Correction to: Voltammetric detection of anti-HIV replication drug based on novel nanocomposite gold-nanoparticle–CaCO3 hybrid material

Human immunodeficiency virus (HIV) continues to have a profound global health impact. New infections continue at a high rate despite the development of prophylactic therapies, prompting the need for development of novel preventative approaches. Antimicrobial peptides (AMPs), such as LL-37, display broad microbicidal properties and have potential as anti-HIV agents. LL-37 has been studied for its anti-HIV activity and the limited data available suggest it can inhibit HIV infection in primary T cells as well as exert inhibitory effects on key HIV enzymes. Its immunomodulatory properties may both enhance and inhibit HIV replication. In addition, LL-37 has both 1) the ability to kill other sexually-transmitted pathogens and 2) spermicidal activity; thus, it is a good candidate for multipurpose prevention technology. Further investigation of its anti-HIV activity is warranted.

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A modified nanostructured graphene-gold nanoparticle carbon screen-printed electrode for the sensitive voltammetric detection of rutin

Measurement ◽

10.1016/j.measurement.2017.09.020 ◽

2018 ◽

Vol 114 ◽

pp. 37-43 ◽

Cited By ~ 18

Author(s):

I.M. Apetrei ◽

C. Apetrei

Keyword(s):

Gold Nanoparticle ◽

Screen Printed Electrode ◽

Voltammetric Detection ◽

Screen Printed

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Soybean-derived Bowman-Birk Inhibitor (BBI) Inhibits HIV Replication in Macrophages

Scientific Reports ◽

10.1038/srep34752 ◽

2016 ◽

Vol 6 (1) ◽

Cited By ~ 7

Author(s):

Tong-Cui Ma ◽

Run-Hong Zhou ◽

Xu Wang ◽

Jie-Liang Li ◽

Ming Sang ◽

...

Keyword(s):

Cost Effective ◽

Peripheral Blood Monocyte ◽

Type I ◽

Restriction Factors ◽

Oligoadenylate Synthetase ◽

Hiv Replication ◽

Inhibitory Protein ◽

Anti Hiv

Abstract The Bowman-Birk inhibitor (BBI), a soybean-derived protease inhibitor, is known to have anti-inflammatory effect in both in vitro and in vivo systems. Macrophages play a key role in inflammation and immune activation, which is implicated in HIV disease progression. Here, we investigated the effect of BBI on HIV infection of peripheral blood monocyte-derived macrophages. We demonstrated that BBI could potently inhibit HIV replication in macrophages without cytotoxicity. Investigation of the mechanism(s) of BBI action on HIV showed that BBI induced the expression of IFN-β and multiple IFN stimulated genes (ISGs), including Myxovirus resistance protein 2 (Mx2), 2′,5′-oligoadenylate synthetase (OAS-1), Virus inhibitory protein (viperin), ISG15 and ISG56. BBI treatment of macrophages also increased the expression of several known HIV restriction factors, including APOBEC3F, APOBEC3G and tetherin. Furthermore, BBI enhanced the phosphorylation of IRF3, a key regulator of IFN-β. The inhibition of IFN-β pathway by the neutralization antibody to type I IFN receptor (Anti-IFNAR) abolished BBI-mediated induction of the anti-HIV factors and inhibition of HIV in macrophages. These findings that BBI could activate IFN-β-mediated signaling pathway, initialize the intracellular innate immunity in macrophages and potently inhibit HIV at multiple steps of viral replication cycle indicate the necessity to further investigate BBI as an alternative and cost-effective anti-HIV natural product.

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Antiviral Characteristics of GSK1265744, an HIV Integrase Inhibitor Dosed Orally or by Long-Acting Injection

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.03909-14 ◽

2014 ◽

Vol 59 (1) ◽

pp. 397-406 ◽

Cited By ~ 49

Author(s):

Tomokazu Yoshinaga ◽

Masanori Kobayashi ◽

Takahiro Seki ◽

Shigeru Miki ◽

Chiaki Wakasa-Morimoto ◽

...

Keyword(s):

Synergistic Effects ◽

Integrase Inhibitor ◽

Culture Conditions ◽

Strand Transfer ◽

Hiv Integrase ◽

Hiv Replication ◽

Data Set ◽

Long Acting ◽

Anti Hiv

ABSTRACTGSK1265744 is a new HIV integrase strand transfer inhibitor (INSTI) engineered to deliver efficient antiviral activity with a once-daily, low-milligram dose that does not require a pharmacokinetic booster. Thein vitroantiviral profile and mechanism of action of GSK1265744 were established through integrase enzyme assays, resistance passage experiments, and cellular assays with site-directed molecular (SDM) HIV clones resistant to other classes of anti-HIV-1 agents and earlier INSTIs. GSK1265744 inhibited HIV replication with low or subnanomolar efficacy and with a selectivity index of at least 22,000 under the same culture conditions. The protein-adjusted half-maximal inhibitory concentration (PA-EC50) extrapolated to 100% human serum was 102 nM. When the virus was passaged in the presence of GSK1265744, highly resistant mutants with more than a 10-fold change (FC) in EC50relative to that of the wild-type were not observed for up to 112 days of culture. GSK1265744 demonstrated activity against SDM clones containing the raltegravir (RAL)-resistant Y143R, Q148K, N155H, and G140S/Q148H signature variants (FC less than 6.1), while these mutants had a high FC in the EC50for RAL (11 to >130). Either additive or synergistic effects were observed when GSK1265744 was tested in combination with representative anti-HIV agents, and no antagonistic effects were seen. These findings demonstrate that, similar to dolutegravir, GSK1265744 is differentiated as a new INSTI, having a markedly distinct resistance profile compared with earlier INSTIs, RAL, and elvitegravir (EVG). The collective data set supports further clinical development of GSK1265744.

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TSAO-T Analogues Bearing Amino Acids at Position N-3 of Thymine: Synthesis and Anti-Human Immunodeficiency Virus Activity

Antiviral Chemistry and Chemotherapy ◽

10.1177/095632020001100106 ◽

2000 ◽

Vol 11 (1) ◽

pp. 61-69 ◽

Cited By ~ 3

Author(s):

C Chamorro ◽

E De Clercq ◽

J Balzarini ◽

M-J Camarasa ◽

A San-Félix

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Inhibitory Effect ◽

Acid Moiety ◽

Hiv Replication ◽

Virus Activity ◽

Immunodeficiency Virus ◽

Amino Acid Moiety ◽

Anti Hiv ◽

Hiv 1

Novel analogues of the anti-HIV-1 lead compound [1-[2‘,5’-bis- O-( tert-butyldimethylsilyl)-β-D-ribofuranosyl]thymine]-3‘-spiro-5’-(4“-amino-1”,2“-oxathiole-2‘,2’-dioxide) (TSAO-T) bearing different amino acids at position N-3 of thymine were prepared and evaluated as inhibitors of HIV replication. The synthesis of the target compounds was accomplished by coupling of the appropriate TSAO intermediate with a conveniently protected (L) amino acid in the presence of BOP and triethylamine, followed by depro-tection of the amino acid moiety. Several TSAO derivatives, bearing at N-3 position of the thymine base an L-amino acid retaining the free carboxylic acid, acquired activity against HIV-2, in addition to their inhibitory effect on HIV-1.

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Amplified Voltammetric Detection of DNA Hybridization via Oxidation of Ferrocene Caps on Gold Nanoparticle/Streptavidin Conjugates

Analytical Chemistry ◽

10.1021/ac0344079 ◽

2003 ◽

Vol 75 (15) ◽

pp. 3941-3945 ◽

Cited By ~ 158

Author(s):

Jun Wang ◽

Jinhua Li ◽

Alfred J. Baca ◽

Jingbo Hu ◽

Feimeng Zhou ◽

...

Keyword(s):

Gold Nanoparticle ◽

Dna Hybridization ◽

Voltammetric Detection

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Sensitivity of human immunodeficiency virus infection to various α, β and γ chemokines

Journal of General Virology ◽

10.1099/0022-1317-80-9-2369 ◽

1999 ◽

Vol 80 (9) ◽

pp. 2369-2373 ◽

Cited By ~ 15

Author(s):

Giampaolo Greco ◽

Carl Mackewicz ◽

Jay A. Levy

Keyword(s):

Cell Culture ◽

Human Immunodeficiency Virus ◽

Virus Infection ◽

Therapeutic Strategies ◽

Hiv Replication ◽

Low Concentrations ◽

Immunodeficiency Virus ◽

Large Panel ◽

High Concentrations ◽

Anti Hiv

Examination of a large panel of chemokines indicates that in addition to RANTES, MIP-1α and MIP-1β, the β-chemokine MCP-2 and, to a lesser extent, the γ-chemokine lymphotactin also show anti-human immunodeficiency virus (HIV) activity in cell culture. The amount of chemokine needed to suppress HIV replication by ≤50% was generally greater (≤250 ng/ml) than that required for inhibition of virus infection by RANTES, MIP-1α and MIP-1β. The β-chemokine MCP-3 was found to enhance the replication of both non-syncytium-inducing (NSI) and syncytium-inducing (SI) viruses at high concentrations (0·5–5 μg/ml). In contrast to a previous report, macrophage-derived chemokine was not found to inhibit HIV replication of either NSI or SI viruses, but at low concentrations enhanced NSI virus replication. When small amounts of RANTES or MCP-2 were added together with high concentrations of non-inhibitory chemokines, the anti-HIV effects were countered. Information on chemokines that affect HIV infection could be useful for future therapeutic strategies.

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