivided into two groupings, one represented by Chp2/Chp3 and the other by ØCPG1/ØCPAR39.

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“…They have small genomes (Ϸ1 Mb) and therefore are easily sequenced. At least six complete genome sequences are available for three of the chlamydial species (7)(8)(9), and more sequences are planned and are being produced by a variety of interested research groups. Annotation, analysis, and comparison of chlamydial genomes have provided a few surprises (e.g., they have the genes required for production of peptidoglycan, but no peptidoglycan is present in the fully infectious form of the organism) and some important insights into possible pathogenic mechanisms (10).…”

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confidence: 99%

Chlamydiauncloaked

Byrne

2003

Proc. Natl. Acad. Sci. U.S.A.

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Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA

Cited by 168 publications

References 13 publications

Chlamydial SET domain protein functions as a histone methyltransferase

Chlamydial SET domain protein functions as a histone methyltransferase

Isolation, Molecular Characterisation and Genome Sequence of a Bacteriophage (Chp3) from Chlamydophila pecorum

Chlamydiauncloaked

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