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Journal articles on the topic 'HIV fusion inhibitor'

Author: Grafiati

Published: 7 September 2021

Last updated: 29 July 2025

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1

Tremblay, Cécile L., Françoise Giguel, Christopher Kollmann, et al. "Anti-Human Immunodeficiency Virus Interactions of SCH-C (SCH 351125), a CCR5 Antagonist, with Other Antiretroviral Agents In Vitro." Antimicrobial Agents and Chemotherapy 46, no. 5 (2002): 1336–39. http://dx.doi.org/10.1128/aac.46.5.1336-1339.2002.

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ABSTRACT SCH-C (SCH 351125) is a small-molecule antagonist of the human immunodeficiency virus type 1(HIV-1) coreceptor CCR5. It has in vitro activity against R5 viruses with 50% inhibitory concentrations ranging from 1.0 to 30.9 nM. We have studied anti-HIV-1 interactions of SCH-C with other antiretroviral agents in vitro. Synergistic interactions were seen with nucleoside reverse transcriptase inhibitors (zidovudine and lamivudine), nonnucleoside reverse transcriptase inhibitors (efavirenz), and protease inhibitors (indinavir) at all inhibitory concentrations evaluated. We have also studied

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2

Xu, Wei, Zhe Cong, Qianyu Duan, et al. "A Protein-Based, Long-Acting HIV-1 Fusion Inhibitor with an Improved Pharmacokinetic Profile." Pharmaceuticals 15, no. 4 (2022): 424. http://dx.doi.org/10.3390/ph15040424.

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Recently, a series of highly effective peptide- or protein-based HIV fusion inhibitors have been identified. However, due to their short half-life, their clinical application is limited. Therefore, the development of long-acting HIV fusion inhibitors is urgently needed. Here, we designed and constructed a protein-based, long-acting HIV fusion inhibitor, termed FLT (FN3-L35-T1144), consisting of a monobody, FN3, which contains an albumin-binding domain (ABD), a 35-mer linker (L35), and a peptide-based HIV fusion inhibitor, T1144. We found that FLT bound, via its FN3 component, with human serum

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3

Descalzi-Montoya, Dante, Jihong Dai, Sukhwinder Singh, and Patricia Fitzgerald-Bocarsly. "Human plasmacytoid dendritic cells and myeloid Dendritic cells fuse with chronically HIV-infected T cells (168.23)." Journal of Immunology 188, no. 1_Supplement (2012): 168.23. http://dx.doi.org/10.4049/jimmunol.188.supp.168.23.

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Abstract Our laboratory has previously shown that plasmacytoid dendritic cells (pDC) fuse with chronically-HIV infected H9 T cells and also with acutely infected CD4+ primary T cells; a process mediated by virus/CD4 and CXCR4 interactions. In the present study, using the Amnis ImageStream, we observed that fusions can also form between chronically-HIV infected H9 T cells and myeloid dendritic cells (mDC). MDC showed a tendency to form more fusions than pDC. Although the fusion of mDC with HIV-infected H9 T cells was prevented by the CXCR4 inhibitor AMD3100, it was not affected by the CCR5 inhi

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4

Balzarini, J., and E. De Clercq. "The Thiocarboxanilides UC-10 and UC-781 Have an Additive Inhibitory Effect against Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Replication in Cell Culture When Combined with other Antiretroviral Drugs." Antiviral Chemistry and Chemotherapy 8, no. 3 (1997): 197–204. http://dx.doi.org/10.1177/095632029700800303.

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The thiocarboxanilides represent a structural class of potent and selective human immunodeficiency virus type 1 (HIV-1)-specific reverse transcriptase (RT) inhibitors. Combinations of the clinical candidate thiocarboxanilides UC-10 (oxime ether derivative) and UC-781 (pentenyloxy ether derivative) with a variety of nucleoside RT inhibitors (NRTIs) and non-nucleoside RT inhibitors (NNRTIs), two HIV protease inhibitors and one fusion/uncoating inhibitor were evaluated for their inhibitory effects on HIV-1 RT activity and HIV-1 replication in CEM cell cultures. The inhibitory activity of the NNRT

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5

BAO, JU, JIN F. LIU, XIAO HE, and JOHN Z. H. ZHANG. "COMPUTATIONAL STUDY OF HIV-1 gp41 NHR TRIMER: INHIBITION MECHANISMS OF N-SUBSTITUTED PYRROLE DERIVATIVES AND FRAGMENT-BASED VIRTUAL SCREENING." Journal of Theoretical and Computational Chemistry 12, no. 08 (2013): 1341001. http://dx.doi.org/10.1142/s0219633613410010.

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Fusion of HIV-1 viral and host cellular membranes is an important step for HIV infection. The HIV-1 envelope glycoprotein mediating the membrane fusion consists of subunits gp120 and gp41 whereas gp120 recognizes the cell-surface receptors and gp41 promotes viral-cell membrane fusion. The trimeric helical complex composed of heterodimer of N-terminal and C-terminal extraviral segments has been used for the gp41 function study, and the trimeric N-terminal teptad repeat (NHR) is considered as an antiviral drug target for developing HIV-1 membrane fusion inhibitors. By using computational solvent

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6

Su, Yang, Huihiui Chong, Shengwen Xiong, Yuanyuan Qiao, Zonglin Qiu, and Yuxian He. "Genetic Pathway of HIV-1 Resistance to Novel Fusion Inhibitors Targeting the Gp41 Pocket." Journal of Virology 89, no. 24 (2015): 12467–79. http://dx.doi.org/10.1128/jvi.01741-15.

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ABSTRACTThe peptide drug enfuvirtide (T20) is the only HIV-1 fusion inhibitor in clinical use, but it easily induces drug resistance, calling for new strategies for developing effective drugs. On the basis of the M-T hook structure, we recently developed highly potent short-peptide HIV-1 fusion inhibitors (MTSC22 and HP23), which mainly target the conserved gp41 pocket and possess high genetic barriers to resistance. Here, we focused on the selection and characterization of HIV-1 escape mutants of MTSC22, which revealed new resistance pathways and mechanisms. Two mutations (E49K and L57R) loca

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7

Naito, Takeshi, Kazuki Izumi, Eiichi Kodama та ін. "SC29EK, a Peptide Fusion Inhibitor with Enhanced α-Helicity, Inhibits Replication of Human Immunodeficiency Virus Type 1 Mutants Resistant to Enfuvirtide". Antimicrobial Agents and Chemotherapy 53, № 3 (2008): 1013–18. http://dx.doi.org/10.1128/aac.01211-08.

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ABSTRACT Peptides derived from the α-helical domains of human immunodeficiency virus (HIV) type 1 (HIV-1) gp41 inhibit HIV-1 fusion to the cell membrane. Enfuvirtide (T-20) is a peptide-based drug that targets the step of HIV fusion, and as such, it effectively suppresses the replication of HIV-1 strains that are either wild type or resistant to multiple reverse transcriptase and/or protease inhibitors. However, HIV-1 variants with T-20 resistance have emerged; therefore, the development of new and potent inhibitors is urgently needed. We have developed a novel HIV fusion inhibitor, SC34EK, wh

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8

Osborne, Newton G. "Enfuvirtide: The First HIV Fusion Inhibitor." Journal of Gynecologic Surgery 20, no. 3 (2004): 103–4. http://dx.doi.org/10.1089/gyn.2004.20.103.

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9

Lazzarin, Adriano. "Enfuvirtide: the first HIV fusion inhibitor." Expert Opinion on Pharmacotherapy 6, no. 3 (2005): 453–64. http://dx.doi.org/10.1517/14656566.6.3.453.

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10

Das, Debananda, Kenji Maeda, Yasuhiro Hayashi, et al. "Insights into the Mechanism of Inhibition of CXCR4: Identification of Piperidinylethanamine Analogs as Anti-HIV-1 Inhibitors." Antimicrobial Agents and Chemotherapy 59, no. 4 (2015): 1895–904. http://dx.doi.org/10.1128/aac.04654-14.

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ABSTRACTThe cellular entry of HIV-1 into CD4+T cells requires ordered interactions of HIV-1 envelope glycoprotein with C-X-C chemokine receptor type 4 (CXCR4) receptors. However, such interactions, which should be critical for rational structure-based discovery of new CXCR4 inhibitors, remain poorly understood. Here we first determined the effects of amino acid substitutions in CXCR4 on HIV-1NL4-3glycoprotein-elicited fusion events using site-directed mutagenesis-based fusion assays and identified 11 potentially key amino acid substitutions, including D97A and E288A, which caused >30% reduc

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11

Pang, Wei, Rui-Rui Wang, Yue-Dong Gao, et al. "A Novel Enzyme-Linked Immunosorbent Assay for Screening HIV-1 Fusion Inhibitors Targeting HIV-1 Gp41 Core Structure." Journal of Biomolecular Screening 16, no. 2 (2011): 221–29. http://dx.doi.org/10.1177/1087057110393333.

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The gp41 subunit of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein mediates the fusion of viral and host cell membranes. As the HIV-1 enters the host cells, the 2 helical regions, HR1 and HR2, in the ectodomain of gp41 can form a 6-helix bundle, which brings the viral and target cell membranes to close proximity and serves as an attractive target for developing HIV-1 fusion inhibitors. Now, there are several cell- and molecule-based assays to identify potential HIV-1 fusion inhibitors targeting gp41. However, these assays cannot be used universally because they are time-

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12

Lin, P. F., H. Samanta, C. M. Bechtold, et al. "Characterization of siamycin I, a human immunodeficiency virus fusion inhibitor." Antimicrobial Agents and Chemotherapy 40, no. 1 (1996): 133–38. http://dx.doi.org/10.1128/aac.40.1.133.

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The human immunodeficiency virus (HIV) fusion inhibitor siamycin I, a 21-residue tricyclic peptide, was identified from a Streptomyces culture by using a cell fusion assay involving cocultivation of HeLa-CD4+ cells and monkey kidney (BSC-1) cells expressing the HIV envelope gp160. Siamycin I is effective against acute HIV type 1 (HIV-1) and HIV-2 infections, with 50% effective doses ranging from 0.05 to 5.7 microM, and the concentration resulting in a 50% decrease in cell viability in the absence of viral infection is 150 microM in CEM-SS cells. Siamycin I inhibits fusion between C8166 cells a

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13

Reeves, Jacqueline D., John L. Miamidian, Mark J. Biscone, et al. "Impact of Mutations in the Coreceptor Binding Site on Human Immunodeficiency Virus Type 1 Fusion, Infection, and Entry Inhibitor Sensitivity." Journal of Virology 78, no. 10 (2004): 5476–85. http://dx.doi.org/10.1128/jvi.78.10.5476-5485.2004.

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ABSTRACT An increasingly large number of antiviral agents that prevent entry of human immunodeficiency virus (HIV) into cells are in preclinical and clinical development. The envelope (Env) protein of HIV is the major viral determinant that affects sensitivity to these compounds. To understand how changes in Env can impact entry inhibitor sensitivity, we introduced six mutations into the conserved coreceptor binding site of the R5 HIV-1 strain YU-2 and measured the effect of these changes on CD4 and coreceptor binding, membrane fusion levels and rates, virus infection, and sensitivity to the f

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14

Schaeffer, Evelyne, Vanessa B. Soros, and Warner C. Greene. "Compensatory Link between Fusion and Endocytosis of Human Immunodeficiency Virus Type 1 in Human CD4 T Lymphocytes." Journal of Virology 78, no. 3 (2004): 1375–83. http://dx.doi.org/10.1128/jvi.78.3.1375-1383.2004.

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ABSTRACT Virions of the type 1 human immunodeficiency virus (HIV-1) can enter target cells by fusion or endocytosis, with sharply different functional consequences. Fusion promotes productive infection of the target cell, while endocytosis generally leads to virion inactivation in acidified endosomes or degradation in lysosomes. Virion fusion and endocytosis occur equally in T cells, but these pathways have been regarded as independent because endocytosis of HIV virions requires neither CD4 nor CCR5/CXCR4 engagement in HeLa-CD4 cells. Using flow cytometric techniques to assess the binding and

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15

He, Yuxian, Jianwei Cheng, Jingjing Li, et al. "Identification of a Critical Motif for the Human Immunodeficiency Virus Type 1 (HIV-1) gp41 Core Structure: Implications for Designing Novel Anti-HIV Fusion Inhibitors." Journal of Virology 82, no. 13 (2008): 6349–58. http://dx.doi.org/10.1128/jvi.00319-08.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) entry into the host cell involves a cascade of events and currently represents one of most attractive targets in the search for new antiviral drugs. The fusion-active gp41 core structure is a stable six-helix bundle (6-HB) folded by its trimeric N-terminal heptad repeat (NHR) and C-terminal heptad repeat (CHR). Peptides derived from the CHR region of HIV-1 gp41 are potent fusion inhibitors that target the NHR to block viral and cellular membrane fusion in a dominant negative fashion. However, all CHR peptides reported to date are derived pri

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16

Reeves, Jacqueline D., Fang-Hua Lee, John L. Miamidian, Cassandra B. Jabara, Marisa M. Juntilla, and Robert W. Doms. "Enfuvirtide Resistance Mutations: Impact on Human Immunodeficiency Virus Envelope Function, Entry Inhibitor Sensitivity, and Virus Neutralization." Journal of Virology 79, no. 8 (2005): 4991–99. http://dx.doi.org/10.1128/jvi.79.8.4991-4999.2005.

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ABSTRACT Enfuvirtide (ENF/T-20/Fuzeon), the first human immunodeficiency virus (HIV) entry inhibitor to be licensed, targets a structural intermediate of the entry process. ENF binds the HR1 domain in gp41 after Env has bound CD4, preventing conformational changes needed for membrane fusion. Mutations in HR1 that confer ENF resistance can arise following ENF therapy. ENF resistance mutations were introduced into an R5- and X4-tropic Env to examine their impact on fusion, infection, and sensitivity to different classes of entry inhibitors and neutralizing antibodies. HR1 mutations could reduce

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17

Pan, Chungen, Lifeng Cai, Hong Lu, Zhi Qi, and Shibo Jiang. "Combinations of the First and Next Generations of Human Immunodeficiency Virus (HIV) Fusion Inhibitors Exhibit a Highly Potent Synergistic Effect against Enfuvirtide- Sensitive and -Resistant HIV Type 1 Strains." Journal of Virology 83, no. 16 (2009): 7862–72. http://dx.doi.org/10.1128/jvi.00168-09.

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ABSTRACT T20 (generic name, enfuvirtide; brand name, Fuzeon) is a first-generation human immunodeficiency virus (HIV) fusion inhibitor approved for salvage therapy of HIV-infected patients refractory to current antiretroviral drugs. However, its clinical use is limited because of rapid emergence of T20-resistant viruses in T20-treated patients. Therefore, T1249 and T1144 are being developed as the second- and third-generation HIV fusion inhibitors, respectively, with improved efficacy and drug resistance profiles. Here, we found that combinations of T20 with T1249 and/or T1144 resulted in exce

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18

Eggink, Dirk, Steven W. de Taeye, Ilja Bontjer, et al. "HIV-1 Escape from a Peptidic Anchor Inhibitor through Stabilization of the Envelope Glycoprotein Spike." Journal of Virology 90, no. 23 (2016): 10587–99. http://dx.doi.org/10.1128/jvi.01616-16.

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ABSTRACTThe trimeric HIV-1 envelope glycoprotein spike (Env) mediates viral entry into cells by using a spring-loaded mechanism that allows for the controlled insertion of the Env fusion peptide into the target membrane, followed by membrane fusion. Env is the focus of vaccine research aimed at inducing protective immunity by antibodies as well as efforts to develop drugs that inhibit the viral entry process. The molecular factors contributing to Env stability and decay need to be understood better in order to optimally design vaccines and therapeutics. We generated viruses with resistance to

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19

Liu, Hui, Xiaomiao Shi, Dongmei Guo, Zuowei Zhao, and Yimin. "Feature Selection Combined with Neural Network Structure Optimization for HIV-1 Protease Cleavage Site Prediction." BioMed Research International 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/263586.

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It is crucial to understand the specificity of HIV-1 protease for designing HIV-1 protease inhibitors. In this paper, a new feature selection method combined with neural network structure optimization is proposed to analyze the specificity of HIV-1 protease and find the important positions in an octapeptide that determined its cleavability. Two kinds of newly proposed features based on Amino Acid Index database plus traditional orthogonal encoding features are used in this paper, taking both physiochemical and sequence information into consideration. Results of feature selection prove thatp2,p

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20

MacFarlane, Emma. "Enfuvirtide: The first fusion inhibitor for HIV." Practice Nursing 16, no. 5 (2005): 220–23. http://dx.doi.org/10.12968/pnur.2005.16.5.18061.

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21

Wang, Rui-Rui, Liu-Meng Yang, Yun-Hua Wang, et al. "Sifuvirtide, a potent HIV fusion inhibitor peptide." Biochemical and Biophysical Research Communications 382, no. 3 (2009): 540–44. http://dx.doi.org/10.1016/j.bbrc.2009.03.057.

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22

Harmon, Brooke, та Lee Ratner. "Induction of the Gαq Signaling Cascade by the Human Immunodeficiency Virus Envelope Is Required for Virus Entry". Journal of Virology 82, № 18 (2008): 9191–205. http://dx.doi.org/10.1128/jvi.00424-08.

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ABSTRACT Binding of human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) with the primary receptor CD4 and one of two coreceptors, CXCR4 or CCR5, activates a signaling cascade resulting in Rac-1 GTPase activation and stimulation of actin cytoskeletal reorganizations critical for HIV-1-mediated membrane fusion. The mechanism by which HIV-1 Env induces Rac-1 activation and subsequent actin cytoskeleton rearrangement is unknown. In this study, we show that Env-mediated Rac-1 activation is dependent on the activation of Gαq and its downstream targets. Fusion and Rac-1 activation

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23

Xu, Liang, Zeye Han, and Hongqian Ren. "Synthesis, Biophysical Characterization, and Anti-HIV-1 Fusion Activity of DNA Quadruplex-based Inhibitors with Dipeptide MT Hook Conjugation." Current HIV Research 19, no. 4 (2021): 317–23. http://dx.doi.org/10.2174/1570162x19666210423121601.

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Background: Human immunodeficiency virus type-1 (HIV-1) infection is the reason for the epidemic of acquired immunodeficiency syndrome (AIDS). The development of HIV-1 fusion inhibitors has gained increasing attention as they were found to be effective in the early stage of HIV-1. DNA G-quadruplex-based inhibitors have been found to interact with HIV-1 envelope glycoprotein, showing anti–HIV-1 fusion activity. C-peptide-derived molecules with Met-Thr terminal also showed potent anti-fusion activity; the Met-Thr dipeptide adopted a hook-like structure (termed MT hook) in the hydrophobic pocket

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24

Kagiampakis, Ioannis, Arbi Gharibi, Marie K. Mankowski, et al. "Potent Strategy To Inhibit HIV-1 by Binding both gp120 and gp41." Antimicrobial Agents and Chemotherapy 55, no. 1 (2010): 264–75. http://dx.doi.org/10.1128/aac.00376-10.

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ABSTRACTThe development of an anti-HIV microbicide is critical in the fight against the spread of HIV. It is shown here that the covalent linking of compounds that bind gp120 with compounds that bind gp41 can inhibit HIV entry even more potently than individual inhibitors or noncovalent combinations. The most striking example involves griffithsin, a potent HIV inhibitor that binds to the surface of HIV gp120. While griffithsin inhibits HIV Env-mediated fusion in a CCR5-tropic cell-cell fusion assay with a 50% inhibitory concentration (IC50) of 1.31 ± 0.87 nM and the gp41-binding peptide C37 sh

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Xie, Hua, Natalya I. Belogortseva, Jie Wu, Wei-Hong Lai, and Chin-ho Chen. "Inhibition of Human Immunodeficiency Virus Type 1 Entry by a Binding Domain of Porphyromonas gingivalis Gingipain." Antimicrobial Agents and Chemotherapy 50, no. 9 (2006): 3070–74. http://dx.doi.org/10.1128/aac.01578-05.

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ABSTRACT Human immunodeficiency virus (HIV) transmission through saliva is extremely low. Several oral components, including secretory immunoglobulin A and secretory leukocyte protease inhibitor, are known as potential inhibitory agents of HIV oral transmission. Here we examined anti-HIV activity of oral bacterial components. We showed that recombinant protein HGP44 derived from Porphyromonas gingivalis, one of the primary infectious agents of periodontitis, was capable of inhibiting HIV type 1 (HIV-1) replication. HGP44 bound specifically to HIV-1 gp120 and blocked HIV-1 envelope-mediated mem

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Su, Yang, Huihiui Chong, Zonglin Qiu, Shengwen Xiong, and Yuxian He. "Mechanism of HIV-1 Resistance to Short-Peptide Fusion Inhibitors Targeting the Gp41 Pocket." Journal of Virology 89, no. 11 (2015): 5801–11. http://dx.doi.org/10.1128/jvi.00373-15.

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ABSTRACTThe deep hydrophobic pocket on the N trimer of HIV-1 gp41 has been considered an ideal drug target. On the basis of the M-T hook structure, we recently developed short-peptide-based HIV-1 fusion inhibitors (MTSC22 and HP23), which mainly target the pocket site and possess highly potent antiviral activity. In this study, we focused on investigating their resistance pathways and mechanisms by escape HIV-1 mutants to SC22EK, a template peptide for MTSC22 and HP23. Two substitutions, E49K and N126K, located, respectively, at the N- and C-heptad repeat regions of gp41, were identified as co

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Moranguinho, Inês, Nuno Taveira, and Inês Bártolo. "Antiretroviral Treatment of HIV-2 Infection: Available Drugs, Resistance Pathways, and Promising New Compounds." International Journal of Molecular Sciences 24, no. 6 (2023): 5905. http://dx.doi.org/10.3390/ijms24065905.

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Currently, it is estimated that 1–2 million people worldwide are infected with HIV-2, accounting for 3–5% of the global burden of HIV. The course of HIV-2 infection is longer compared to HIV-1 infection, but without effective antiretroviral therapy (ART), a substantial proportion of infected patients will progress to AIDS and die. Antiretroviral drugs in clinical use were designed for HIV-1 and, unfortunately, some do not work as well, or do not work at all, for HIV-2. This is the case for non-nucleoside reverse transcriptase inhibitors (NNRTIs), the fusion inhibitor enfuvirtide (T-20), most p

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Ray, Neelanjana, Jessamina E. Harrison, Leslie A. Blackburn, Jeffrey N. Martin, Steven G. Deeks, and Robert W. Doms. "Clinical Resistance to Enfuvirtide Does Not Affect Susceptibility ofHuman Immunodeficiency Virus Type 1 to Other Classes of Entry Inhibitors." Journal of Virology 81, no. 7 (2007): 3240–50. http://dx.doi.org/10.1128/jvi.02413-06.

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ABSTRACT The clinical use of the human immunodeficiency virus (HIV) fusion inhibitor enfuvirtide (ENF) can select for drug-resistant HIV-1 strains bearing mutations in the HR1 region of the viral envelope (Env) protein. We analyzed the properties of multiple Env proteins isolated from five patients who experienced an initial decline in viral load after ENF therapy followed by subsequent rebound due to emergence of ENF-resistant HIV-1. Prior to ENF therapy, each patient harbored genetically and phenotypically diverse Env proteins that used CCR5 and/or CXCR4 to elicit membrane fusion. Coreceptor

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Dwipayana, I. Dewa Agung Panji, Yana Maolana Syah, Reza Aditama, Feraliana Feraliana, and Azzania Fibriani. "Development of a dimer-based screening system for dimerization inhibitor of HIV-1 protease." Journal of Microbial Systematics and Biotechnology 2, no. 2 (2020): 1–11. http://dx.doi.org/10.37604/jmsb.v2i2.42.

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An in vitro dimer-based screening system (DBSS) for selecting new HIV-1 protease dimerization inhibitor candidates from natural compounds had been established. This system utilizes a fusion between HIV-1 protease and dimer binding domain of AraC protein (proteaseHIV1-AraCDBD) where fluorescence signal will be emitted in the presence of HIV-1 protease inhibitor. However, this screening system had not been evaluated. Therefore, this study was aimed to evaluate it in recombinant Escherichia coli culture. The expression of proteaseHIV1-AraCDBD fusion gene was observed for 18 hours. Its crude lysat

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Jiang, Shibo, Hong Lu, Shuwen Liu, Qian Zhao, Yuxian He, and Asim K. Debnath. "N-Substituted Pyrrole Derivatives as Novel Human Immunodeficiency Virus Type 1 Entry Inhibitors That Interfere with the gp41 Six-Helix Bundle Formation and Block Virus Fusion." Antimicrobial Agents and Chemotherapy 48, no. 11 (2004): 4349–59. http://dx.doi.org/10.1128/aac.48.11.4349-4359.2004.

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ABSTRACT A recently approved peptidic human immunodeficiency virus type 1 (HIV-1) fusion inhibitor, T-20 (Fuzeon; Trimeris Inc.), has shown significant promise in clinical application for treating HIV-1-infected individuals who have failed to respond to the currently available antiretroviral drugs. However, T-20 must be injected twice daily and is too expensive. Therefore, it is essential to develop orally available small molecule HIV-1 fusion inhibitors. By screening a chemical library consisting of “drug-like” compounds, we identified two N-substituted pyrroles, designated NB-2 and NB-64, th

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Xu, Ling, Chao Wang, Wei Xu, et al. "A dePEGylated Lipopeptide-Based Pan-Coronavirus Fusion Inhibitor Exhibits Potent and Broad-Spectrum Anti-HIV-1 Activity without Eliciting Anti-PEG Antibodies." International Journal of Molecular Sciences 24, no. 11 (2023): 9779. http://dx.doi.org/10.3390/ijms24119779.

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We previously identified a lipopeptide, EK1C4, by linking cholesterol to EK1, a pan-CoV fusion inhibitory peptide via a polyethylene glycol (PEG) linker, which showed potent pan-CoV fusion inhibitory activity. However, PEG can elicit antibodies to PEG in vivo, which will attenuate its antiviral activity. Therefore, we designed and synthesized a dePEGylated lipopeptide, EKL1C, by replacing the PEG linker in EK1C4 with a short peptide. Similar to EK1C4, EKL1C displayed potent inhibitory activity against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and other coronaviruses. In this

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McFadden, Karyn, Patricia Fletcher, Fiorella Rossi, et al. "Antiviral Breadth and Combination Potential of Peptide Triazole HIV-1 Entry Inhibitors." Antimicrobial Agents and Chemotherapy 56, no. 2 (2011): 1073–80. http://dx.doi.org/10.1128/aac.05555-11.

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ABSTRACTThe first stage of human immunodeficiency virus type 1 (HIV-1) infection involves the fusion of viral and host cellular membranes mediated by viral envelope glycoprotein gp120. Inhibitors that specifically target gp120 are gaining increased attention as therapeutics or preventatives to prevent the spread of HIV-1. One promising new group of inhibitors is the peptide triazoles, which bind to gp120 and simultaneously block its interaction with both CD4 and the coreceptor. In this study, we assessed the most potent peptide triazole, HNG-156, for inhibitory breadth, cytotoxicity, and effic

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Greenberg, M. L. "Resistance to enfuvirtide, the first HIV fusion inhibitor." Journal of Antimicrobial Chemotherapy 54, no. 2 (2004): 333–40. http://dx.doi.org/10.1093/jac/dkh330.

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Lin, P. F., H. Samanta, C. M. Bechtold, et al. "Characterization of siamycin I, an HIV fusion inhibitor." Antiviral Research 26, no. 3 (1995): A260. http://dx.doi.org/10.1016/0166-3542(95)94762-q.

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35

Stoddart, Cheryl A., Geneviève Nault, Sofiya A. Galkina, et al. "Albumin-conjugated C34 Peptide HIV-1 Fusion Inhibitor." Journal of Biological Chemistry 283, no. 49 (2008): 34045–52. http://dx.doi.org/10.1074/jbc.m805536200.

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36

Wang, Haiyan, Benoit Gallet, Christine Moriscot, et al. "An Inducible ESCRT-III Inhibition Tool to Control HIV-1 Budding." Viruses 15, no. 12 (2023): 2289. http://dx.doi.org/10.3390/v15122289.

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HIV-1 budding as well as many other cellular processes require the Endosomal Sorting Complex Required for Transport (ESCRT) machinery. Understanding the architecture of the native ESCRT-III complex at HIV-1 budding sites is limited due to spatial resolution and transient ESCRT-III recruitment. Here, we developed a drug-inducible transient HIV-1 budding inhibitory tool to enhance the ESCRT-III lifetime at budding sites. We generated autocleavable CHMP2A, CHMP3, and CHMP4B fusion proteins with the hepatitis C virus NS3 protease. We characterized the CHMP-NS3 fusion proteins in the absence and pr

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Chinnadurai, Raghavan, Devi Rajan, Jan Münch, and Frank Kirchhoff. "Human Immunodeficiency Virus Type 1 Variants Resistant to First- and Second-Version Fusion Inhibitors and Cytopathic in Ex Vivo Human Lymphoid Tissue." Journal of Virology 81, no. 12 (2007): 6563–72. http://dx.doi.org/10.1128/jvi.02546-06.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) fusion inhibitors blocking viral entry by binding the gp41 heptad repeat 1 (HR1) region offer great promise for antiretroviral therapy, and the first of these inhibitors, T20 (Fuzeon; enfuvirtide), is successfully used in the clinic. It has been reported previously that changes in the 3-amino-acid GIV motif at positions 36 to 38 of gp41 HR1 mediate resistance to T20 but usually not to second-version fusion inhibitors, such as T1249, which target an overlapping but distinct region in HR1 including a conserved hydrophobic pocket (HP). Based on

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Welch, Brett D., J. Nicholas Francis, Joseph S. Redman, et al. "Design of a Potent d-Peptide HIV-1 Entry Inhibitor with a Strong Barrier to Resistance." Journal of Virology 84, no. 21 (2010): 11235–44. http://dx.doi.org/10.1128/jvi.01339-10.

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ABSTRACT The HIV gp41 N-trimer pocket region is an ideal viral target because it is extracellular, highly conserved, and essential for viral entry. Here, we report on the design of a pocket-specific d-peptide, PIE12-trimer, that is extraordinarily elusive to resistance and characterize its inhibitory and structural properties. d-Peptides (peptides composed of d-amino acids) are promising therapeutic agents due to their insensitivity to protease degradation. PIE12-trimer was designed using structure-guided mirror-image phage display and linker optimization and is the first d-peptide HIV entry i

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Smith, Elizabeth B., Robert A. Ogert, David Pechter, et al. "HIV Cell Fusion Assay." Journal of Biomolecular Screening 19, no. 1 (2013): 108–18. http://dx.doi.org/10.1177/1087057113500074.

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The health and disease-related biology of the CXCR4 chemokine receptor presents the challenge of finding a small molecule that can bind CXCR4 and block T-cell tropic human immunodeficiency virus type 1 (HIV-1) cell entry, while preserving the ability of CXCR4 to respond to its native ligand, CXCL12. HIV entry into the host cell involves the interaction of the viral envelope glycoprotein gp120 binding to CD4, followed by a rearrangement in gp120, and subsequent interaction with the chemokine receptor CXCR4 or CCR5. These initial events can be re-created in a cell fusion assay that represents a

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Song, Kunzhong, Ju Bao, Yueming Sun, and John Z. H. Zhang. "Binding ofN-substituted pyrrole derivatives to HIV-1 gp41." Journal of Theoretical and Computational Chemistry 13, no. 02 (2014): 1450018. http://dx.doi.org/10.1142/s0219633614500187.

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Developing small molecule inhibitors of human immunodeficiency virus type 1 (HIV-1) fusion has attracted significant interest. Recently, Jiang have reported several natural and synthetic N -substituted pyrrole derivatives targeting gp41 that are experimentally shown to inhibit cell–cell fusion in the low micromolar range. In order to help gain insight on the binding mechanism, we carried out computational study to help identify possible binding modes and to characterize structures of binding complexes. Detailed gp41-molecule binding interactions and free energies of binding are obtained throug

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Nsanzabana, Christian, and Philip J. Rosenthal. "In VitroActivity of Antiretroviral Drugs against Plasmodium falciparum." Antimicrobial Agents and Chemotherapy 55, no. 11 (2011): 5073–77. http://dx.doi.org/10.1128/aac.05130-11.

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ABSTRACTMalaria and HIV infection are both very common in many developing countries. With the increasing availability of therapy for HIV infection, it was of interest to determine whether antiretroviral drugs exert antimalarial effects. We therefore tested thein vitroactivity of 19 antiretroviral drugs against the W2 and 3D7 strains ofPlasmodium falciparumat concentrations up to 50 μM. None of 5 tested nucleoside reverse transcriptase inhibitors demonstrated activity. Two nonnucleoside reverse transcriptase inhibitors, efavirenz (mean 50% inhibitory concentration [IC50] of 22 to 30 μM against

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Giroud, Charline, Mariana Marin, Jason Hammonds, Paul Spearman, and Gregory B. Melikyan. "P2X1 Receptor Antagonists Inhibit HIV-1 Fusion by Blocking Virus-Coreceptor Interactions." Journal of Virology 89, no. 18 (2015): 9368–82. http://dx.doi.org/10.1128/jvi.01178-15.

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ABSTRACTHIV-1 Env glycoprotein-mediated fusion is initiated upon sequential binding of Env to CD4 and the coreceptor CXCR4 or CCR5. Whereas these interactions are thought to be necessary and sufficient to promote HIV-1 fusion, other host factors can modulate this process. Previous studies reported potent inhibition of HIV-1 fusion by selective P2X1 receptor antagonists, including NF279, and suggested that these receptors play a role in HIV-1 entry. Here we investigated the mechanism of antiviral activity of NF279 and found that this compound does not inhibit HIV-1 fusion by preventing the acti

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Wei, Bangdong L., Paul W. Denton, Eduardo O'Neill, Tianci Luo, John L. Foster, and J. Victor Garcia. "Inhibition of Lysosome and Proteasome Function Enhances Human Immunodeficiency Virus Type 1 Infection." Journal of Virology 79, no. 9 (2005): 5705–12. http://dx.doi.org/10.1128/jvi.79.9.5705-5712.2005.

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ABSTRACT We previously reported that inhibition of endosomal/lysosomal function can dramatically enhance human immunodeficiency virus type 1 (HIV-1) infectivity, suggesting that under these conditions productive HIV-1 infection can occur via the endocytic pathway. Here we further examined this effect with bafilomycin A1 (BFLA-1) and show that this enhancement of infectivity extends to all HIV-1 isolates tested regardless of coreceptor usage. However, isolate-specific differences were observed in the magnitude of the effect. This was particularly evident in the case of the weakly infectious HIV

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Latinovic, Olga, Janaki Kuruppu, Charles Davis, Nhut Le, and Alonso Heredia. "Pharmacotherapy of HIV-1 Infection: Focus on CCR5 Antagonist Maraviroc." Clinical Medicine. Therapeutics 1 (January 2009): CMT.S2365. http://dx.doi.org/10.4137/cmt.s2365.

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Sustained inhibition of HIV-1, the goal of antiretroviral therapy, is often impeded by the emergence of viral drug resistance. For patients infected with HIV-1 resistant to conventional drugs from the viral reverse transcriptase and protease inhibitor classes, the recently approved entry and integration inhibitors effectively suppress HIV-1 and offer additional therapeutic options. Entry inhibitors are particularly attractive because, unlike conventional antiretrovirals, they target HIV-1 extracellularly, thereby sparing cells from both viral- and drug-induced toxicities. The fusion inhibitor

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Visseaux, Benoit, Charlotte Charpentier, Margarita Hurtado-Nedelec, et al. "In VitroPhenotypic Susceptibility of HIV-2 Clinical Isolates to CCR5 Inhibitors." Antimicrobial Agents and Chemotherapy 56, no. 1 (2011): 137–39. http://dx.doi.org/10.1128/aac.05313-11.

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ABSTRACTHIV-2 is naturally resistant to nonnucleoside reverse transcriptase inhibitors, to a fusion inhibitor, and to some of the protease inhibitors. Maraviroc is the first drug of the new anti-CCR5 drug class and is effective only on CCR5-tropic (R5) HIV-1. No previous studies concerning HIV-2 susceptibility to maraviroc have been reported yet. We developed a phenotypic maraviroc susceptibility test using a peripheral blood mononuclear cell (PBMC) model. We analyzed the maraviroc susceptibility of 13 R5 HIV-2, 2 X4R5 (dual) HIV-2, and 2 CXCR4-tropic (X4) HIV-2 clinical isolates. We also test

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Jamjian, M. Christine, and Ian R. McNicholl. "Enfuvirtide: first fusion inhibitor for treatment of HIV infection." American Journal of Health-System Pharmacy 61, no. 12 (2004): 1242–47. http://dx.doi.org/10.1093/ajhp/61.12.1242.

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Golding, Hana, Julio Aliberti, Lisa R. King, et al. "Inhibition of HIV-1 infection by a CCR5-binding cyclophilin from Toxoplasma gondii." Blood 102, no. 9 (2003): 3280–86. http://dx.doi.org/10.1182/blood-2003-04-1096.

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AbstractThe activation of murine dendritic cells by Toxoplasma gondii has recently been shown to depend on a parasite protein that signals through the chemokine receptor CCR5. Here we demonstrate that this molecule, cyclophilin-18 (C-18), is an inhibitor of HIV-1 cell fusion and infection with cell-free virus. T gondii C-18 efficiently blocked syncytium formation between human T cells and effector cells expressing R5 but not X4 envelopes. Neither human nor Plasmodium falciparum cyclophilins possess such inhibitory activity. Importantly, C-18 protected peripheral blood leukocytes from infection

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Murray, Edward J., Daniel P. Leaman, Nishant Pawa, et al. "A Low-Molecular-Weight Entry Inhibitor of both CCR5- and CXCR4-Tropic Strains of Human Immunodeficiency Virus Type 1 Targets a Novel Site on gp41." Journal of Virology 84, no. 14 (2010): 7288–99. http://dx.doi.org/10.1128/jvi.00535-10.

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ABSTRACT A low-molecular-weight human immunodeficiency virus type 1 (HIV-1) inhibitor, PF-68742 (molecular weight, 573), has been identified in a high-throughput screen for compounds that block HIV-1 envelope glycoprotein (Env)-mediated fusion. The compound is shown to be potent against R5 and X4 isolates in both cell-cell fusion and antiviral assays (50% effective concentrations of ∼0.1 to 1 μM). Postfusion and HIV-1 pseudotyping control experiments confirm that PF-68742 is an entry inhibitor with Env as the specific target for antiviral action. PF-68742 was not able to block binding of monom

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Wang, Chen, Shuihong Cheng, Yuanyuan Zhang, et al. "Long-Acting HIV-1 Fusion Inhibitory Peptides and their Mechanisms of Action." Viruses 11, no. 9 (2019): 811. http://dx.doi.org/10.3390/v11090811.

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The clinical application of HIV fusion inhibitor, enfuvirtide (T20), was limited mainly because of its short half-life. Here we designed and synthesized two PEGylated C34 peptides, PEG2kC34 and PEG5kC34, with the PEG chain length of 2 and 5 kDa, respectively, and evaluated their anti-HIV-1 activity and mechanisms of action. We found that these two PEGylated peptides could bind to the HIV-1 peptide N36 to form high affinity complexes with high α-helicity. The peptides PEG2kC34 and PEG5kC34 effectively inhibited HIV-1 Env-mediated cell–cell fusion with an effective concentration for 50% inhibiti

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Zhou, Guangyan, Li He, Kathy H. Li, Cássio C. S. Pedroso, and Miriam Gochin. "A targeted covalent small molecule inhibitor of HIV-1 fusion." Chemical Communications 57, no. 37 (2021): 4528–31. http://dx.doi.org/10.1039/d1cc01013a.

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