期刊
JOURNAL OF VIROLOGY
卷 74, 期 10, 页码 4634-4644出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.74.10.4634-4644.2000
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资金
- NIAID NIH HHS [R37 AI020201, R37 AI-20201] Funding Source: Medline
Influenza viruses encoding hemagglutinin (HA) and neuraminidase (NA) glycoproteins with deletions in one or both cytoplasmic tails (HAt- or NAt-) have a reduced association with detergent-insoluble glycolipids (DIGs). Mutations which eliminated various combinations of the three palmitoylation sites in HA exhibited reduced amounts of DIG-associated HA in virus-infected cells. The influenza virus matrix (M-1) protein was also found to be associated with DIGs, but this association was decreased in cells infected with HAt- or NAt-virus. Regardless of the amount of DIG-associated protein, the EW and NA glycoproteins were targeted primarily to the apical surface of virus-infected, polarized cells. The uncoupling of DIG association and apical transport was augmented by the observation that the influenza A virus M-2 protein as well as the influenza C virus HA-esterase-fusion glycoprotein were not associated with DIGs but were apically targeted. The reduced DIG association of HAt- and NAt- is an intrinsic property of the glycoproteins, as similar reductions in DIG association were observed when the proteins were expressed from cDNA, Examination of purified virions indicated reduced amounts of DIG-associated Lipids in the envelope of HAt- and NAt- viruses. The data indicate that deletion of both the HA and NA cytoplasmic tails results in reduced DIG association and changes in both virus poly-peptide and lipid composition.
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