ArticleBiology2012
The Surprising Role of Amyloid Fibrils in HIV Infection.
Article in Biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 61 citations in OpenAlex.
- Disease-disease interactions: molecular links of neurodegenerative diseases with cancer, viral infections, and type 2 diabetes.Translational neurodegeneration · 2025Review
- α-Synuclein fibrils enhance HIV-1 infection of human T cells, macrophages and microglia.Nature communications · 2025Article
- Unraveling the Role of Functional Amyloids and Amyloid Peptides in Disease Detection.Protein and peptide letters · 2025Review
- Investigating the Effects of the POPC-POPG Lipid Bilayer Composition on PAP248-286 Binding Using CG Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- Could a Non-Cellular Molecular Interactome in the Blood Circulation Influence Pathogens' Infectivity?Cells · 2023Review
- Extent of N-Terminus Folding of Semenogelin 1 Cleavage Product Determines Tendency to Amyloid Formation.International journal of molecular sciences · 2023Article
- Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition.Molecules (Basel, Switzerland) · 2022Review
- Dual concentration-dependent effect of ascorbic acid on PAP(248-286) amyloid formation and SEVI-mediated HIV infection.RSC chemical biology · 2021Article
- Prion-Like Proteins in Phase Separation and Their Link to Disease.Biomolecules · 2021Review
- Supramolecular Mechanism of Viral Envelope Disruption by Molecular Tweezers.Journal of the American Chemical Society · 2020Article
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Tolcapone Potently Inhibits Seminal Amyloid Fibrils Formation and Blocks Entry of Ebola Pseudoviruses.Frontiers in microbiology · 2020Article
- Impact of semen-derived amyloid (SEVI) on sperm viability and motility: its implication in male reproductive fitness.European biophysics journal : EBJ · 2019Article
- Natural Inhibitor of Human Cytomegalovirus in Human Seminal Plasma.Journal of virology · 2019Article
- Inhibitory Effect of Naphthoquinone-Tryptophan Hybrid towards Aggregation of PAP f39 Semen Amyloid.Molecules (Basel, Switzerland) · 2018Article
- Myricetin antagonizes semen-derived enhancer of viral infection (SEVI) formation and influences its infection-enhancing activity.Retrovirology · 2018Article
- Enhancement of Ebola virus infection by seminal amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structure, function and antagonism of semen amyloids.Chemical communications (Cambridge, England) · 2018Review
- Semen-derived amyloidogenic peptides-Key players of HIV infection.Protein science : a publication of the Protein Society · 2018Review
- Semen inhibits Zika virus infection of cells and tissues from the anogenital region.Nature communications · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Despite its discovery over 30 years ago, human immunodeficiency virus (HIV) continues to threaten public health worldwide. Semen is the principal vehicle for the transmission of this retrovirus and several endogenous peptides in semen, including fragments of prostatic acid phosphatase (PAP248-286 and PAP85-120) and semenogelins (SEM1 and SEM2), assemble into amyloid fibrils that promote HIV infection. For example, PAP248-286 fibrils, termed SEVI (Semen derived Enhancer of Viral Infection), potentiate HIV infection by up to 105-fold. Fibrils enhance infectivity by facilitating virion attachment and fusion to target cells, whereas soluble peptides have no effect. Importantly, the stimulatory effect is greatest at low viral titers, which mimics mucosal transmission of HIV, where relatively few virions traverse the mucosal barrier. Devising a method to rapidly reverse fibril formation (rather than simply inhibit it) would provide an innovative and urgently needed preventative strategy for reducing HIV infection via the sexual route. Targeting a host-encoded protein conformer represents a departure from traditional microbicidal approaches that target the viral machinery, and could synergize with direct antiviral approaches. Here, we review the identification of these amyloidogenic peptides, their mechanism of action, and various strategies for inhibiting their HIV-enhancing effects.
Identifiers
What OpenQuestion holds
Registered trials
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.