Literature DB >> 7957116

The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity.

H Jin1, G P Leser, R A Lamb.   

Abstract

The influenza A virus hemagglutinin (HA) glycoprotein contains a cytoplasmic tail which consists of 10-11 amino acids, of which five residues re conserved in all subtypes of influenza A virus. As the cytoplasmic tail is not needed for intracellular transport to the plasma membrane, it has become virtually dogma that the role of the cytoplasmic tail is in forming protein-protein interactions necessary for creating an infectious budding virus. To investigate the role of the HA cytoplasmic tail in virus replication, reverse genetics was used to obtain an influenza virus that lacked an HA cytoplasmic tail. The rescued virus contained the HA of subtype A/Udorn/72 in a helper virus (subtype A/WSN/33) background. Biochemical analysis indicated that only the introduced tail- HA was incorporated into virions and these particles lacked a detectable fragment of the helper virus HA. The tail- HA rescued virus assembled and replicated almost as efficiently as virions containing wild-type HA, suggesting that the cytoplasmic tail is not essential for the virus assembly process. Nonetheless, a revertant virus was isolated, suggesting that possession of a cytoplasmic tail does confer an advantage.

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Year:  1994        PMID: 7957116      PMCID: PMC395508          DOI: 10.1002/j.1460-2075.1994.tb06885.x

Source DB:  PubMed          Journal:  EMBO J        ISSN: 0261-4189            Impact factor:   11.598


  40 in total

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Authors:  C Wang; K Takeuchi; L H Pinto; R A Lamb
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2.  Nucleocapsid-glycoprotein interactions required for assembly of alphaviruses.

Authors:  S Lopez; J S Yao; R J Kuhn; E G Strauss; J H Strauss
Journal:  J Virol       Date:  1994-03       Impact factor: 5.103

3.  Synthesis of influenza virus proteins in infected cells: translation of viral polypeptides, including three P polypeptides, from RNA produced by primary transcription.

Authors:  R A Lamb; P W Choppin
Journal:  Virology       Date:  1976-10-15       Impact factor: 3.616

4.  Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.

Authors:  P Palese; K Tobita; M Ueda; R W Compans
Journal:  Virology       Date:  1974-10       Impact factor: 3.616

5.  Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions.

Authors:  P Bilsel; M R Castrucci; Y Kawaoka
Journal:  J Virol       Date:  1993-11       Impact factor: 5.103

6.  Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface.

Authors:  R A Lamb; S L Zebedee; C D Richardson
Journal:  Cell       Date:  1985-03       Impact factor: 41.582

Review 7.  The budding mechanisms of enveloped animal viruses.

Authors:  K Simons; H Garoff
Journal:  J Gen Virol       Date:  1980-09       Impact factor: 3.891

8.  Evidence for a ninth influenza viral polypeptide.

Authors:  R A Lamb; P R Etkind; P W Choppin
Journal:  Virology       Date:  1978-11       Impact factor: 3.616

9.  Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum.

Authors:  W E Balch; J M McCaffery; H Plutner; M G Farquhar
Journal:  Cell       Date:  1994-03-11       Impact factor: 41.582

10.  DNA sequencing with chain-terminating inhibitors.

Authors:  F Sanger; S Nicklen; A R Coulson
Journal:  Proc Natl Acad Sci U S A       Date:  1977-12       Impact factor: 11.205

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  50 in total

1.  Plasmid-driven formation of influenza virus-like particles.

Authors:  G Neumann; T Watanabe; Y Kawaoka
Journal:  J Virol       Date:  2000-01       Impact factor: 5.103

2.  The membrane-proximal stem region of vesicular stomatitis virus G protein confers efficient virus assembly.

Authors:  C S Robison; M A Whitt
Journal:  J Virol       Date:  2000-03       Impact factor: 5.103

3.  Influenza virus matrix protein is the major driving force in virus budding.

Authors:  P Gómez-Puertas; C Albo; E Pérez-Pastrana; A Vivo; A Portela
Journal:  J Virol       Date:  2000-12       Impact factor: 5.103

4.  Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.

Authors:  C Kozerski; E Ponimaskin; B Schroth-Diez; M F Schmidt; A Herrmann
Journal:  J Virol       Date:  2000-08       Impact factor: 5.103

5.  Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion.

Authors:  G B Melikyan; S Lin; M G Roth; F S Cohen
Journal:  Mol Biol Cell       Date:  1999-06       Impact factor: 4.138

6.  Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.

Authors:  H Jin; G P Leser; J Zhang; R A Lamb
Journal:  EMBO J       Date:  1997-03-17       Impact factor: 11.598

Review 7.  The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement.

Authors:  F S Cohen; G B Melikyan
Journal:  J Membr Biol       Date:  2004-05-01       Impact factor: 1.843

Review 8.  Virus maturation by budding.

Authors:  H Garoff; R Hewson; D J Opstelten
Journal:  Microbiol Mol Biol Rev       Date:  1998-12       Impact factor: 11.056

9.  Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin.

Authors:  M Ohuchi; C Fischer; R Ohuchi; A Herwig; H D Klenk
Journal:  J Virol       Date:  1998-05       Impact factor: 5.103

10.  Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles.

Authors:  Benjamin J Chen; George P Leser; Eiji Morita; Robert A Lamb
Journal:  J Virol       Date:  2007-05-02       Impact factor: 5.103

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