Cell-specific envelope glycosylation distinguishes FIV glycoproteins produced in cytopathically and noncytopathically infected cells

Mary Poss, Steven W. Dow, Edward A. Hoover

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Feline immunodeficiency virus (FIV) infection induces syncytium formation and cell death in primary feline astrocyte cultures but persistently and noncytopathically infects Crandall feline kidney cells (CrFK). Because viral envelope glycoproteins are implicated in cell fusion events we evaluated the astrocyte-produced FIV surface glycoprotein for properties that might distinguish it from that produced in CrFK cells. The surface glycoprotein from astrocytes migrated faster on SDS-PAGE and contained more Endo H-sensitive oligosaccharides than that from CrFK, although the precursor and deglycosylated envelope glycoproteins from both cells were the same size. Castanospermine treatment of infected astrocytes, which blocks glucose trimming from oligosaccharide side chains of glycoproteins, both obliterated the mobility difference between astrocyte- and CrFK-produced FIV surface glycoproteins and prevented syncytium in infected astrocyte cultures. These results demonstrate the importance of the infected cell type in viral envelope protein glycosylation and implicate cell type-specific carbohydrate structures on retroviral glycoproteins as mediators of cell fusion.

Original languageEnglish (US)
Pages (from-to)25-32
Number of pages8
JournalVirology
Volume188
Issue number1
DOIs
StatePublished - Jan 1 1992

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Feline Immunodeficiency Virus
Glycosylation
Glycoproteins
Astrocytes
Felidae
Membrane Glycoproteins
Kidney
Cell Fusion
Giant Cells
Oligosaccharides
Viral Envelope Proteins
Surface Properties
Virus Diseases
Polyacrylamide Gel Electrophoresis
Cell Death
Carbohydrates
Glucose

All Science Journal Classification (ASJC) codes

  • Virology
  • Infectious Diseases

Cite this

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abstract = "Feline immunodeficiency virus (FIV) infection induces syncytium formation and cell death in primary feline astrocyte cultures but persistently and noncytopathically infects Crandall feline kidney cells (CrFK). Because viral envelope glycoproteins are implicated in cell fusion events we evaluated the astrocyte-produced FIV surface glycoprotein for properties that might distinguish it from that produced in CrFK cells. The surface glycoprotein from astrocytes migrated faster on SDS-PAGE and contained more Endo H-sensitive oligosaccharides than that from CrFK, although the precursor and deglycosylated envelope glycoproteins from both cells were the same size. Castanospermine treatment of infected astrocytes, which blocks glucose trimming from oligosaccharide side chains of glycoproteins, both obliterated the mobility difference between astrocyte- and CrFK-produced FIV surface glycoproteins and prevented syncytium in infected astrocyte cultures. These results demonstrate the importance of the infected cell type in viral envelope protein glycosylation and implicate cell type-specific carbohydrate structures on retroviral glycoproteins as mediators of cell fusion.",
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Cell-specific envelope glycosylation distinguishes FIV glycoproteins produced in cytopathically and noncytopathically infected cells. / Poss, Mary; Dow, Steven W.; Hoover, Edward A.

In: Virology, Vol. 188, No. 1, 01.01.1992, p. 25-32.

Research output: Contribution to journalArticle

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T1 - Cell-specific envelope glycosylation distinguishes FIV glycoproteins produced in cytopathically and noncytopathically infected cells

AU - Poss, Mary

AU - Dow, Steven W.

AU - Hoover, Edward A.

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N2 - Feline immunodeficiency virus (FIV) infection induces syncytium formation and cell death in primary feline astrocyte cultures but persistently and noncytopathically infects Crandall feline kidney cells (CrFK). Because viral envelope glycoproteins are implicated in cell fusion events we evaluated the astrocyte-produced FIV surface glycoprotein for properties that might distinguish it from that produced in CrFK cells. The surface glycoprotein from astrocytes migrated faster on SDS-PAGE and contained more Endo H-sensitive oligosaccharides than that from CrFK, although the precursor and deglycosylated envelope glycoproteins from both cells were the same size. Castanospermine treatment of infected astrocytes, which blocks glucose trimming from oligosaccharide side chains of glycoproteins, both obliterated the mobility difference between astrocyte- and CrFK-produced FIV surface glycoproteins and prevented syncytium in infected astrocyte cultures. These results demonstrate the importance of the infected cell type in viral envelope protein glycosylation and implicate cell type-specific carbohydrate structures on retroviral glycoproteins as mediators of cell fusion.

AB - Feline immunodeficiency virus (FIV) infection induces syncytium formation and cell death in primary feline astrocyte cultures but persistently and noncytopathically infects Crandall feline kidney cells (CrFK). Because viral envelope glycoproteins are implicated in cell fusion events we evaluated the astrocyte-produced FIV surface glycoprotein for properties that might distinguish it from that produced in CrFK cells. The surface glycoprotein from astrocytes migrated faster on SDS-PAGE and contained more Endo H-sensitive oligosaccharides than that from CrFK, although the precursor and deglycosylated envelope glycoproteins from both cells were the same size. Castanospermine treatment of infected astrocytes, which blocks glucose trimming from oligosaccharide side chains of glycoproteins, both obliterated the mobility difference between astrocyte- and CrFK-produced FIV surface glycoproteins and prevented syncytium in infected astrocyte cultures. These results demonstrate the importance of the infected cell type in viral envelope protein glycosylation and implicate cell type-specific carbohydrate structures on retroviral glycoproteins as mediators of cell fusion.

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