Literature DB >> 2177097

Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins.

P Chambers1, C R Pringle, A J Easton.   

Abstract

Extensive regions of heptad repeat units consistent with an alpha-helical coiled coil conformation are located adjacent to hydrophobic, potentially fusion-related regions in the amino acid sequences of paramyxovirus fusion and retrovirus envelope glycoproteins. Similar arrangements of hydrophobic peptides and heptad repeat units exist in coronavirus peplomer proteins and influenza virus haemagglutinins. This suggests that there may be similarities in the structures of these proteins and in the functions of the hydrophobic fusion-related regions during virus entry.

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Year:  1990        PMID： 2177097     DOI： 10.1099/0022-1317-71-12-3075

Source DB:  PubMed          Journal:  J Gen Virol        ISSN： 0022-1317            Impact factor:   3.891


  121 in total

1.  Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion.

Authors:  Z Luo; A M Matthews; S R Weiss
Journal:  J Virol       Date:  1999-10       Impact factor: 5.103

2.  The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil.

Authors:  J M Matthews; T F Young; S P Tucker; J P Mackay
Journal:  J Virol       Date:  2000-07       Impact factor: 5.103

3.  Mutations in the fusion peptide and adjacent heptad repeat inhibit folding or activity of the Newcastle disease virus fusion protein.

Authors:  T A Sergel; L W McGinnes; T G Morrison
Journal:  J Virol       Date:  2001-09       Impact factor: 5.103

4.  Variable sensitivity to substitutions in the N-terminal heptad repeat of Mason-Pfizer monkey virus transmembrane protein.

Authors:  Chisu Song; Eric Hunter
Journal:  J Virol       Date:  2003-07       Impact factor: 5.103

5.  Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses.

Authors:  X M Zhang; K G Kousoulas; J Storz
Journal:  Virology       Date:  1991-07       Impact factor: 3.616

6.  Intracellular processing of the paramyxovirus F protein: critical role of the predicted amphipathic alpha helix adjacent to the fusion domain.

Authors:  C Wang; G Raghu; T Morrison; M E Peeples
Journal:  J Virol       Date:  1992-07       Impact factor: 5.103

7.  Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis.

Authors:  M Lu; M O Stoller; S Wang; J Liu; M B Fagan; J H Nunberg
Journal:  J Virol       Date:  2001-11       Impact factor: 5.103

8.  Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex.

Authors:  C Wild; J W Dubay; T Greenwell; T Baird; T G Oas; C McDanal; E Hunter; T Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  1994-12-20       Impact factor: 11.205

9.  One proline deletion in the fusion peptide of neurotropic mouse hepatitis virus (MHV) restricts retrograde axonal transport and neurodegeneration.

Authors:  Saurav Saswat Rout; Manmeet Singh; Kenneth S Shindler; Jayasri Das Sarma
Journal:  J Biol Chem       Date:  2020-04-05       Impact factor: 5.157

10.  Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.

Authors:  Berend Jan Bosch; Willem Bartelink; Peter J M Rottier
Journal:  J Virol       Date:  2008-06-18       Impact factor: 5.103
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