Directed Egress of Animal Viruses Promotes Cell-to-Cell Spread

Johnson, David C.; Huber, Mary T.

doi:10.1128/jvi.76.1.1-8.2002

Cited by 231 publications

(201 citation statements)

References 103 publications

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“…Internalization of double-membrane GJ vesicles is an intriguing process with similarities to phagocytosis or intracellular pathogen (protozoa, bacteria, or viruses) invasion and cell-to-cell spreading (Johnson and Huber, 2002;Cossart et al, 2003;Gruenheid and Finlay, 2003;Rust et al, 2004;Gouin et al, 2005). AGJ vesicle formation requires active double-membrane protrusion and/or invagination, neck restriction, and double-membrane fission/resealing.…”

Section: Comparable Clathrin-mediated Internalization Processesmentioning

confidence: 99%

Internalization of Large Double-Membrane Intercellular Vesicles by a Clathrin-dependent Endocytic Process

Piehl

Lehmann

Gumpert

et al. 2007

MBoC

156

233

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Beyond its well-documented role in vesicle endocytosis, clathrin has also been implicated in the internalization of large particles such as viruses, pathogenic bacteria, and even latex beads. We have discovered an additional clathrin-dependent endocytic process that results in the internalization of large, double-membrane vesicles at lateral membranes of cells that are coupled by gap junctions (GJs). GJ channels bridge apposing cell membranes to mediate the direct transfer of electrical currents and signaling molecules from cell to cell. Here, we report that entire GJ plaques, clusters of GJ channels, can be internalized to form large, double-membrane vesicles previously termed annular gap junctions (AGJs). These internalized AGJ vesicles subdivide into smaller vesicles that are degraded by endo/lysosomal pathways. Mechanistic analyses revealed that clathrin-dependent endocytosis machinery-components, including clathrin itself, the alternative clathrin-adaptor Dab2, dynamin, myosin-VI, and actin are involved in the internalization, inward movement, and degradation of these large, intercellular double-membrane vesicles. These findings contribute to the understanding of clathrin's numerous emerging functions. INTRODUCTIONThe role of clathrin in endocytosis is well documented. This protein forms a typical curved lattice around endocytic vesicles that are internalized at the plasma membrane (PM). In addition, the involvement of clathrin in several uncharacteristic endocytic processes has been reported, including the internalization of viruses, pathogenic bacteria, and large latex beads (Aggeler and Werb, 1982;Ehrlich et al., 2004;Rust et al., 2004;Veiga and Cossart, 2005). Here, we describe another function of the clathrin-dependent endocytic machinery that results in the internalization of large, doublemembrane vesicles at lateral PMs of cells that are coupled by gap junctions (GJs).GJs are ubiquitously distributed channels that connect the cytoplasms of two apposing cells each participating in this connection via a half channel termed a connexon to provide direct cell-to-cell communication. Connexons are hexamers of four-pass membrane proteins called connexins (Cxs;Bruzzone et al., 1996;Kumar and Gilula, 1996). Once transported to the PM, GJ channels cluster into two-dimensional arrays termed plaques that can be composed of a few to many thousands of individual channels and vary from a few square nanometers to many square micrometers (Bruzzone et al., 1996; Falk, 2000a;Severs et al., 2001). GJ channels can open and close (gate) and physiological parameters, including intracellular pH, Ca 2ϩ concentration, and Cx phosphorylation, are known to modulate GJ channel gating and the extent of GJ-mediated intercellular coupling (Delmar et al., 2004;Lampe and Lau, 2004;Moreno, 2005). However, the extent of intercellular coupling could also be regulated through altering the number of GJ channels in the PM.Cxs have a surprisingly short half-life of only 1-5 h, leading to a rapid GJ and Cx protein turnover (Fallon and Goodeno...

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Section: Comparable Clathrin-mediated Internalization Processesmentioning

confidence: 99%

Internalization of Large Double-Membrane Intercellular Vesicles by a Clathrin-dependent Endocytic Process

Piehl

Lehmann

Gumpert

et al. 2007

MBoC

156

233

View full text Add to dashboard Cite

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“…We therefore conclude that the tested cancer cells, and the B25 H-Ras transformed fibroblasts, lacked the requirement of anchorage during cytokinesis. Oncogenic H-Ras promotes anchorage-independent growth in soft agar (16,17) and may thus be able to abolish the control in cytokinesis. However, transfection of H-Ras V12 alone induces senescence in primary fibroblasts, and we therefore used the immortalized BJT cells as a model system for studies of the role of H-Ras V12 in cytokinesis (18).…”

Section: Cell Attachment Facilitates Complete Cleavage Furrow Ingressionmentioning

confidence: 99%

Oncogenic H-Ras V12 promotes anchorage-independent cytokinesis in human fibroblasts

Thullberg

Gad

Guyader

et al. 2007

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

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Cell anchorage is required for cell proliferation of untransformed cells, whereas anchorage-independent growth can be induced by oncogenes and is a hallmark of transformation. Whereas anchorage-dependent control of the progression of the G1 phase of the cell cycle has been extensively studied, it is less clear whether and how anchorage may control other cell cycle phases and whether oncogenes may affect such controls. Here, we found that lack of cell anchorage did not influence progression through the cell cycle S phase, G2 phase, or most of mitosis of primary human fibroblasts. However, unanchored fibroblasts could not complete cytokinesis. The cleavage furrow and central spindle were still formed in the absence of anchorage, but cells were unable to complete ingression, causing binucleation. Importantly, V12 H-Ras-transformed fibroblasts and two cancer cell lines progressed through the entire cell cycle without anchorage, including through cytokinesis. This indicates that oncogenic signaling may contribute to anchorageindependent growth and tumorigenesis by promoting the final cleavage furrow ingression during cytokinesis.cell adhesion ͉ integrin ͉ extracellular matrix ͉ signaling ͉ cell cycle

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“…1,2). The molecular mechanism of this mode of transmission is poorly understood, but it is known to share some mechanistic details with the entry of extracellular virions (1), namely the use of the essential core fusion machinery, consisting of glycoproteins B, D, H, and L (gB, gD, gH, and gL, respectively). Moreover, it requires glycoproteins E and I (gE and gI, respectively) (1), which are not necessary for "cell-free" transmission (3).…”

mentioning

confidence: 99%

Function of glycoprotein E of herpes simplex virus requires coordinated assembly of three tegument proteins on its cytoplasmic tail

Han

Chadha

Starkey

et al. 2012

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

140

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Glycoprotein E (gE) of HSV plays a key role in cell-to-cell spread and virus-induced cell fusion. Here, we report that this function of gE requires the cooperation of tegument proteins UL11, UL16, and UL21. We found that the four proteins come together with very high efficiency to form a complex in transfected cells and in a manner that is regulated and coordinated. In particular, the inefficient interaction of UL16 with each membrane protein (UL11 and gE) observed in pairwise transfections became efficient when other binding partners were present. The significance of these interactions was revealed in studies of viral mutants, which showed that each of these tegument proteins is critical for processing, transport, and biological activity of gE. These findings provide insights into the mechanisms of how gE executes its function and also have implications in understanding HSV assembly and budding.

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Directed Egress of Animal Viruses Promotes Cell-to-Cell Spread

Cited by 231 publications

References 103 publications

Internalization of Large Double-Membrane Intercellular Vesicles by a Clathrin-dependent Endocytic Process

Internalization of Large Double-Membrane Intercellular Vesicles by a Clathrin-dependent Endocytic Process

Oncogenic H-Ras V12 promotes anchorage-independent cytokinesis in human fibroblasts

Function of glycoprotein E of herpes simplex virus requires coordinated assembly of three tegument proteins on its cytoplasmic tail

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