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Text
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URL Address
<a href="http://doi.org/10.1007/bf01323238" target="_blank" rel="noreferrer noopener">http://doi.org/10.1007/bf01323238</a>
Pages
2163–2181
Issue
12
Volume
140
Dublin Core
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Title
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A block in glycoprotein processing correlates with small plaque morphology and virion targetting to cell-cell junctions for an oral and an anal strain of herpes simplex virus type-1.
Publisher
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Archives of virology
Date
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1995
1995
Subject
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*Protein Processing; Anal Canal/virology; Animals; Cercopithecus aethiops; Electron; Fluorescent Antibody Technique; Genetic Complementation Test; Herpesvirus 1; Human/genetics/isolation & purification/*physiology; Humans; Indirect; Intercellular Junctions/physiology/*virology; Kinetics; Microscopy; Mouth/virology; Post-Translational; Species Specificity; Vero Cells; Viral Envelope Proteins/*biosynthesis/metabolism; Viral Plaque Assay; Virion/*physiology
Creator
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Dick J W; Rosenthal K S
Description
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The characteristics of two clinical isolates of HSV-1 obtained from an oral (424) and an anal (490) lesion were compared with the highly passaged KOS strain. In contrast to KOS, the clinical isolates produced small plaques, were more cell-associated and the predominant viral glycoprotein species for gC and gD in infected cell lysates was the precursor, high mannose glycoform. Total virus production in Vero cells was equivalent for the three virus strains in one-step growths. Pulse-chase studies of glycoprotein C processing showed a reduction in rate at 7.5 h post infection and a significant block in processing at 10.5 h post infection for 424 and 490 but not KOS. Similar results were obtained for gD. The significant reduction in glycoprotein processing for 424 and 490 suggests a block in transport of viral glycoproteins or virions to and through the Golgi apparatus. Extracellular virions and the cell surface, prior to cell lysis, contained the processed gC glycoform suggesting a competent cellular glycan processing system. Upon co-infection of 424 or 490 with KOS or a gC- KOS strain, gC was processed to levels equivalent to KOS indicating that 424 and 490 are not inhibitory but that an activity(s) encoded by KOS facilitates maturation of gC from 424 and 490. Unlike KOS infected Vero cells, virion-containing vacuoles were observed in the cytoplasm at 12 h p.i. and extracellular virions were concentrated at cell-cell junctions of 424 or 490 infected cells but not in the perinuclear region. These results suggest that intracellular transport of viral glycoproteins and virions in 424 and 490 infected cells is different from KOS infected cells. The reduced level of viral glycoprotein maturation, virus release, cell surface presence and presence of virions at cell-cell junctions are consistent with small plaque production in tissue culture cells.
Identifier
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<a href="http://doi.org/10.1007/bf01323238" target="_blank" rel="noreferrer noopener">10.1007/bf01323238</a>
Rights
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Protein Processing
1995
Anal Canal/virology
Animals
Archives of virology
Cercopithecus aethiops
Dick J W
Electron
Fluorescent Antibody Technique
Genetic Complementation Test
Herpesvirus 1
Human/genetics/isolation & purification/*physiology
Humans
Indirect
Intercellular Junctions/physiology/*virology
Kinetics
Microscopy
Mouth/virology
Post-Translational
Rosenthal K S
Species Specificity
Vero Cells
Viral Envelope Proteins/*biosynthesis/metabolism
Viral Plaque Assay
Virion/*physiology