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Basic Characteristics of Mutations
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Mutation Site
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R189S |
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Mutation Site Sentence
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However, antibody responses to peptide 3b, which included all of the SGA-observed variants in segment 3, or peptide 3c, which included only 1 of the segment 3 mutations (Arg189eSer) resulted in approximately a 3-fold lower antibody response compared to the corresponding T/F 3a peptide (Figure 4b). |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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Env |
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Standardized Encoding Gene
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Env
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Genotype/Subtype
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HIV-1 |
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Viral Reference
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K03455.1
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Functional Impact and Mechanisms
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Disease
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HIV Infections
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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Thailand |
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Literature Information
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PMID
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31010245
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Title
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Humoral Response to the HIV-1 Envelope V2 Region in a Thai Early Acute Infection Cohort
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Author
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Trinh HV,Gohain N,Pham PT,Hamlin C,Song H,Sanders-Buell E,Bose M,Eller LA,Jain S,Uritskiy G,Rao VB,Tovanabutra S,Michael NL,Robb ML,Joyce MG,Rao M
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Journal
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Cells
|
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Journal Info
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2019 Apr 19;8(4):365
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Abstract
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Reduced risk of HIV-1 infection correlated with antibody responses to the envelope variable 1 and 2 regions in the RV144 vaccine trial. To understand the relationship between antibody responses, V2 sequence, and structure, plasma samples (n = 16) from an early acute HIV-1 infection cohort from Thailand infected with CRF01_AE strain were analyzed for binding to V2 peptides by surface plasmon resonance. Five participants with a range of V2 binding responses at week 24 post-infection were further analyzed against a set of four overlapping V2 peptides that were designed based on envelope single-genome amplification. Antibody responses that were relatively consistent over the four segments of the V2 region or a focused response to the C-strand (residues 165-186) of the V2 region were observed. Viral escape in the V2 region resulted in significantly reduced antibody binding. Structural modeling indicated that the C-strand and the sites of viral variation were highly accessible in the open conformation of the HIV-1 Env trimer. V2 residues, 165-186 are preferentially targeted during acute infection. Residues 169-184 were also preferentially targeted by the protective immune response in the RV144 trial, thus emphasizing the importance of these residues for vaccine design.
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Sequence Data
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MK656525-MK656857
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