{"title":"Vpx 与 SAMHD1 之间的相互作用,对 SAMHD1 的抑制作用至关重要。","authors":"Zahra Hasanshahi, Behzad Dehghani, Ava Hashempour","doi":"10.1089/AID.2023.0052","DOIUrl":null,"url":null,"abstract":"<p><p>It was confirmed that the sterile alpha motif and HD domain 1 (<i>SAMHD1</i>) limits human immunodeficiency virus type 1 (HIV-1) replication. In contrast, viral protein x (<i>Vpx</i>) in HIV-2 and some simian immunodeficiency viruses can counteract this effect. The possible interaction between <i>SAMHD1</i> and <i>Vpx</i> was suggested by previous studies; however, there are no data to confirm this interaction. Therefore, this study aimed to study the interaction between two proteins and the properties of <i>Vpx</i> protein for the first time using bioinformatic tools. <i>Vpx</i> and <i>SAMHD1</i> sequences were obtained from the National Center for Biotechnology Information GenBank. Several software were used to define <i>Vpx</i> properties and the interaction between <i>Vpx</i> and different <i>SAMHD1</i> isoforms. Our findings indicated the difference in interaction sites among different <i>Vpx</i>. However, in all <i>Vpx</i> proteins, this region is from amino acids 4 to 90. In addition, two regions (26-31 and 134-139) and two amino acids 425 and 429 in <i>SAMHD1</i> are vital in the possible interaction. In addition, our analysis determined the physicochemical and immunological properties of the <i>Vpx</i>. Considering all factors, this study could confirm that <i>Vpx</i> interacts with <i>SAMHD1</i>, which could inhibit <i>SAMHD1</i>. Moreover, our findings can pave the way for future studies to express and purify <i>Vpx</i> in the laboratory and study this protein <i>in vitro</i>.</p>","PeriodicalId":7544,"journal":{"name":"AIDS research and human retroviruses","volume":" ","pages":"384-392"},"PeriodicalIF":1.5000,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Interaction Between <i>Vpx</i> and <i>SAMHD1</i>, Vital for <i>SAMHD1</i> Inhibition.\",\"authors\":\"Zahra Hasanshahi, Behzad Dehghani, Ava Hashempour\",\"doi\":\"10.1089/AID.2023.0052\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>It was confirmed that the sterile alpha motif and HD domain 1 (<i>SAMHD1</i>) limits human immunodeficiency virus type 1 (HIV-1) replication. In contrast, viral protein x (<i>Vpx</i>) in HIV-2 and some simian immunodeficiency viruses can counteract this effect. The possible interaction between <i>SAMHD1</i> and <i>Vpx</i> was suggested by previous studies; however, there are no data to confirm this interaction. Therefore, this study aimed to study the interaction between two proteins and the properties of <i>Vpx</i> protein for the first time using bioinformatic tools. <i>Vpx</i> and <i>SAMHD1</i> sequences were obtained from the National Center for Biotechnology Information GenBank. Several software were used to define <i>Vpx</i> properties and the interaction between <i>Vpx</i> and different <i>SAMHD1</i> isoforms. Our findings indicated the difference in interaction sites among different <i>Vpx</i>. However, in all <i>Vpx</i> proteins, this region is from amino acids 4 to 90. In addition, two regions (26-31 and 134-139) and two amino acids 425 and 429 in <i>SAMHD1</i> are vital in the possible interaction. In addition, our analysis determined the physicochemical and immunological properties of the <i>Vpx</i>. Considering all factors, this study could confirm that <i>Vpx</i> interacts with <i>SAMHD1</i>, which could inhibit <i>SAMHD1</i>. Moreover, our findings can pave the way for future studies to express and purify <i>Vpx</i> in the laboratory and study this protein <i>in vitro</i>.</p>\",\"PeriodicalId\":7544,\"journal\":{\"name\":\"AIDS research and human retroviruses\",\"volume\":\" \",\"pages\":\"384-392\"},\"PeriodicalIF\":1.5000,\"publicationDate\":\"2024-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"AIDS research and human retroviruses\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.1089/AID.2023.0052\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2023/12/26 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q4\",\"JCRName\":\"IMMUNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"AIDS research and human retroviruses","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1089/AID.2023.0052","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/12/26 0:00:00","PubModel":"Epub","JCR":"Q4","JCRName":"IMMUNOLOGY","Score":null,"Total":0}
Interaction Between Vpx and SAMHD1, Vital for SAMHD1 Inhibition.
It was confirmed that the sterile alpha motif and HD domain 1 (SAMHD1) limits human immunodeficiency virus type 1 (HIV-1) replication. In contrast, viral protein x (Vpx) in HIV-2 and some simian immunodeficiency viruses can counteract this effect. The possible interaction between SAMHD1 and Vpx was suggested by previous studies; however, there are no data to confirm this interaction. Therefore, this study aimed to study the interaction between two proteins and the properties of Vpx protein for the first time using bioinformatic tools. Vpx and SAMHD1 sequences were obtained from the National Center for Biotechnology Information GenBank. Several software were used to define Vpx properties and the interaction between Vpx and different SAMHD1 isoforms. Our findings indicated the difference in interaction sites among different Vpx. However, in all Vpx proteins, this region is from amino acids 4 to 90. In addition, two regions (26-31 and 134-139) and two amino acids 425 and 429 in SAMHD1 are vital in the possible interaction. In addition, our analysis determined the physicochemical and immunological properties of the Vpx. Considering all factors, this study could confirm that Vpx interacts with SAMHD1, which could inhibit SAMHD1. Moreover, our findings can pave the way for future studies to express and purify Vpx in the laboratory and study this protein in vitro.
期刊介绍:
AIDS Research and Human Retroviruses was the very first AIDS publication in the field over 30 years ago, and today it is still the critical resource advancing research in retroviruses, including AIDS. The Journal provides the broadest coverage from molecular biology to clinical studies and outcomes research, focusing on developments in prevention science, novel therapeutics, and immune-restorative approaches. Cutting-edge papers on the latest progress and research advances through clinical trials and examination of targeted antiretroviral agents lead to improvements in translational medicine for optimal treatment outcomes.
AIDS Research and Human Retroviruses coverage includes:
HIV cure research
HIV prevention science
- Vaccine research
- Systemic and Topical PreP
Molecular and cell biology of HIV and SIV
Developments in HIV pathogenesis and comorbidities
Molecular biology, immunology, and epidemiology of HTLV
Pharmacology of HIV therapy
Social and behavioral science
Rapid publication of emerging sequence information.