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Literature DB >> 1871979

Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties.

D A Steinhauer¹, S A Wharton, D C Wiley, J J Skehel.

Abstract

The effects of deacylating the H3 influenza hemagglutinin (HA) on its membrane fusion activity were investigated. Chemical deacylation caused no change in the ability of HA to fuse liposomes in vitro. Site-specific mutagenesis of the three cysteine residues in the cytoplasmic tail singly, or in combination, showed that all three were palmitoylated. Substitution of one, two, or all three cysteines with serine and subsequent lack of palmitoylation at mutated sites had no effect on the pH of the conformational change in HA required for fusion activity or the extent of fusion activity.

Entities: Chemical

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Year: 1991 PMID： 1871979 DOI： 10.1016/0042-6822(91)90867-b

Source DB: PubMed Journal: Virology ISSN： 0042-6822 Impact factor: 3.616

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Cited

36 in total

1. Effects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutinin.

Authors: H Y Naim; B Amarneh; N T Ktistakis; M G Roth
Journal: J Virol Date: 1992-12 Impact factor: 5.103

2. Dual role of the cysteine-string domain in membrane binding and palmitoylation-dependent sorting of the molecular chaperone cysteine-string protein.

Authors: Jennifer Greaves; Luke H Chamberlain
Journal: Mol Biol Cell Date: 2006-08-30 Impact factor: 4.138

Review 3. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme.

Authors: Judith M White; Sue E Delos; Matthew Brecher; Kathryn Schornberg
Journal: Crit Rev Biochem Mol Biol Date: 2008 May-Jun Impact factor: 8.250

4. 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

5. Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity.

Authors: D A Steinhauer; J Martín; Y P Lin; S A Wharton; M B Oldstone; J J Skehel; D C Wiley
Journal: Proc Natl Acad Sci U S A Date: 1996-11-12 Impact factor: 11.205

Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties.

1. Effects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutinin.

2. Dual role of the cysteine-string domain in membrane binding and palmitoylation-dependent sorting of the molecular chaperone cysteine-string protein.

Review 3. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme.

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

5. Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity.

6. Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity.

7. Murine leukemia virus R Peptide inhibits influenza virus hemagglutinin-induced membrane fusion.

8. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin.

9. Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin.

10. Cleavage activation of human-adapted influenza virus subtypes by kallikrein-related peptidases 5 and 12.