ArticleAntimicrobial agents and chemotherapy2015
ADS-J1 inhibits semen-derived amyloid fibril formation and blocks fibril-mediated enhancement of HIV-1 infection.
Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- ADS-J21 is a novel HIV-1 entry inhibitor targeting gp41.Current research in microbial sciences · 2024Article
- Dual concentration-dependent effect of ascorbic acid on PAP(248-286) amyloid formation and SEVI-mediated HIV infection.RSC chemical biology · 2021Article
- Tolcapone Potently Inhibits Seminal Amyloid Fibrils Formation and Blocks Entry of Ebola Pseudoviruses.Frontiers in microbiology · 2020Article
- Article
- The anti-parasitic drug suramin potently inhibits formation of seminal amyloid fibrils and their interaction with HIV-1.The Journal of biological chemistry · 2019Article
- Inhibitory Effect of Naphthoquinone-Tryptophan Hybrid towards Aggregation of PAP f39 Semen Amyloid.Molecules (Basel, Switzerland) · 2018Article
- [PSB0739 inhibits formation of semen-derived amyloid fibril].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018Article
- Myricetin antagonizes semen-derived enhancer of viral infection (SEVI) formation and influences its infection-enhancing activity.Retrovirology · 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
- Sulfonated Compounds Bind with Prostatic Acid Phosphatase (PAPChemistryOpen · 2018Article
- [ADS-J1 antagonizes semen-derived enhancer of virus infection-mediated enhancement of transmitted founder HIV-1 and its matched chronic control strain infection].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018Article
- 3-Hydroxyphthalic Anhydride- Modified Rabbit Anti-PAP IgG as a Potential Bifunctional HIV-1 Entry Inhibitor.Frontiers in microbiology · 2018Article
- [Lactic acid inhibits the formation of semen-derived amyloid fibrils].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2017Article
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Authors and funding
14 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Semen-derived enhancer of viral infection (SEVI) is composed of amyloid fibrils that can greatly enhance HIV-1 infectivity. By its cationic property, SEVI promotes viral sexual transmission by facilitating the attachment and internalization of HIV-1 to target cells. Therefore, semen-derived amyloid fibrils are potential targets for microbicide design. ADS-J1 is an anionic HIV-1 entry inhibitor. In this study, we explored an additional function of ADS-J1: inhibition of SEVI fibril formation and blockage of SEVI-mediated enhancement of viral infection. We found that ADS-J1 bound to an amyloidogenic peptide fragment (PAP248-286, comprising amino acids 248 to 286 of the enzyme prostatic acid phosphatase), thereby inhibiting peptide assembly into amyloid fibrils. In addition, ADS-J1 binds to mature amyloid fibrils and antagonizes fibril-mediated enhancement of viral infection. Unlike cellulose sulfate, a polyanion that failed in clinical trial to prevent HIV-1 sexual transmission, ADS-J1 shows no ability to facilitate fibril formation. More importantly, the combination of ADS-J1 with several antiretroviral drugs exhibited synergistic effects against HIV-1 infection in semen, with little cytotoxicity to vaginal epithelial cells. Our results suggest that ADS-J1 or a derivative may be incorporated into a combination microbicide for prevention of the sexual transmission of HIV-1.
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