Optimal development of Chlamydophila psittaci in L929 fibroblast and BGM epithelial cells requires the participation of microfilaments and microtubule-motor proteins

Escalante-Ochoa, Cristina; Ducatelle, Richard; Haesebrouck, Freddy

doi:10.1006/mpat.2000.0352

Cited by 11 publications

(6 citation statements)

References 57 publications

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“…This is in agreement with studies that have previously localized dynein to the developing inclusions and shown that Na3VO4, a general inhibitor of tyrosine phosphatases that inhibits dynein, detrimentally affects chlamydial development when cells are treated concurrently with infection (Clausen et al, 1997). In addition, optimal growth of C. psittaci appears to be dependent upon a functional microtubule network (Escalante-Ochoa et al, 2000). Although chlamydial migration requires dynein and appears to have many similarities to host endocytic trafficking, it differs significantly in that an intact dynactin complex is apparently not necessary.…”

Section: Discussionsupporting

confidence: 79%

Chlamydia trachomatis uses host cell dynein to traffic to the microtubule-organizing center in a p50 dynamitin-independent process

Grieshaber¹,

Grieshaber²,

Hackstadt³

2003

Journal of Cell Science

171

183

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Chlamydiae are pathogenic obligate intracellular bacteria with a biphasic developmental cycle that involves cell types adapted for extracellular survival (elementary bodies, EBs) and intracellular multiplication (reticulate bodies, RBs). The intracellular development of chlamydiae occurs entirely within a membrane-bound vacuole termed an inclusion. Within 2 hours after entry into host cells, Chlamydia trachomatis EBs are trafficked to the perinuclear region of the host cell and remain in close proximity to the Golgi apparatus, where they begin to fuse with a subset of host vesicles containing sphingomyelin. Here, we provide evidence that chlamydial migration from the cell periphery to the peri-Golgi region resembles host cell vesicular trafficking. Chlamydiae move towards the minus end of microtubules and aggregate at the microtubule-organizing center (MTOC). In mammalian cells the most important minus-end-directed microtubule motor is cytoplasmic dynein. Microinjection of antibodies to a subunit of cytoplasmic dynein inhibited movement of chlamydiae to the MTOC, whereas microinjection of antibodies to the plus-directed microtubule motor, kinesin, had no effect. Surprisingly, overexpression of the protein p50 dynamitin, a subunit of the dynactin complex that links vesicular cargo to the dynein motor in minus directed vesicle trafficking, did not abrogate chlamydial migration even though host vesicle transport was inhibited. Nascent chlamydial inclusions did, however, colocalize with the p150(Glued) dynactin subunit, which suggests that p150(Glued) may be required for dynein activation or processivity but that the cargo-binding activity of dynactin, supplied by p50 dynamitin subunits and possibly other subunits, is not. Because chlamydial transcription and translation were required for this intracellular trafficking, chlamydial proteins modifying the cytoplasmic face of the inclusion membrane are probable candidates for proteins fulfilling this function.

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Section: Discussionsupporting

confidence: 79%

Chlamydia trachomatis uses host cell dynein to traffic to the microtubule-organizing center in a p50 dynamitin-independent process

Grieshaber¹,

Grieshaber²,

Hackstadt³

2003

Journal of Cell Science

171

183

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“…29,30 Interestingly, the closely related bacterium Chlamydia psittaci requires an intact microtubular network for optimal growth. 54 Recently, a unique role for the cytoskeleton during the replicative stage of the chlamydial developmental cycle was demonstrated. 55 Chlamydia was found to remodel host actin and intermediate filaments to form scaffolding surrounding the inclusion that is necessary to maintain inclusion integrity and morphology.…”

Section: Methodsmentioning

confidence: 99%

Autophagy-independent function of MAP-LC3 during intracellular propagation ofChlamydia trachomatis

Al-Younes¹,

Al‐Zeer²,

Khalil³

et al. 2011

Autophagy

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Microtubule-associated protein 1 (MAP1) light chain 3 (LC3) has proven useful as autophagosomal marker in studies on the interaction between pathogens and the host autophagic machinery. However, the function of LC3 is known to extend above and beyond its role in autophagosome formation. We previously reported that intrinsic LC3 is associated with the intracellular Chlamydia trachomatis inclusion in human epithelial cells. Here we show that LC3, most likely the cytoplasmic nonlipidated form, interacts with the C. trachomatis inclusion as a microtubule-associated protein rather than an autophagosome-associated component. In contrast, N-terminally GFP-tagged LC3 exclusively targets autophagosomes rather than chlamydial inclusions. Immunofluorescence analysis revealed an association of LC3 and MAP1 subunits A and B with the inclusion as early as 18 h post infection. Inclusion-bound LC3 was connected with the microtubular network. Depolymerization of the microtubular architecture disrupted the association of LC3/MAP1s with the inclusion. Furthermore, siRNA-mediated silencing of the MAP1 and LC3 proteins revealed their essential function in the intracellular growth of C. trachomatis. Interestingly, defective autophagy remarkably enhanced chlamydial growth, suggesting a suppressive effect of the autophagic machinery on bacterial development. However, depletion of LC3 in autophagy-deficient cells noticeably reduced chlamydial propagation. Thus, our findings demonstrate a new function for LC3, distinct from autophagy, in intracellular bacterial pathogenesis.

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“…The nascent chlamydial inclusion acquires the host cell minus‐end‐directed motor protein, dynein, by a process that requires chlamydial protein synthesis and migrates along microtubule tracks to the microtubule organizing center (MTOC) (5). This centripetal migration is conserved in all chlamydial species, and the inhibition of dynein results in reduced development (6,7). The mechanism of dynein recruitment and activation is unique to chlamydiae in that the requirement for the cellular dynein‐activating complex dynactin is circumvented by a chlamydial factor(s), thus bypassing the normal regulation of dynein activity (5).…”

mentioning

confidence: 99%

Chlamydia trachomatis Causes Centrosomal Defects Resulting in Chromosomal Segregation Abnormalities

Grieshaber¹,

Grieshaber²,

Miller³

et al. 2006

Traffic

100

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Chlamydiae traffic along microtubules to the microtubule organizing center (MTOC) to establish an intracellular niche within the host cell. Trafficking to the MTOC is dynein dependent although the activating and cargolinking function of the dynactin complex is supplanted by unknown chlamydial protein(s). We demonstrate that once localized to the MTOC, the chlamydial inclusion maintains a tight association with cellular centrosomes. This association is sustained through mitosis and leads to a significant increase in supernumerary centrosomes, abnormal spindle poles, and chromosomal segregation defects. Chlamydial infection thus can lead to chromosome instability in cells that recover from infection.

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Optimal development of Chlamydophila psittaci in L929 fibroblast and BGM epithelial cells requires the participation of microfilaments and microtubule-motor proteins

Cited by 11 publications

References 57 publications

Chlamydia trachomatis uses host cell dynein to traffic to the microtubule-organizing center in a p50 dynamitin-independent process

Chlamydia trachomatis uses host cell dynein to traffic to the microtubule-organizing center in a p50 dynamitin-independent process

Autophagy-independent function of MAP-LC3 during intracellular propagation ofChlamydia trachomatis

Chlamydia trachomatis Causes Centrosomal Defects Resulting in Chromosomal Segregation Abnormalities

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