Abstract: One major DRM (L44 M), many secondary DRMs (including N126 K, E137 K, S138A), and lots of polymorphisms were found in the study, which have been proved to elevate resistance to ENF.
Structural and Functional Characterization of the Secondary Mutation N126K Selected by Various HIV-1 Fusion Inhibitors.
Abstract: Fifth, we determined the crystal structure of a 6-HB bearing the N126K mutation, which revealed the interhelical and intrahelical interactions underlying the increased thermostability.
Abstract: First, we show that a single N126K mutation across several HIV-1 isolates conferred mild to moderate cross-resistances.
Abstract: Fourth, the N126K mutation was verified to enhance the thermal stability of 6-HB conformation.
Abstract: In this study, the functional and structural relevance of the N126K mutation has been characterized from multiple angles.
Abstract: Second, the N126K mutation exerted different effects on Env-mediated HIV-1 entry and cell-cell fusion.
Abstract: The resistance profiles of various HIV-1 fusion inhibitors were previous
Molecular mechanism of HIV-1 resistance to sifuvirtide, a clinical trial-approved membrane fusion inhibitor.
PMID: 29929981
2018
The Journal of biological chemistry
Abstract: Three primary substitutions (V38A, A47I, and Q52R) located at the inhibitor-binding site of HIV-1's envelope protein (Env) and one secondary substitution (N126K) located at the C-terminal heptad repeat region of the viral protein gp41, which is part of the envelope, conferred high SFT resistance and cross-resistance to the anti-HIV-1 drug T20 and the template peptide C34.
Mechanism of HIV-1 Resistance to an Electronically Constrained alpha-Helical Peptide Membrane Fusion Inhibitor.
Abstract: Three mutant viruses, which possessed two (N43K/E49A) or three (Q39R/N43K/N126K and N43K/E49A/N126K) amino acid substitutions in the N- and C-terminal repeat regions of gp41 were identified as conferring high resistance to SC29EK and cross-resistance to the first-generation (T20 and C34) and newly designed (sifuvirtide, MT-SC29EK, and 2P23) fusion inhibitors.
Adding an Artificial Tail-Anchor to a Peptide-Based HIV-1 Fusion Inhibitor for Improvement of Its Potency and Resistance Profile.
Discussion: For example, substitution N126K in the gp41 CHR domain has been reported to cause resistance to several HIV-1 drugs.
Discussion: Here, we found that HP23-E6-IDL could still inhibit HIV-1 variants with N126K, Q79E/N126K, K90E/N126K, E49K/N126K, and D36G/E49K/N126K mutations, proving its high affinity to the prehairpin intermediate of gp41.
Enhanced antibody-mediated neutralization of HIV-1 variants that are resistant to fusion inhibitors.
Abstract: In this study, the HIV-1 mutants resistant to MTSC22 were selected and characterized, which revealed that the E49K and L57R substitutions at the inhibitor-binding site and the N126K and E136G substitutions at the C-terminal heptad repeat region of gp41 critically determine the resistance phenotype.
Abstract: Two mutations (E49K and L57R) located at the inhibitor-binding site and two mutations (N126K and E136G) located at the C-terminal heptad repeat region of gp41 were identified as conferring high resistance either singly or in combination.
Abstract: Unlike E49K and
Mechanism of HIV-1 Resistance to Short-Peptide Fusion Inhibitors Targeting the Gp41 Pocket.
Abstract: Two substitutions, E49K and N126K, located, respectively, at the N- and C-heptad repeat regions of gp41, were identified as conferring high resistance to the inhibitors targeting the pocket and cross-resistance to enfuvirtide (T20) and sifuvirtide (SFT).
Characterization of Gp41 polymorphisms in the fusion peptide domain and T-20 (Enfuvirtide) resistance-associated regions in Korean HIV-1 isolates.
PMID: 24616600
2014
Journal of Korean medical science
Abstract: Minor T-20 resistance mutations such as L45M (1.2%), N126K (1.2%), and E137K (6.7%) were detected, but the critical T-20 resistance mutations were not detected in the gp41 HR1 and HR2 regions.
Introduction: Recently, it has also been reported that T-20 resistance is greatly increased by a combined mutation of HR1 with secondary and/or compensatory mutations in the HR2 region (N126K, E137K, S138A).
Introduction: Several mutations (N126K, E137K, and S138A) in the HR2 domain contributed to enhanced viral fusion activity and reduced the susceptibility to T-20.
Introduction: The minor T-20 resistance mutations detected
Mechanism of resistance to S138A substituted enfuvirtide and its application to peptide design.
PMID: 23357451
2013
The international journal of biochemistry & cell biology
Abstract: We found that when starting with WT background, I37N and L44M emerged in the N-HR of gp41, and N126K in the C-HR.
Introduction: In this case, we designed a variant of C34 carrying a secondary escape mutation, N126K, selected for the induction of C34 resistance and also present in HIV-1 isolates from T-20 experienced patients.
Result: At P-60 (3.3 muM), L44M and N126K in the gp41 further emerged.
Result: C34E137K and C34E137K/S138A significantly suppressed all HIV-1 variants tested except for HIV-1I37N/L44M/N126K by C34E137K.
HIV mutation literature information.
PMID: 
2021
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