Peptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures.
Peptide dendrimers are a class of molecules that exhibit a large array of biological effects including antiviral activity. In this report, we analyzed the antiviral activity of the peptide-derivatized SB105-A10 dendrimer, which is a tetra-branched dendrimer synthetized on a lysine core, in activated...
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2013
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oai:doaj.org-article:4cf657f2ec314e03aa554e6599afaf102021-11-18T08:52:13ZPeptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures.1932-620310.1371/journal.pone.0076482https://doaj.org/article/4cf657f2ec314e03aa554e6599afaf102013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24116111/?tool=EBIhttps://doaj.org/toc/1932-6203Peptide dendrimers are a class of molecules that exhibit a large array of biological effects including antiviral activity. In this report, we analyzed the antiviral activity of the peptide-derivatized SB105-A10 dendrimer, which is a tetra-branched dendrimer synthetized on a lysine core, in activated peripheral blood mononuclear cells (PBMCs) that were challenged with reference and wild-type human immunodeficiency virus type 1 (HIV-1) strains. SB105-A10 inhibited infections by HIV-1 X4 and R5 strains, interfering with the early phases of the viral replication cycle. SB105-A10 targets heparan sulfate proteoglycans (HSPGs) and, importantly, the surface plasmon resonance (SPR) assay revealed that SB105-A10 strongly binds gp41 and gp120, most likely preventing HIV-1 attachment/entry through multiple mechanisms. Interestingly, the antiviral activity of SB105-A10 was also detectable in an organ-like structure of human cervicovaginal tissue, in which SB105-A10 inhibited the HIV-1ada R5 strain infection without altering the tissue viability. These results demonstrated the strong antiviral activity of SB105-A10 and suggest a potential microbicide use of this dendrimer to prevent the heterosexual transmission of HIV-1.Isabella BonDavid LemboMarco RusnatiAlberto ClòSilvia MoriniAnna MiserocchiAntonella BugattiSonia GrigolonGiuseppina MusumeciSanto LandolfoMaria Carla ReDavide GibelliniPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e76482 (2013) |
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EN |
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Medicine R Science Q |
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Medicine R Science Q Isabella Bon David Lembo Marco Rusnati Alberto Clò Silvia Morini Anna Miserocchi Antonella Bugatti Sonia Grigolon Giuseppina Musumeci Santo Landolfo Maria Carla Re Davide Gibellini Peptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures. |
| description |
Peptide dendrimers are a class of molecules that exhibit a large array of biological effects including antiviral activity. In this report, we analyzed the antiviral activity of the peptide-derivatized SB105-A10 dendrimer, which is a tetra-branched dendrimer synthetized on a lysine core, in activated peripheral blood mononuclear cells (PBMCs) that were challenged with reference and wild-type human immunodeficiency virus type 1 (HIV-1) strains. SB105-A10 inhibited infections by HIV-1 X4 and R5 strains, interfering with the early phases of the viral replication cycle. SB105-A10 targets heparan sulfate proteoglycans (HSPGs) and, importantly, the surface plasmon resonance (SPR) assay revealed that SB105-A10 strongly binds gp41 and gp120, most likely preventing HIV-1 attachment/entry through multiple mechanisms. Interestingly, the antiviral activity of SB105-A10 was also detectable in an organ-like structure of human cervicovaginal tissue, in which SB105-A10 inhibited the HIV-1ada R5 strain infection without altering the tissue viability. These results demonstrated the strong antiviral activity of SB105-A10 and suggest a potential microbicide use of this dendrimer to prevent the heterosexual transmission of HIV-1. |
| format |
article |
| author |
Isabella Bon David Lembo Marco Rusnati Alberto Clò Silvia Morini Anna Miserocchi Antonella Bugatti Sonia Grigolon Giuseppina Musumeci Santo Landolfo Maria Carla Re Davide Gibellini |
| author_facet |
Isabella Bon David Lembo Marco Rusnati Alberto Clò Silvia Morini Anna Miserocchi Antonella Bugatti Sonia Grigolon Giuseppina Musumeci Santo Landolfo Maria Carla Re Davide Gibellini |
| author_sort |
Isabella Bon |
| title |
Peptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures. |
| title_short |
Peptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures. |
| title_full |
Peptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures. |
| title_fullStr |
Peptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures. |
| title_full_unstemmed |
Peptide-derivatized SB105-A10 dendrimer inhibits the infectivity of R5 and X4 HIV-1 strains in primary PBMCs and cervicovaginal histocultures. |
| title_sort |
peptide-derivatized sb105-a10 dendrimer inhibits the infectivity of r5 and x4 hiv-1 strains in primary pbmcs and cervicovaginal histocultures. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2013 |
| url |
https://doaj.org/article/4cf657f2ec314e03aa554e6599afaf10 |
| work_keys_str_mv |
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