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Basic Characteristics of Mutations
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Mutation Site
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T26S |
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Mutation Site Sentence
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A single sequence exhibited an active site mutation (T26S). |
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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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PR |
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Standardized Encoding Gene
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gag-pol
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Genotype/Subtype
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HIV-1 |
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Viral Reference
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-
|
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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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Location
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Mexica |
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Literature Information
|
|
PMID
|
31552748
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Title
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Mexican HIV-1 Protease Sequence Diversity
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Author
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Hernandez-Sanchez PG,Guerra-Palomares SE,Arguello JR,Noyola DE,Garcia-Sepulveda CA
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Journal
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AIDS research and human retroviruses
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Journal Info
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2020 Feb;36(2):161-166
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Abstract
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Protease is one of three enzymes encoded within HIV's pol gene, responsible for the cleavage of viral Gag-Pol polypeptide into mature viral proteins and a target of current anti-retroviral therapy. Protease diversity analysis in Latin America has been lacking in spite of extensive studies of protease-inhibitor resistance mutations. We studied the diversity of 777 Mexican protease sequences and found that all were subtype B except one (CRF02_AG). Phylogenetic analysis suggested the existence of six different clades with geospecific contributions. Thirty-three percent of sites were conserved, 25% had conservative substitutions, and 41% exhibited physicochemical changes. The most conserved regions surrounded the active site, most of the flap domain, and a region between the 60's loop and C-terminal triad. A single sequence exhibited an active site mutation (T26S). Variable sites were mapped to a crystallographic structure, providing further insight into the distribution and functional relevance of variable sites among Mexican isolates.
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Sequence Data
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KC168702.1
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