The nucleotide and derived amino acid sequence of the<i>omp</i>2 gene of<i>Chlamydia trachomatis</i>serovar E

Coles, Anthony M.; Allan, I.; Pearce, J. H.

doi:10.1093/nar/18.22.6713

Cited by 11 publications

(5 citation statements)

References 5 publications

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“…3 (1, 2, 12 54% overall amino acid identity. Although the overall conservation of sequence is modest, all 13 cysteine residues in the small CRP of the C. trachomatis strains are located at identical positions in the C. psittaci protein, suggesting an important functional or structural role for these residues. Other features in common include a 16-amino-acid segment of identity within the N-terminal half of the protein, a potential lipid modification-signal peptidase II site (50), and charged amino acids located throughout the length of the protein.…”

Section: Resultsmentioning

confidence: 98%

Sequence analysis and lipid modification of the cysteine-rich envelope proteins of Chlamydia psittaci 6BC

Everett

Hatch

1991

J Bacteriol

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The envelopes of elementary bodies of Chiamydia spp. consist largely of disulfide-cross-linked major outer membrane protein (MOMP) and two cysteine-rich proteins (CRPs). The MOMP gene of Chlamydia psittaci 6BC has been sequenced previously, and the genes encoding the small and large CRPs from this strain were cloned and sequenced in this study. The CRP genes were found to be tandemly arranged on the chlamydial chromosome but could be independently expressed in Escherichia coli. The deduced 87-amino-acid sequence of the small-CRP gene (envA) contains 15 cysteine residues, a potential signal peptide, and a potential signal peptidase II-lipid modification site. Hydropathy plot and conformation analysis of the small-CRP amino acid sequence indicated that the protein was unlikely to be associated with a membrane. However, the small CRP was specifically labeled in host cells incubated with [3H]palmitic acid and may therefore be associated with a membrane through a covalently attached lipid portion of the molecule. The deduced 557-amino-acid sequence of the large-CRP gene (envB) contains 37 cysteine residues and a single putative signal peptidase I cleavage site. In one recombinant done the large CRP appeared to be posttranslationally cleaved at two sites, forming a doublet in a manner similar to the large-CRP doublet made in native C. psittaci 6BC. Comparison of the deduced amino acid sequences of the CRPs from chlamydial strains indicated that the small CRP is moderately conserved, with 54% identity between C. psiutaci 6BC and Chiamydia trachomatis, and the large CRP is highly conserved, with 71% identity between C. psittaci and C. trachomatis and 85% identity between C. psittaci 6BC and Chlamydia pneumoniae. The positions of the cysteine residues in both CRPs are highly conserved in Chlamydia spp. From the number of cysteine residues in the MOMP and the CRPs and the relative incorporation of [35S]cysteine into these proteins, it was calculated that the molar ratio of C. psittaci 6BC elementary body envelope proteins is about one large-CRP molecule to two small-CRP molecules to five MOMP molecules.

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Section: Resultsmentioning

confidence: 98%

Sequence analysis and lipid modification of the cysteine-rich envelope proteins of Chlamydia psittaci 6BC

Everett

Hatch

1991

J Bacteriol

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“…This gene is expressed late in the chlamydial life cycle [9], and its presence in RNA preparations from infected monocytes in culture suggests that the infecting bacteria reach that late stage, even though they do not complete the cycle to produce new EB. In as yet unpublished studies, we have shown that synovial chlamydial also express omp2, thus confirming another congruence between the in vivo and in vitro systems under study.…”

Section: Discussionmentioning

confidence: 99%

“…RT-PCR assays used 1 µg RNA/reaction. Primer sets targeted the chlamydial genes specifying the 16 S rRNA [10,11], r-proteins S5 and L5 [14], glycyl-tRNA synthetase (glyQS; [28]), KDO transferase (gseA; [19], 57-kDa heat shock protein (hsp60; [7]), cysteine-rich outer membrane protein (omp2; [9]) and major outer membrane protein (MOMP; omp1; [27]). Primer sequences used in all assays are given in Table 1 (see also [11,12]).…”

Section: Rna Preparation and Analysismentioning

confidence: 99%

Viability and gene expression in Chlamydia trachomatis during persistent infection of cultured human monocytes

Gérard

Köhler²,

Branigan

et al. 1998

Medical Microbiology and Immunology

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The principal host cell for persistently infecting synovial Chlamydia trachomatis is the macrophage. During infection of human monocytes/macrophages in culture this bacterium displays aberrant morphology and produces no new elementary bodies, reflecting the situation in synovium. Here we investigate the metabolic status of C. trachomatis (serovar K) during an extended infection of human peripheral monocytes in vitro. Using reverse transcription-polymerase chain reaction assays, we have shown that primary transcripts from the chlamydial rRNA operons are present throughout a 10-day course of infection. Other assays targeting mRNAs from chlamydial genes encoding r-proteins S5 and L5, the glycyl-tRNA synthetase, the 60-kDa cysteine-rich outer membrane protein, and the KDO transferase indicate that these messengers are also present throughout the entire 10-day period. The gene encoding the 57-kDa heat-shock protein (hsp60) is expressed by the bacterium throughout the 10-day infection of cultured monocytes, but transcript levels from the gene encoding the major outer membrane protein (omp1) appear to be attenuated. Western analyses targeting these latter proteins confirm the presence of the hsp60 gene product, and the virtual absence of major outer membrane protein, in chlamydia-infected cultured human monocytes. Thus, during extended infection of human monocytes in vitro, chlamydia are non-productive but transcriptionally active; the pattern of transcriptional activity reflects that known for persistent C. trachomatis infection in vivo in synovial tissue.

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“…OmcB (CT443) is a 553-aa residue protein also referred to as the 60-kDa cysteine-rich outer membrane protein. This protein is highly conserved among the C. trachomatis serovars (19,(32)(33)(34)(35), sharing between 98 and 99% aa sequence identity. OmcB from C. trachomatis shares ϳ71% aa sequence identity with its homologue in C. pneumoniae (36).…”

Section: Identification Of a Chlamydia-specific Cd8 ϩ T Cell Agmentioning

confidence: 99%

Human CD8+ T Cells Recognize the 60-kDa Cysteine-Rich Outer Membrane Protein fromChlamydia trachomatis

Gervassi

Grabstein

Probst

et al. 2004

The Journal of Immunology

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The intracellular bacterial pathogen Chlamydia is sequestered from the host cell cytoplasm by remaining within an inclusion body during its replication cycle. Nevertheless, CD8+ T cells recognizing Chlamydia Ags in the context of MHC class I molecules are primed during infection. We have recently described derivation of Chlamydia-specific human CD8+ T cells by using infected dendritic cells as a surrogate system to reflect Chlamydia-specific CD8+ T cell responses in vivo. These CD8+ T cell clones recognize chlamydial Ags processed via the conventional class Ia processing pathway, as assessed by treatment of infected APC with lactacystin and brefeldin A, suggesting that the Ags are translocated from the chlamydial inclusion into the host cell cytosol. In this study, outer membrane protein 2 (OmcB) was identified as the Ag recognized by one of these Chlamydia-specific human CD8+ T cells, and we defined the HLA*A0101-restricted epitope from this Ag. CD8+ T cell responses to this epitope were present at high frequencies in the peripheral blood of both of two HLA*A0101 donors tested. In vitro chlamydial growth was completely inhibited by the OmcB-specific CD8+ T cell clone independently of lytic mechanisms. OmcB is a 60-kDa protein that has been postulated to be associated with the Chlamydia outer membrane complex. The subcellular localization of OmcB to the cytosol of infected cells, as determined by conventional MHC class I Ag processing and presentation, suggests the possibility of an additional, cytosolic-associated function for this protein.

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The nucleotide and derived amino acid sequence of theomp2 gene ofChlamydia trachomatisserovar E

Cited by 11 publications

References 5 publications

Sequence analysis and lipid modification of the cysteine-rich envelope proteins of Chlamydia psittaci 6BC

Sequence analysis and lipid modification of the cysteine-rich envelope proteins of Chlamydia psittaci 6BC

Viability and gene expression in Chlamydia trachomatis during persistent infection of cultured human monocytes

Human CD8+ T Cells Recognize the 60-kDa Cysteine-Rich Outer Membrane Protein fromChlamydia trachomatis

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