ArticleBiophysical journal2009
Helical conformation of the SEVI precursor peptide PAP248-286, a dramatic enhancer of HIV infectivity, promotes lipid aggregation and fusion.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 54 citations in OpenAlex.
- 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
- SEVI Inhibits Aβ Amyloid Aggregation by Capping the β-Sheet Elongation Edges.Journal of chemical information and modeling · 2023Article
- Early stages of misfolding of PAP248-286 at two different pH values: An insight from molecular dynamics simulations.Computational and structural biotechnology journal · 2022Article
- Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology.Biophysical chemistry · 2021Review
- Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.Biophysical chemistry · 2020Review
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- 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
- Sulfonated Compounds Bind with Prostatic Acid Phosphatase (PAPChemistryOpen · 2018Article
- Polydiacetylenyl β-cyclodextrin based smart vesicles for colorimetric assay of arginine and lysine.Scientific reports · 2016Article
- In Situ Investigation of Peptide-Lipid Interaction Between PAP248-286 and Model Cell Membranes.The Journal of membrane biology · 2016Article
- Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.Scientific reports · 2015Article
- Morphology-Dependent HIV-Enhancing Effect of Semen-Derived Enhancer of Viral Infection.Biophysical journal · 2015Article
- Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78).Biochemistry · 2013Article
- Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Biochemistry · 2012Article
- Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286).The journal of physical chemistry. B · 2012Article
- Oligovalent amyloid-binding agents reduce SEVI-mediated enhancement of HIV-1 infection.Journal of the American Chemical Society · 2012Article
- Exploring new biological functions of amyloids: bacteria cell agglutination mediated by host protein aggregation.PLoS pathogens · 2012Article
- The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.Biochimica et biophysica acta · 2011Article
- Enhancement of HIV-1 infectivity by simple, self-assembling modular peptides.Biophysical journal · 2011Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In previous in vivo studies, amyloid fibers formed from a peptide ubiquitous in human seminal fluid (semen-derived enhancer of viral infection (SEVI)) were found to dramatically enhance the infectivity of the HIV virus (3-5 orders of magnitude by some measures). To complement those studies, we performed in vitro assays of PAP(248-286), the most active precursor to SEVI, and other polycationic polymers to investigate the physical mechanisms by which the PAP(248-286) promotes the interaction with lipid bilayers. At acidic (but not at neutral) pH, freshly dissolved PAP(248-286) catalyzes the formation of large lipid flocculates in a variety of membrane compositions, which may be linked to the promotion of convective transport in the vaginal environment rather than transport by a random Brownian motion. Furthermore, PAP(248-286) is itself fusiogenic and weakens the integrity of the membrane in such a way that may promote fusion by the HIV gp41 protein. An alpha-helical conformation of PAP(248-286), lying parallel to the membrane surface, is implicated in promoting bridging interactions between membranes by the screening of the electrostatic repulsion that occurs when two membranes are brought into close contact. This suggests that nonspecific binding of monomeric or small oligomeric forms of SEVI in a helical conformation to lipid membranes may be an additional mechanism by which SEVI enhances the infectivity of the HIV virus.
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