Chunfu Wang, Haichang Huang, Lourdes Valera, Kyle Parcella, Christiana Iwuagwu, Brian McAuliffe, Paul J Falk, Donald R O'Boyle Ii, Ronald E Rose, Ricardo Ramírez Padilla, Chunxiang Wu, Yong Xiong, John Kadow, Umesh Hanumegowda, Luca Sardo, Eric P Gillis, Mark Krystal, Robert A Fridell
{"title":"HIV-1衣壳抑制剂VH4004280和VH4011499的临床前病毒学分析","authors":"Chunfu Wang, Haichang Huang, Lourdes Valera, Kyle Parcella, Christiana Iwuagwu, Brian McAuliffe, Paul J Falk, Donald R O'Boyle Ii, Ronald E Rose, Ricardo Ramírez Padilla, Chunxiang Wu, Yong Xiong, John Kadow, Umesh Hanumegowda, Luca Sardo, Eric P Gillis, Mark Krystal, Robert A Fridell","doi":"10.1128/aac.00309-25","DOIUrl":null,"url":null,"abstract":"<p><p>With its high degree of conservation and critical role in multiple steps of the HIV-1 life cycle, the HIV-1 capsid protein presents an attractive therapeutic target. Herein, the virologic properties of the HIV-1 capsid inhibitors VH4004280 (VH-280) and VH4011499 (VH-499), including potency, mechanisms of action, and resistance profiles, are described. VH-280 and VH-499 inhibited panels of HIV-1 laboratory strains and viruses containing capsid sequences from clinical isolates with half-maximal effective concentrations in the picomolar range. Time-of-addition experiments determined that the primary block to HIV-1 replication occurred after nuclear import and before integration; however, measurements of replication intermediates by quantitative polymerase chain reaction, Gag degradation, p24 release, and virion morphology by cryo-electron microscopy indicate that VH-280 and VH-499 also block nuclear import, total reverse transcript production, integration, virion assembly, and maturation. <i>In vitro</i> resistance selection identified Q67H, A105E, T107D/N, and combinations of these substitutions as conferring 6- to >5,000-fold reductions in susceptibility to both compounds. Certain resistance-associated mutations selected by other capsid inhibitors also reduced susceptibility. Overall, the preclinical virology profiles and other drug-like properties support the potential of VH-280 and VH-499 as long-acting agents for HIV-1 treatment and prevention.</p>","PeriodicalId":8152,"journal":{"name":"Antimicrobial Agents and Chemotherapy","volume":" ","pages":"e0030925"},"PeriodicalIF":4.5000,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Preclinical virology profiles of the HIV-1 capsid inhibitors VH4004280 and VH4011499.\",\"authors\":\"Chunfu Wang, Haichang Huang, Lourdes Valera, Kyle Parcella, Christiana Iwuagwu, Brian McAuliffe, Paul J Falk, Donald R O'Boyle Ii, Ronald E Rose, Ricardo Ramírez Padilla, Chunxiang Wu, Yong Xiong, John Kadow, Umesh Hanumegowda, Luca Sardo, Eric P Gillis, Mark Krystal, Robert A Fridell\",\"doi\":\"10.1128/aac.00309-25\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>With its high degree of conservation and critical role in multiple steps of the HIV-1 life cycle, the HIV-1 capsid protein presents an attractive therapeutic target. Herein, the virologic properties of the HIV-1 capsid inhibitors VH4004280 (VH-280) and VH4011499 (VH-499), including potency, mechanisms of action, and resistance profiles, are described. VH-280 and VH-499 inhibited panels of HIV-1 laboratory strains and viruses containing capsid sequences from clinical isolates with half-maximal effective concentrations in the picomolar range. Time-of-addition experiments determined that the primary block to HIV-1 replication occurred after nuclear import and before integration; however, measurements of replication intermediates by quantitative polymerase chain reaction, Gag degradation, p24 release, and virion morphology by cryo-electron microscopy indicate that VH-280 and VH-499 also block nuclear import, total reverse transcript production, integration, virion assembly, and maturation. <i>In vitro</i> resistance selection identified Q67H, A105E, T107D/N, and combinations of these substitutions as conferring 6- to >5,000-fold reductions in susceptibility to both compounds. Certain resistance-associated mutations selected by other capsid inhibitors also reduced susceptibility. Overall, the preclinical virology profiles and other drug-like properties support the potential of VH-280 and VH-499 as long-acting agents for HIV-1 treatment and prevention.</p>\",\"PeriodicalId\":8152,\"journal\":{\"name\":\"Antimicrobial Agents and Chemotherapy\",\"volume\":\" \",\"pages\":\"e0030925\"},\"PeriodicalIF\":4.5000,\"publicationDate\":\"2025-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Antimicrobial Agents and Chemotherapy\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.1128/aac.00309-25\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2025/9/3 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q2\",\"JCRName\":\"MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Antimicrobial Agents and Chemotherapy","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1128/aac.00309-25","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/9/3 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
Preclinical virology profiles of the HIV-1 capsid inhibitors VH4004280 and VH4011499.
With its high degree of conservation and critical role in multiple steps of the HIV-1 life cycle, the HIV-1 capsid protein presents an attractive therapeutic target. Herein, the virologic properties of the HIV-1 capsid inhibitors VH4004280 (VH-280) and VH4011499 (VH-499), including potency, mechanisms of action, and resistance profiles, are described. VH-280 and VH-499 inhibited panels of HIV-1 laboratory strains and viruses containing capsid sequences from clinical isolates with half-maximal effective concentrations in the picomolar range. Time-of-addition experiments determined that the primary block to HIV-1 replication occurred after nuclear import and before integration; however, measurements of replication intermediates by quantitative polymerase chain reaction, Gag degradation, p24 release, and virion morphology by cryo-electron microscopy indicate that VH-280 and VH-499 also block nuclear import, total reverse transcript production, integration, virion assembly, and maturation. In vitro resistance selection identified Q67H, A105E, T107D/N, and combinations of these substitutions as conferring 6- to >5,000-fold reductions in susceptibility to both compounds. Certain resistance-associated mutations selected by other capsid inhibitors also reduced susceptibility. Overall, the preclinical virology profiles and other drug-like properties support the potential of VH-280 and VH-499 as long-acting agents for HIV-1 treatment and prevention.
期刊介绍:
Antimicrobial Agents and Chemotherapy (AAC) features interdisciplinary studies that build our understanding of the underlying mechanisms and therapeutic applications of antimicrobial and antiparasitic agents and chemotherapy.