ArticleBiophysical journal2011
Enhancement of HIV-1 infectivity by simple, self-assembling modular peptides.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Comparison of Pleated and Rippled β-Sheet Assembly of Sequence Isomers of an Amphipathic Self-Assembling Peptide.Biochemistry · 2026Article
- A Neutralization Assay Based on Pseudo-Typed Lentivirus with SARS CoV-2 Spike Protein in ACE2-Expressing CRFK Cells.Pathogens (Basel, Switzerland) · 2021Article
- Functional Mammalian Amyloids and Amyloid-Like Proteins.Life (Basel, Switzerland) · 2020Review
- 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
- Review
- Development of peptide inhibitors of HIV transmission.Bioactive materials · 2016Review
- In Situ Investigation of Peptide-Lipid Interaction Between PAP248-286 and Model Cell Membranes.The Journal of membrane biology · 2016Article
- Morphology-Dependent HIV-Enhancing Effect of Semen-Derived Enhancer of Viral Infection.Biophysical journal · 2015Article
- Article
- Fluorescence detection of cationic amyloid fibrils in human semen.Bioorganic & medicinal chemistry letters · 2013Article
- Semen-derived enhancer of viral infection (SEVI) binds bacteria, enhances bacterial phagocytosis by macrophages, and can protect against vaginal infection by a sexually transmitted bacterial pathogen.Antimicrobial agents and chemotherapy · 2013Article
- Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper.European biophysics journal : EBJ · 2012Article
- Seminal plasma accelerates semen-derived enhancer of viral infection (SEVI) fibril formation by the prostatic acid phosphatase (PAP248-286) peptide.The Journal of biological chemistry · 2012Article
- Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286).The journal of physical chemistry. B · 2012Article
- Self-assembling peptide scaffolds for regenerative medicine.Chemical communications (Cambridge, England) · 2012Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Semen-derived enhancer of viral infection (SEVI), an amyloid fibril formed from a cationic peptide fragment of prostatic acidic phosphatase (PAP), dramatically enhances the infectivity of human immunodeficiency virus type 1 (HIV-1). Insoluble, sedimentable fibrils contribute to SEVI-mediated enhancement of virus infection. However, the SEVI-forming PAP(248-286) peptide is able to produce infection-enhancing structures much more quickly than it forms amyloid fibrils. This suggests that soluble supramolecular assemblies may enhance HIV-1 infection. To address this question, non-SEVI amyloid-like fibrils were derived from general amphipathic peptides of sequence Ac-K(n)(XKXE)(2)-NH(2). These cationic peptides efficiently self-assembled to form soluble, fibril-like structures that were, in some cases, able to enhance HIV-1 infection even more efficiently than SEVI. Experiments were also performed to determine whether agents that efficiently shield the charged surface of SEVI fibrils block SEVI-mediated infection-enhancement. To do this, we generated self-assembling anionic peptides of sequence Ac-E(n)(XKXE)(2)-NH(2). One of these peptides completely abrogated SEVI-mediated enhancement of HIV-1 infection, without altering HIV-1 infectivity in the absence of SEVI. Collectively, these data suggest that soluble SEVI assemblies may mediate infection-enhancement, and that anionic peptide supramolecular assemblies have the potential to act as anti-SEVI microbicides.
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