Short Communication: Characterization of a New HIV-1 Group N Isolate Originating from a Cameroonian Patient

2018 ◽  
Vol 34 (7) ◽  
pp. 621-625
Author(s):  
Paul Alain Tagnouokam Ngoupo ◽  
Serge Alain Sadeuh-Mba ◽  
Fabienne De Oliveira ◽  
Elodie Téclaire Ngo-Malabo ◽  
Laure Ngono ◽  
...  
Keyword(s):  
Short Communication ◽  
Hiv 1

Characterization of HIV‐1 virus‐like particles and determination of Gag stoichiometry for different production platforms

2021 ◽  
Author(s):  
Jesús Lavado‐García ◽  
Inmaculada Jorge ◽  
Arnau Boix‐Besora ◽  
Jesús Vázquez ◽  
Francesc Gòdia ◽  
...  
Keyword(s):  
Virus Like Particles ◽  
Hiv 1

scholarly journals Development of a User-Friendly Pipeline for Mutational Analyses of HIV Using Ultra-Accurate Maximum-Depth Sequencing

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1338
Author(s):  
Morgan E. Meissner ◽  
Emily J. Julik ◽  
Jonathan P. Badalamenti ◽  
William G. Arndt ◽  
Lauren J. Mills ◽  
...  
Keyword(s):  
Error Rates ◽  
Maximum Depth ◽  
Sequencing Data ◽  
Background Error ◽  
High Background ◽  
Immunodeficiency Virus ◽  
User Friendly ◽  
Viral Mutagenesis ◽  
Hiv 1

Human immunodeficiency virus type 2 (HIV-2) accumulates fewer mutations during replication than HIV type 1 (HIV-1). Advanced studies of HIV-2 mutagenesis, however, have historically been confounded by high background error rates in traditional next-generation sequencing techniques. In this study, we describe the adaptation of the previously described maximum-depth sequencing (MDS) technique to studies of both HIV-1 and HIV-2 for the ultra-accurate characterization of viral mutagenesis. We also present the development of a user-friendly Galaxy workflow for the bioinformatic analyses of sequencing data generated using the MDS technique, designed to improve replicability and accessibility to molecular virologists. This adapted MDS technique and analysis pipeline were validated by comparisons with previously published analyses of the frequency and spectra of mutations in HIV-1 and HIV-2 and is readily expandable to studies of viral mutation across the genomes of both viruses. Using this novel sequencing pipeline, we observed that the background error rate was reduced 100-fold over standard Illumina error rates, and 10-fold over traditional unique molecular identifier (UMI)-based sequencing. This technical advancement will allow for the exploration of novel and previously unrecognized sources of viral mutagenesis in both HIV-1 and HIV-2, which will expand our understanding of retroviral diversity and evolution.

scholarly journals An extensive thermodynamic characterization of the dimerization domain of the HIV-1 capsid protein

2005 ◽  
Vol 14 (9) ◽  
pp. 2387-2404 ◽  
Author(s):  
María C. Lidón-Moya ◽  
Francisco N. Barrera ◽  
Marta Bueno ◽  
Raúl Pérez-Jiménez ◽  
Javier Sancho ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Dimerization Domain ◽  
Thermodynamic Characterization ◽  
Hiv 1

scholarly journals Characterization of a hepatitis C virus genotype 1 divergent isolate from an HIV-1 coinfected individual in Germany assigned to a new subtype 1o

2019 ◽  
Vol 16 (1) ◽  
Author(s):  
Bo Wang ◽  
Luise Krüger ◽  
Patrycja Machnowska ◽  
Amare Eshetu ◽  
Barbara Gunsenheimer-Bartmeyer ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Genotype 1 ◽  
Virus Genotype ◽  
Hiv 1

scholarly journals High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Betty Ha ◽  
Kevin P. Larsen ◽  
Jingji Zhang ◽  
Ziao Fu ◽  
Elizabeth Montabana ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Viral Entry ◽  
Reverse Transcription ◽  
Molecular Mechanisms ◽  
Dissociation Kinetics ◽  
Structural Mechanism ◽  
Medium Resolution ◽  
Kinetics Of ◽  
Hiv 1

AbstractReverse transcription of the HIV-1 viral RNA genome (vRNA) is an integral step in virus replication. Upon viral entry, HIV-1 reverse transcriptase (RT) initiates from a host tRNALys3 primer bound to the vRNA genome and is the target of key antivirals, such as non-nucleoside reverse transcriptase inhibitors (NNRTIs). Initiation proceeds slowly with discrete pausing events along the vRNA template. Despite prior medium-resolution structural characterization of reverse transcriptase initiation complexes (RTICs), higher-resolution structures of the RTIC are needed to understand the molecular mechanisms that underlie initiation. Here we report cryo-EM structures of the core RTIC, RTIC–nevirapine, and RTIC–efavirenz complexes at 2.8, 3.1, and 2.9 Å, respectively. In combination with biochemical studies, these data suggest a basis for rapid dissociation kinetics of RT from the vRNA–tRNALys3 initiation complex and reveal a specific structural mechanism of nucleic acid conformational stabilization during initiation. Finally, our results show that NNRTIs inhibit the RTIC and exacerbate discrete pausing during early reverse transcription.

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