Chlamydia trachomatis has penicillin-binding proteins but not detectable muramic acid

Barbour, Alan G.; Amano, Koh; Hackstadt, Ted; Perry, Linda L.; Caldwell, Harlan D.

doi:10.1128/jb.151.1.420-428.1982

Cited by 156 publications

(75 citation statements)

References 43 publications

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“…Thus, synthesis of the cysteine-rich proteins associated with RB-EB differentiation [20][21][22], whose expression is under strict gene regulation [23], may well have been impaired [1]; these proteins have been reported absent from penicillin-induced chlamydial forms [23,24]. A possible explanation for our findings may be that under amino acid limitation chlamydial multiplication is affected by interference with the expression of genes encoding the penicillin-binding proteins [25] -enzymes known to be involved in envelope expansion and septum formation in other bacteria, and suggested to be functionally active in Chlamydia [25]. Indeed, changes in bacterial shape, peptidoglycan properties and synthesis of penicillin-binding proteins have been reported for Escherichia coli growing at reduced rate [26][27][28].…”

Section: Discussionmentioning

confidence: 99%

Low-nutrient induction of abnormal chlamydial development: A novel component of chlamydial pathogenesis?

Coles

Reynolds

Harper

et al. 1993

FEMS Microbiology Letters

105

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The intracellular development of chlamydiae in McCoy cells incubated in Eagle's minimal essential medium lacking all 13 amino acids was examined both by fluorescence and electron microscopy and by infectivity titration. Aberrant development occurred in almost all inclusions of strains of Chlamydia trachomatis and C. psittaci with the production of abnormal forms which differed in size, shape and internal structure from normal reticulate and elementary body forms. Detailed analysis of the response of C. trachomatis L2 strain 434 to graded reductions in amino acid level showed that infectivity was reduced and morphological abnormality increased as amino acid concentrations were lowered from 33 to 0% of amino acids present in minimal essential medium. Reversion of inclusions to normal and reappearance of infectious forms occurred on restoration of amino acids and further incubation. It is suggested that aberrant development may account for the presence in vivo of non-cultivable chlamydiae and that such development can arise via tryptophan deprivation mediated by local release of interferon gamma.

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Section: Discussionmentioning

confidence: 99%

Low-nutrient induction of abnormal chlamydial development: A novel component of chlamydial pathogenesis?

Coles

Reynolds

Harper

et al. 1993

FEMS Microbiology Letters

105

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“…Work from the laboratory of Caldwell demonstrated that Chlamydia possesses three Pbps (Barbour et al, 1982). The sequencing of the first chlamydial genome, C. trachomatis serovar D, identified two HMW Pbps annotated as Ct270 and Ct682 (Stephens et al, 1998).…”

Section: Bioinformatics Analysis Of the Hmw Pbps Of Chlamydiamentioning

confidence: 99%

“…The function of the HMW Pbps is to catalyse the polymerization of the PG subunits (Ghuysen and Goffin, 1999). The presence of Pbps and the sensitivity of chlamydiae to penicillin were surprising given that no peptidoglycan (PG) has yet been detected in the bacteria (Barbour et al, 1982). Moulder (1993) referred to this as the 'Chlamydial Anomaly'.…”

Section: Introductionmentioning

confidence: 99%

Chlamydia co‐opts the rod shape‐determining proteins MreB and Pbp2 for cell division

Ouellette

Karimova

Subtil

et al. 2012

Molecular Microbiology

159

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SummaryChlamydiae are obligate intracellular bacterial pathogens that have extensively reduced their genome in adapting to the intracellular environment. The chlamydial genome contains only three annotated cell division genes and lacks ftsZ. How this obligate intracellular pathogen divides is uncharacterized. Chlamydiae contain two high-molecular-weight (HMW) penicillin binding proteins (Pbp) implicated in peptidoglycan synthesis, Pbp2 and Pbp3/FtsI. We show here, using HMW Pbp-specific penicillin derivatives, that both Pbp2 and Pbp3 are essential for chlamydial cell division. Ultrastructural analyses of antibiotictreated cultures revealed distinct phenotypes: Pbp2 inhibition induced internal cell bodies within a single outer membrane whereas Pbp3 inhibition induced elongated phenotypes with little internal division. Each HMW Pbp interacts with the Chlamydia cell division protein FtsK. Chlamydiae are coccoid yet contain MreB, a rod shape-determining protein linked to Pbp2 in bacilli. Using MreB-specific antibiotics, we show that MreB is essential for chlamydial growth and division. Importantly, co-treatment with MreB-specific and Pbp-specific antibiotics resulted in the MreB-inhibited phenotype, placing MreB upstream of Pbp function in chlamydial cell division. Finally, we showed that MreB also interacts with FtsK. We propose that, in Chlamydia, MreB acts as a central co-ordinator at the division site to substitute for the lack of FtsZ in this bacterium.

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“…The disulfide bonds form an extensive intermolecular network that increases the structural rigidity of the outer membrane. [22][23][24] The intermolecular network at the outer membrane is called chlamydial outer membrane complex (COMC) and is thought to substitute for the very limited amount of chlamydial cell wall peptidoglycan, a component that provides rigidity and structural strength against osmotic pressure to the wall of Gram-negative bacteria. 22 The major constituents of COMC are MOMP and two cysteine rich proteins OmcA and OmcB.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation

et al. 2018

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Chlamydial major outer membrane protein (MOMP) is the major protein constituent of the bacterial pathogen Chlamydia trachomatis. Chlamydia trachomatis Serovars D–K are the leading cause of genital tract infections which can lead to infertility or ectopic pregnancies. A vaccine against Chlamydia is highly desirable but currently not available. MOMP accounts for ~ 60% of the chlamydial protein mass and is considered to be one of the lead vaccine candidates against C. trachomatis. We report on the spectroscopic analysis of C. trachomatis native MOMP Serovars D, E, F, and J as well as C. muridarum MOMP by size exclusion chromatography multi angle light scattering (SEC MALS), circular dichroism (CD) and attenuated total reflectance Fourier transform infrared spectroscopy (ATR‐FTIR). MOMP was purified from the native bacterium grown in either adherent HeLa cells or in different suspension cell lines. Our results confirm that MOMP forms homo‐trimers in detergent micelles. The secondary structure composition of C. trachomatis MOMP was conserved across serovars, but different from composition of C. muridarum MOMP with a 13% (CD) to 18% (ATR‐FTIR) reduction in β‐sheet conformation for C. trachomatis MOMP. When Serovar E MOMP was isolated from suspension cell lines the α‐helix content increased by 7% (CD) to 13% (ATIR‐FTIR). Maintenance of a native‐like tertiary and quaternary structure in subunit vaccines is important for the generation of protective antibodies. This biophysical characterization of MOMP presented here serves, in the absence of functional assays, as a method for monitoring the structural integrity of MOMP.

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Chlamydia trachomatis has penicillin-binding proteins but not detectable muramic acid

Cited by 156 publications

References 43 publications

Low-nutrient induction of abnormal chlamydial development: A novel component of chlamydial pathogenesis?

Low-nutrient induction of abnormal chlamydial development: A novel component of chlamydial pathogenesis?

Chlamydia co‐opts the rod shape‐determining proteins MreB and Pbp2 for cell division

Spectroscopic analysis of chlamydial major outer membrane protein in support of structure elucidation

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