ArticleJournal of virology2005
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.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- NLK interacts with 14‑3‑3ζ to restore the expression of E‑cadherin.Oncology reports · 2020Article
- Arginine 37 of Glycine Linker Dictates Regulatory Function of HapR.Frontiers in microbiology · 2020Article
- The HTLV-1 gp21 fusion peptide inhibits antigen specific T-cell activation in-vitro and in mice.PLoS pathogens · 2018Article
- Linkers in the structural biology of protein-protein interactions.Protein science : a publication of the Protein Society · 2013Review
- Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation.European biophysics journal : EBJ · 2012Article
- Cellular Factors Involved in HTLV-1 Entry and Pathogenicit.Frontiers in microbiology · 2012Article
- The SCHOOL of nature: IV. Learning from viruses.Self/nonself · 2010Article
- Article
- Mutational analysis of the hepatitis C virus E1 glycoprotein in retroviral pseudoparticles and cell-culture-derived H77/JFH1 chimeric infectious virus particles.Journal of viral hepatitis · 2009Article
- Viral pathogenesis, modulation of immune receptor signaling and treatment.Advances in experimental medicine and biology · 2008Review
- SCHOOL model and new targeting strategies.Advances in experimental medicine and biology · 2008Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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 approximately 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.
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