Association of Caveolin with Chlamydia trachomatis Inclusions at Early and Late Stages of Infection

Norkin, Leonard C.; Wolfrom, Scott A.; Stuart, Elizabeth S.

doi:10.1006/excr.2001.5202

Cited by 94 publications

(93 citation statements)

References 46 publications

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“…Interestingly, these caveolincontaining vesicles, or caveosomes, traffic along a pathway independent of the clathrin pathway to perinuclear compartments (including Golgi and endoplasmic reticulum) that bypass the lysosomes and hence degradation (42). Caveosomes also retain a neutral pH throughout, and these properties ensure the viability and integrity of trafficking proteins and pathogens (42)(43)(44). In contrast, endocytosis via clathrin-dependent pathways is well-established to connect with endosomes that use the Rab family of adapter molecules, have an acidic pH, and feed into the lysosomal pathway (30,45).…”

Section: Discussionmentioning

confidence: 99%

Lipid Microdomains Are Required Sites for the Selective Endocytosis and Nuclear Translocation of IFN-γ, Its Receptor Chain IFN-γ Receptor-1, and the Phosphorylation and Nuclear Translocation of STAT1α

Subramaniam

Johnson

2002

The Journal of Immunology

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IFN-γ contains a nuclear localization sequence that may play a role in the nuclear transport of activated STAT1α via a complex of IFN-γ/IFN-γ receptor (IFNGR)-1/STAT1α with the nuclear importer nucleoprotein interactor 1. In this study, we examine the mechanism of endocytosis of IFNGR-1 and the relationship of its nuclear translocation to that of STAT1α. In untreated WISH cells, both IFNGR-1 and IFNGR-2 were constitutively localized within caveolae-like microdomains isolated from plasma membrane. However, treatment of cells with IFN-γ resulted in rapid migration of IFNGR-1, but not IFNGR-2, from these microdomains. Filipin pretreatment, which specifically inhibits endocytosis from caveolae-like microdomains, inhibited the nuclear translocation of IFN-γ and IFNGR-1 as well as the tyrosine phosphorylation and nuclear translocation of STAT1α, but did not affect the binding of IFN-γ to these cells. In the Jurkat T lymphocyte cell line, which does not express caveolin-1, nuclear translocation of IFNGR-1 and STAT1α were similarly inhibited by filipin pretreatment. Isolation of lipid microdomains from Jurkat cells showed that both IFNGR-1 and IFNGR-2 were associated with lipid microdomains only after stimulation with IFN-γ, suggesting that the IFNGR subunits are recruited to lipid microdomains by IFN-γ binding in lymphocytes (Jurkat) in contrast to their constitutive presence in epithelial (WISH) cells. In contrast, treatments that block clathrin-dependent endocytosis did not inhibit either activation or nuclear translocation of STAT1α or the nuclear translocation of IFN-γ or IFNGR-1. Thus, membrane lipid microdomains play an important role in IFN-γ-initiated endocytic events involving IFNGR-1, and the nuclear translocation of IFN-γ, IFNGR-1, and STAT1α.

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Section: Discussionmentioning

confidence: 99%

Lipid Microdomains Are Required Sites for the Selective Endocytosis and Nuclear Translocation of IFN-γ, Its Receptor Chain IFN-γ Receptor-1, and the Phosphorylation and Nuclear Translocation of STAT1α

Subramaniam

Johnson

2002

The Journal of Immunology

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“…The actin rearrangements that occur during entry are transient and may be terminated by secreted chlamydial effectors such as CT166, which glucosylates Rac1 (Thalmann et al 2010), or CT694, which interacts and colocalizes with AHNAK, an actin-binding protein (Hower et al 2009). Additional host factors that contribute to uptake into nonphagocytic cells include clathrin (Boleti et al 1999;Hybiske and Stephens 2007a) and cholesterol-rich microdomains (Norkin et al 2001;Jutras et al 2003;Stuart et al 2003;Gabel et al 2004). …”

Section: Mechanisms Of Chlamydia Invasion Of Epithelial Cellsmentioning

confidence: 99%

Chlamydial Intracellular Survival Strategies

Bastidas

Elwell

Engel

et al. 2013

Cold Spring Harbor Perspectives in Medicine

206

197

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Chlamydia trachomatis is the most common sexually transmitted bacterial pathogen and the causative agent of blinding trachoma. Although Chlamydia is protected from humoral immune responses by residing within remodeled intracellular vacuoles, it still must contend with multilayered intracellular innate immune defenses deployed by its host while scavenging for nutrients. Here we provide an overview of Chlamydia biology and highlight recent findings detailing how this vacuole-bound pathogen manipulates host -cellular functions to invade host cells and maintain a replicative niche.

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“…In addition, a variety of other obligate intracellular pathogens, including protozoa and bacteria, are now known to enter cells via caveolae or caveolae-like raft domains (reviewed in reference 45). Those pathogens include the protozoa Toxoplasma gondii (41) and Plasmodium falciparum (28) and the bacteria Campylobacter jejuni (69), FimH-expressing E. coli (5,61), and serovar K of Chlamydia trachomatis (48). Each of these intracellular protozoan and bacterial pathogens must find an appropriate niche within the host cell in which they can survive and propagate.…”

Section: Vol 76 2002 Bfa-sensitive Sv40 Entry and Release Of Vp2 Inmentioning

confidence: 99%

Caveolar Endocytosis of Simian Virus 40 Is Followed by Brefeldin A-Sensitive Transport to the Endoplasmic Reticulum, Where the Virus Disassembles

Norkin

Anderson

Wolfrom

et al. 2002

J Virol

182

197

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Simian virus 40 (SV40) enters cells by atypical endocytosis mediated by caveolae that transports the virus to the endoplasmic reticulum (ER) instead of to the endosomal-lysosomal compartment, which is the usual destination for viruses and other cargo that enter by endocytosis. We show here that SV4O is transported to the ER via an intermediate compartment that contains ␤-COP, which is best known as a component of the COPI coatamer complexes that are required for the retrograde retrieval pathway from the Golgi to the ER. Additionally, transport of SV40 to the ER, as well as infection, is sensitive to brefeldin A. This drug acts by specifically inhibiting the ARF1 GTPase, which is known to regulate assembly of COPI coat complexes on Golgi cisternae. Moreover, some ␤-COP colocalizes with intracellular caveolin-1, which was previously shown to be present on a new organelle ( Simian virus 40 (SV40) enters host cells by an atypical endocytic process mediated by caveolae (1,10,44,53,58,65), rather than by clathrin-coated pits. Caveolae are small invaginations of the plasma membrane that are distinguished from clathrin-coated pits by their size (70 to 100 nm), distinctive flask-like shape, and lack of a visible coat in thin sections.

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Association of Caveolin with Chlamydia trachomatis Inclusions at Early and Late Stages of Infection

Cited by 94 publications

References 46 publications

Lipid Microdomains Are Required Sites for the Selective Endocytosis and Nuclear Translocation of IFN-γ, Its Receptor Chain IFN-γ Receptor-1, and the Phosphorylation and Nuclear Translocation of STAT1α

Lipid Microdomains Are Required Sites for the Selective Endocytosis and Nuclear Translocation of IFN-γ, Its Receptor Chain IFN-γ Receptor-1, and the Phosphorylation and Nuclear Translocation of STAT1α

Chlamydial Intracellular Survival Strategies

Caveolar Endocytosis of Simian Virus 40 Is Followed by Brefeldin A-Sensitive Transport to the Endoplasmic Reticulum, Where the Virus Disassembles

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