ArticleThe Journal of biological chemistry2011
Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 37 citations in OpenAlex.
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- Reconstructing a Missing Link of HIV-1 Assembly: HIV-1 Envelope-Matrix Interactions in a Native Viral Context.bioRxiv : the preprint server for biology · 2026Article
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- Viral and Host Factors Regulating HIV-1 Envelope Protein Trafficking and Particle Incorporation.Viruses · 2022Review
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- Synonymous Codon Pair Recoding of the HIV-1Cells · 2021Article
- Interaction Interface of Mason-Pfizer Monkey Virus Matrix and Envelope Proteins.Journal of virology · 2020Article
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- Gp41-targeted antibodies restore infectivity of a fusion-deficient HIV-1 envelope glycoprotein.PLoS pathogens · 2020Article
- Cross-Species Transmission and Evolution of SIV Chimpanzee Progenitor Viruses Toward HIV-1 in Humanized Mice.Frontiers in microbiology · 2020Article
- Identification of HIV gp41-specific antibodies that mediate killing of infected cells.PLoS pathogens · 2019Article
- Reassessment of the capacity of the HIV-1 Env cytoplasmic domain to trigger NF-κB activation.Virology journal · 2018Article
- Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.Structure (London, England : 1993) · 2017Article
- Statistical correlation of nonconservative substitutions of HIV gp41 variable amino acid residues with the R5X4 HIV-1 phenotype.Virology journal · 2016Article
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- Phylogenetic analysis of HIV type 1 CRF02_AG in multiple genes in Italian and African patients living in Italy.AIDS research and human retroviruses · 2014Article
- The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems.Chemical Society reviews · 2014Review
- Unique functional properties of conserved arginine residues in the lentivirus lytic peptide domains of the C-terminal tail of HIV-1 gp41.The Journal of biological chemistry · 2014Article
- Structural plasticity in the topology of the membrane-interacting domain of HIV-1 gp41.Biophysical journal · 2014Article
- Structural and functional comparisons of retroviral envelope protein C-terminal domains: still much to learn.Viruses · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Although the HIV-1 Env gp120 and gp41 ectodomain have been extensively characterized in terms of structure and function, similar characterizations of the C-terminal tail (CTT) of HIV gp41 remain relatively limited and contradictory. The current study was designed to examine in detail CTT sequence conservation relative to gp120 and the gp41 ectodomain and to examine the conservation of predicted physicochemical and structural properties across a number of divergent HIV clades and groups. Results demonstrate that CTT sequences display intermediate levels of sequence evolution and diversity in comparison to the more diverse gp120 and the more conserved gp41 ectodomain. Despite the relatively high level of CTT sequence variation, the physicochemical properties of the lentivirus lytic peptide domains (LLPs) within the CTT are evidently highly conserved across clades/groups. Additionally, predictions using PEP-FOLD indicate a high level of structural similarity in the LLP regions that was confirmed by circular dichroism measurements of secondary structure of LLP peptides from clades B, C, and group O. Results demonstrate that LLP peptides adopt helical structure in the presence of SDS or trifluoroethanol but are predominantly unstructured in aqueous buffer. Thus, these data for the first time demonstrate strong conservations of characteristic CTT physicochemical and structural properties despite substantial sequence diversity, apparently indicating a delicate balance between evolutionary pressures and the conservation of CTT structure and associated functional roles in virus replication.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.