1998
DOI: 10.1074/jbc.273.22.13430
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Intracellular Transport of the Glycoproteins gE and gI of the Varicella-Zoster Virus

Abstract: The varicella-zoster virus (VZV) is the etiological agent of two different human pathologies, chickenpox (varicella) and shingles (zoster). This alphaherpesvirus is believed to acquire its lipidic envelope in the transGolgi network (TGN). This is consistent with previous data showing that the most abundant VZV envelope glycoprotein gE accumulates at steady-state in this organelle when expressed from cloned cDNA. In the present study, we have investigated the intracellular trafficking of gI, another VZV envelop… Show more

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Cited by 42 publications
(23 citation statements)
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“…The experiments were designed to test predictions about patterns of trafficking of gI and gE in cells infected with the mutant virions. These predictions were based on the assumptions that gI and gE interact at the N-terminal domains of the molecules and that a complex of these two proteins is formed in the RER (1,13,14,21,24). The sorting of gI has previously been studied at the light microscopic level, both in infected cells (20,30) and in transfected cells expressing only gI (1,31,34).…”
Section: Resultsmentioning
confidence: 99%
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“…The experiments were designed to test predictions about patterns of trafficking of gI and gE in cells infected with the mutant virions. These predictions were based on the assumptions that gI and gE interact at the N-terminal domains of the molecules and that a complex of these two proteins is formed in the RER (1,13,14,21,24). The sorting of gI has previously been studied at the light microscopic level, both in infected cells (20,30) and in transfected cells expressing only gI (1,31,34).…”
Section: Resultsmentioning
confidence: 99%
“…These predictions were based on the assumptions that gI and gE interact at the N-terminal domains of the molecules and that a complex of these two proteins is formed in the RER (1,13,14,21,24). The sorting of gI has previously been studied at the light microscopic level, both in infected cells (20,30) and in transfected cells expressing only gI (1,31,34). Nevertheless, the effects of deleting gI, or particular regions of the molecule, on the structure of the TGN, the concentration of other gly- The trafficking of gI in cells infected with intact VZV has previously been described (30) and is thus the expected pattern in cells infected with intact virions.…”
Section: Resultsmentioning
confidence: 99%
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“…The distal C-terminal region of CAPS contains an acidic cluster consisting of MKDSDEEDEEDD, which resembles recently identified sorting motifs in several proteins. Acidic cluster sorting motifs are present in the cytosolic domains of several proteins with different membrane trafficking itineraries (41), including proprotein convertases furin and PC6B, mannose 6-phosphate receptors, herpes virus envelope glycoproteins, and human immunodeficiency virus type 1 Nef (42)(43)(44)(45)(46)(47). Such clusters often contain consensus sites for phosphorylation by casein kinase II, as does that for CAPS, and phosphorylation by casein kinase II regulates sorting.…”
Section: Fig 1 Caps Contains Central C2 and Ph Domainsmentioning
confidence: 99%