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 HIV mutation literature information.


  Molecular basis for reduced cleavage activity and drug resistance in D30N HIV-1 protease.
 PMID: 17209774       2006       AIDS research and human retroviruses
Abstract: First, D30N was positively associated with N88D but negatively associated with N88S.
Abstract: In 16 patients having isolates with more than one combination of mutations at positions 30, 88, and 90, all exhibited one of the steps in the following progression: D30N-->D30N+N88D-->D30N+N88D+L90M-->D30N+N88D+L90M+(L33F+/-I84V or M46I/L+/-I54V).
Abstract: Second, D30N and L90M were negatively associated except in the presence of N88D<


  Compensatory mutations at the HIV cleavage sites p7/p1 and p1/p6-gag in therapy-naive and therapy-experienced patients.
 PMID: 17302250       2006       Antiviral therapy
Abstract: The analysis of CS and PR mutations in therapy-experienced viruses revealed several positive correlations--A431V with L24I-M46I/L-I54V-V82A; I437V with I54V-V82F/T/S; L449V with I54M/L/S/T/A; and L449F/R452S/P453L: with D30N-I84V--whereas P453L and V82A were negatively correlated.


  Novel human immunodeficiency virus type 1 protease mutations potentially involved in resistance to protease inhibitors.
 PMID: 15855527       2005       Antimicrobial agents and chemotherapy
Abstract: K45R and K20T, which were associated with nelfinavir treatment, were specifically associated with D30N and N88D and with L90M, respectively.


  Diverse pattern of protease inhibitor resistance mutations in HIV-1 infected patients failing nelfinavir.
 PMID: 15977242       2005       Journal of medical virology
Abstract: A surprisingly diverse pattern of primary PI mutations was seen: M46I (n=7), D30N (n=6), L90M (n=5), and V82A (n=4).
Abstract: The diverse pattern of the evolved PI-mutations and the relative low occurrence of the D30N mutation in the material was unexpected and did not seem to be related to the viral subtype.


  Treatment response and drug resistance in patients infected with HIV type 1 group O viruses.
 PMID: 16060830       2005       AIDS research and human retroviruses
Abstract: Another selected mutations K70N, V75A, and M184V at the RT, and D30D/N and I84V at the protease while failing on indinavir.


  Nelfinavir: a review of its use in the management of HIV infection.
 PMID: 16225378       2005       Drugs
Abstract: Resistance to nelfinavir may develop, but the most common mutation (D30N, appearing mainly in HIV-1 subtype B) does not confer resistance to other protease inhibitors, thereby conserving these agents for later use.


  HIV-1 genotypes related to failure of nelfinavir as the first protease inhibitor treatment.
 PMID: 16270125       2005       The Brazilian journal of infectious diseases
Abstract: Failure with nelfinavir has been associated with two protease gene mutations, D30N and L90M.
Abstract: In the tests for protease gene mutations, the D30N mutation was found in 57%, L90M in 18% and the wild-type virus in 25%.
Abstract: The D30N mutation does not result in cross-resistance with other protease inhibitors, and it decreases viral fitness.


  Resistant mechanism against nelfinavir of human immunodeficiency virus type 1 proteases.
 PMID: 16851048       2005       The journal of physical chemistry. B
Abstract: D30N mutation causes the disappearance of the hydrogen bond between the m-phenol group of NFV and the 30th residue.
Abstract: Among patients who failed in the inhibitor nelfinavir (NFV) treatment, D30N, N88D, and L90M mutations of HIV-1 protease are often observed.
Abstract: In this study, we executed molecular dynamics simulations of the NFV-bound proteases in the wild-type and D30N, N88D, D30N/N88D, and L90M mutants.


  Substitutions in the Reverse Transcriptase and Protease Genes of HIV-1 Subtype B in Untreated Individuals and Patients Treated With Antiretroviral Drugs.
 PMID: 19825125       2005       Journal of the International AIDS Society
Result: In contrast, only 14.7% harbored D30N and 11.7% harbored M46I, both of which result from a G A transition.


  Molecular Dynamics Simulations of HIV-1 Protease Suggest Different Mechanisms Contributing to Drug Resistance.
 PMID: 26641303       2005       Journal of chemical theory and computation
Abstract: A decreased interaction energy between protease and Nelfinavir was observed for the D30N mutant giving a plausible explanation for resistance, while the N88S mutation did not significantly affect the interaction energies in the bound form.
Abstract: In the present work molecular dynamics simulations of an active-site mutation (D30N) and a nonactive-site mutation (N88S) of HIV-1 protease that both directly confer resistance to the protease inhibitor Nelfinavir but not to Amprenavir were performed and compared to wild-type HIV-protease.



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