Paper Details

  1. Home
  2. Paper Details

Energetic effects for observed and unobserved HIV-1 reverse transcriptase mutations of residues L100, V106, and Y181 in the presence of nevirapine and efavirenz.

Author: FranklinAmanda M, JorgensenWilliam L, RaderLenea H, SmithKatie D, SmithMarilyn B Kroeger, SmithRichard H, TaylorEmily V, Tirado-RivesJulian

Journal ArticleAn article published in an academic or professional journal that reports original research or scholarly analysis.
Research Support, N.I.H., ExtramuralResearch funding provided by the NIH to external research institutions and researchers.

Overview

This study investigated the effect of mutations on amino acid residues L100, V106, and Y181 for unbound HIV-1 reverse transcriptase (RT) and RT bound to nevirapine and efavirenz using Monte Carlo/free energy perturbation calculations. The results showed that the variant observed in patients dosed with either nevirapine or efavirenz binds the drug most weakly, suggesting it is the most effective of all possible codon change mutations.
Paper Details　
Original Abstract of the Article :
The effect of mutations on amino acid residues L100, V106, and Y181 for unbound HIV-1 reverse transcriptase (RT) and RT bound to nevirapine and efavirenz was investigated using Monte Carlo/free energy perturbation calculations. Using both native and bound crystal structures of RT, mutation of the am...See full text at original site
Dr.Camel IconDr.Camel's Paper Summary Blogラクダ博士について

ラクダ博士は、Health Journal が論文の内容を分かりやすく解説するために作成した架空のキャラクターです。
難解な医学論文を、専門知識のない方にも理解しやすいように、噛み砕いて説明することを目指しています。

* ラクダ博士による解説は、あくまで論文の要点をまとめたものであり、原論文の完全な代替となるものではありません。詳細な内容については、必ず原論文をご参照ください。
* ラクダ博士は架空のキャラクターであり、実際の医学研究者や医療従事者とは一切関係がありません。
* 解説の内容は Health Journal が独自に解釈・作成したものであり、原論文の著者または出版社の見解を反映するものではありません。


引用元：
https://pubmed.ncbi.nlm.nih.gov/18166457

データ提供：米国国立医学図書館（NLM）

HIV-1 Reverse Transcriptase: Understanding Drug Resistance Through Mutations

The fight against HIV-1 infection is a continuous battle, with the virus constantly evolving and adapting to antiviral therapies. This study delves into the intricate mechanisms of drug resistance, focusing on mutations within the HIV-1 reverse transcriptase (RT) enzyme, which plays a key role in viral replication.

Mapping the Desert of Drug Resistance

The study uses computational modeling to investigate how mutations in specific amino acid residues within RT can affect the enzyme's ability to bind to antiretroviral drugs, like nevirapine and efavirenz. The researchers discovered that mutations that are commonly observed in patients are those that reduce the enzyme's affinity for the drugs, leading to resistance.

Implications for HIV Treatment and Prevention

This study underscores the critical importance of understanding drug resistance mechanisms in HIV treatment. It highlights the need for regular monitoring of viral mutations and adapting treatment strategies accordingly. The findings can inform the development of novel antiretroviral drugs that are less susceptible to resistance, helping to ensure long-term success in the battle against HIV.

Dr.Camel's Conclusion

Just as a desert traveler must constantly adjust their course to navigate the shifting sands, researchers are constantly seeking new strategies to outmaneuver the ever-evolving HIV virus. This study provides valuable insights into the complex landscape of drug resistance, helping to guide future research and treatment strategies.
Date :
  1. Date Completed 2008-03-24
  2. Date Revised 2020-12-09
Further Info :

Pubmed ID

18166457

DOI: Digital Object Identifier

NIHMS211224

Related Literature

Article Analysis
・Effects of nevirapine
SNS
PICO Info
in preparation
Languages

English

Positive IndicatorAn AI analysis index that serves as a benchmark for how positive the results of the study are. Note that it is a benchmark and requires careful interpretation and consideration of different perspectives.

This site uses cookies. Visit our privacy policy page or click the link in any footer for more information and to change your preferences.