AustralieFrV1, Main, Exploration, bibRecord, 00A401

The conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function

Identifieur interne : 00A401 ( Main/Exploration ); précédent : 00A400; suivant : 00A402

The conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function

Auteurs : Kirilee A. Wilson [Australie] ; Séverine B R [France] ; Anne L. Maerz [Australie] ; Marc Alizon [France] ; Pantelis Poumbourios [Australie]

Source :

Journal of virology [ 0022-538X ] ; 2005.

RBID : Pascal:05-0175399

Descripteurs français

Pascal (Inist)
- Homme, Virus, Peptide, Lymphocyte T, Cellule tumorale, Glycoprotéine, Fusion membranaire, Microbiologie, Virologie, Glycine.
Wicri :
- topic : Homme.

English descriptors

KwdEn :
- Glycine, Glycoprotein, Human, Membrane fusion, Microbiology, Peptides, T-Lymphocyte, Tumor cell, Virology, Virus.

Abstract

Retroviral transmembrane proteins (TMs) contain an N-terminal fusion peptide that initiates virus-cell membrane fusion. The fusion peptide is linked to the coiled-coil core through a conserved sequence that is often rich in glycines. We investigated the functional role of the glycine-rich segment, Met-326 to Ser-337, of the human T-cell leukemia virus type 1 (HTLV-1) TM, gp21, by alanine and proline scanning mutagenesis. Alanine substitution for the hydrophobic residue Ile-334 caused an ∼90% reduction in cell-cell fusion activity without detectable effects on the lipid-mixing and pore formation phases of fusion. Alanine substitutions at other positions had smaller effects (Gly-329, Val-330, and Gly-332) or no effect on fusion function. Proline substitution for glycine residues inhibited cell-cell fusion function with position-dependent effects on the three phases of fusion. Retroviral glycoprotein fusion function thus appears to require flexibility within the glycine-rich segment and hydrophobic contacts mediated by this segment.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1061562

Affiliations:

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<front><div type="abstract" xml:lang="en">Retroviral transmembrane proteins (TMs) contain an N-terminal fusion peptide that initiates virus-cell membrane fusion. The fusion peptide is linked to the coiled-coil core through a conserved sequence that is often rich in glycines. We investigated the functional role of the glycine-rich segment, Met-326 to Ser-337, of the human T-cell leukemia virus type 1 (HTLV-1) TM, gp21, by alanine and proline scanning mutagenesis. Alanine substitution for the hydrophobic residue Ile-334 caused an ∼90% reduction in cell-cell fusion activity without detectable effects on the lipid-mixing and pore formation phases of fusion. Alanine substitutions at other positions had smaller effects (Gly-329, Val-330, and Gly-332) or no effect on fusion function. Proline substitution for glycine residues inhibited cell-cell fusion function with position-dependent effects on the three phases of fusion. Retroviral glycoprotein fusion function thus appears to require flexibility within the glycine-rich segment and hydrophobic contacts mediated by this segment.</div>
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The conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function

The conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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