Pinocytotic uptake and intralysosomal crystal formation of Coxsackievirus A9 in monkey kidney cells

Hecker, W.; Meyer, Jürg; Boeni, Regula; Bienz, Kurt

doi:10.1007/bf01240216

Cited by 5 publications

(6 citation statements)

References 39 publications

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“…After 1 h, the virus also began to enter the ␤2M-silenced cells, but this delayed entry did not result in the production of new virus progeny. Thus, without ␤2M, CAV9 seems to be directed to an unproductive endocytic pathway The existence of such an unproductive pathway is supported by the early finding of Hecker et al, who showed that most endocytosed CAV9 particles became accumulated in lysosomes without causing an infection (28). Arf6 is a small GTPase that has multiple roles in the regulation of endosomal membrane traffic and other cellular functions (19).…”

Section: Vol 84 2010mentioning

confidence: 59%

“…An early electron microscopic work by Hecker et al has shown that single CAV9 particles enter monkey kidney cells in vesicles, which then occasionally fuse and form larger structures (28). Interestingly, they found that most internalized virus particles became eventually trapped in large vacuoles, presumably lysosomes, where they were confined without proceeding to capsid uncoating and RNA release.…”

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confidence: 99%

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Internalization of Coxsackievirus A9 Is Mediated by β2-Microglobulin, Dynamin, and Arf6 but Not by Caveolin-1 or Clathrin

Heikkilä

Susi

Tevaluoto

et al. 2010

J Virol

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Coxsackievirus A9 (CAV9) is a member of the human enterovirus B species within the Enterovirus genus of the family Picornaviridae. It has been shown to utilize ␣V integrins, particularly ␣V␤6, as its receptors. The endocytic pathway by which CAV9 enters human cells after the initial attachment to the cell surface has so far been unknown. Here, we present a systematic study concerning the internalization mechanism of CAV9 to A549 human lung carcinoma cells. The small interfering RNA (siRNA) silencing of integrin ␤6 subunit inhibited virus proliferation, confirming that ␣V␤6 mediates the CAV9 infection. However, siRNAs against integrinlinked signaling molecules, such as Src, Fyn, RhoA, phosphatidylinositol 3-kinase, and Akt1, did not reduce CAV9 proliferation, suggesting that the internalization of the virus does not involve integrin-linked signaling events. CAV9 endocytosis was independent of clathrin or caveolin-1 but was restrained by dynasore, an inhibitor of dynamin. The RNA interference silencing of ␤2-microglobulin efficiently inhibited virus infection and caused CAV9 to accumulate on the cell surface. Furthermore, CAV9 infection was found to depend on Arf6 as both silencing of this molecule by siRNA and the expression of a dominant negative construct resulted in decreased virus infection. In conclusion, the internalization of CAV9 to A549 cells follows an endocytic pathway that is dependent on integrin ␣V␤6, ␤2-microglobulin, dynamin, and Arf6 but independent of clathrin and caveolin-1.

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Section: Vol 84 2010mentioning

confidence: 59%

mentioning

confidence: 99%

Internalization of Coxsackievirus A9 Is Mediated by β2-Microglobulin, Dynamin, and Arf6 but Not by Caveolin-1 or Clathrin

Heikkilä

Susi

Tevaluoto

et al. 2010

J Virol

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“…Endocytosis of CV-A9 has mainly been followed in green monkey kidney (GMK) and human lung carcinoma (A549) cell lines [72, 88, 89]. Hecker et al [88] demonstrated in their early work by electron microscopy that CV-A9 particles enter GMK cells in vesicles, which then occasionally fuse and form larger structures.…”

Section: Mechanisms Of Endocytosis Of Integrin-binding Human Picormentioning

confidence: 99%

“…Hecker et al [88] demonstrated in their early work by electron microscopy that CV-A9 particles enter GMK cells in vesicles, which then occasionally fuse and form larger structures. It was also found that most internalized virus particles became trapped in large vacuoles (presumably lysosomes) where they were confined without proceeding to capsid uncoating and RNA release.…”

Section: Mechanisms Of Endocytosis Of Integrin-binding Human Picormentioning

confidence: 99%

“…The recent findings from our laboratory indicate that HPeV-1 binds preferably integrin β 1 and that β 2M participates in the entry process (P. Merilahti and P. Susi, manuscript in preparation). It has been suggested that the clustering and activation of β 1-integrins trigger caveolar endocytosis with the subsequent removal of β 1-integrins from the plasma membrane [43, 107], which is evidently in contradiction with the suggestion that HPeV-1 is endocytosed via clathrin-mediated pathway [88]. On the other hand, MHC I (with β 2M) has been linked to internalization of β 1-integrins, but previously not shown to be involved in HPeV-1 infection [88].…”

Section: Mechanisms Of Endocytosis Of Integrin-binding Human Picormentioning

confidence: 99%

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Endocytosis of Integrin-Binding Human Picornaviruses

Merilahti

Koskinen

Heikkilä

et al. 2012

Advances in Virology

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Picornaviruses that infect humans form one of the largest virus groups with almost three hundred virus types. They include significant enteroviral pathogens such as rhino-, polio-, echo-, and coxsackieviruses and human parechoviruses that cause wide range of disease symptoms. Despite the economic importance of picornaviruses, there are no antivirals. More than ten cellular receptors are known to participate in picornavirus infection, but experimental evidence of their role in cellular infection has been shown for only about twenty picornavirus types. Three enterovirus types and one parechovirus have experimentally been shown to bind and use integrin receptors in cellular infection. These include coxsackievirus A9 (CV-A9), echovirus 9, and human parechovirus 1 that are among the most common and epidemic human picornaviruses and bind to αV-integrins via RGD motif that resides on virus capsid. In contrast, echovirus 1 (E-1) has no RGD and uses integrin α2β1 as cellular receptor. Endocytosis of CV-A9 has recently been shown to occur via a novel Arf6- and dynamin-dependent pathways, while, contrary to collagen binding, E-1 binds inactive β1 integrin and enters via macropinocytosis. In this paper, we review what is known about receptors and endocytosis of integrin-binding human picornaviruses.

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Morphogenesis of the Nodamura virus in the larvae of the lepidopteranGalleria mellonella (L.)

Garzón

Charpentier

Kurstak

1978

Archives of Virology

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The pathogenesis and morphogenesis of the Nodamura virus, an insect picorna- virus which can also infect vertebrates such as newborn mice, are described in the larvae of G. mellonella. Examination of thin sections of muscle, salivary and moulting glands, hemocytes adipose tissue and hypodermis of the infected larvae of G. mellonella shows in the cytoplasm the accumulation of viral particles either dispersed or in a stringlike or paracrystalline array. These arrays of virions can be within membrane- bound vesicles. Helical filaments of 110 A of diameter can be observed inside the basal membranes and later in the cytoplasm, in relation to the infection of muscular or adipose tissues. The morphogenesis of Nodamura virus in G. mellonella or in suckling mice is very similar to that of the Coxsackie A virus observed in the mouse.

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Pinocytotic uptake and intralysosomal crystal formation of Coxsackievirus A9 in monkey kidney cells

Cited by 5 publications

References 39 publications

Internalization of Coxsackievirus A9 Is Mediated by β2-Microglobulin, Dynamin, and Arf6 but Not by Caveolin-1 or Clathrin

Internalization of Coxsackievirus A9 Is Mediated by β2-Microglobulin, Dynamin, and Arf6 but Not by Caveolin-1 or Clathrin

Endocytosis of Integrin-Binding Human Picornaviruses

Morphogenesis of the Nodamura virus in the larvae of the lepidopteranGalleria mellonella (L.)

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