Natural polymorphisms of HIV-1 subtype-C integrase coding region in a large group of ARV-naïve infected individuals

S. Dimonte; M. Babakir-Mina; S. Aquaro; C. F. Perno

doi:10.1007/s15010-013-0464-5

Natural polymorphisms of HIV-1 subtype-C integrase coding region in a large group of ARV-naïve infected individuals

S. Dimonte, M. Babakir-Mina, S. Aquaro, C. F. Perno

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

Research output: Contribution to journal › Article › peer-review

Abstract

Purpose: Integrase (IN) is an enzyme produced by human immunodeficiency virus (HIV)-1 that enables its genetic material to be integrated into the DNA of the infected cell. Still now, few data are available with detailed analysis of the natural IN polymorphisms of HIV-1 subtype-C in datasets retrieved from antiretroviral-naïve patients; this study focuses on these polymorphisms. Methods: The analysis included 335 HIV-1 subtype-C IN sequences (one per patient). Multi-alignment of IN sequences was performed, and for the definition of a polymorphism, only amino acid changes with prevalence ≥3 % among treatment-naïve patients were considered. Results: Seventy IN amino acid positions were fully conserved. Differently, forty-six IN amino acid polymorphic positions were observed, 12 within the N-terminal domain and 13 within the C-terminal domain. In the DDE-catalytic motif, only one mutation per site (D64G/D116G/E152K) was found, while a low variability (

Original language	English
Pages (from-to)	1097-1102
Number of pages	6
Journal	Infection
Volume	41
Issue number	6
DOIs	https://doi.org/10.1007/s15010-013-0464-5
Publication status	Published - Dec 2013

Keywords

Drug resistance
HIV
Integrase inhibitors
Polymorphism
Prevalence
Subtype-C

ASJC Scopus subject areas

Microbiology (medical)
Infectious Diseases

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10.1007/s15010-013-0464-5

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title = "Natural polymorphisms of HIV-1 subtype-C integrase coding region in a large group of ARV-na{\"i}ve infected individuals",

abstract = "Purpose: Integrase (IN) is an enzyme produced by human immunodeficiency virus (HIV)-1 that enables its genetic material to be integrated into the DNA of the infected cell. Still now, few data are available with detailed analysis of the natural IN polymorphisms of HIV-1 subtype-C in datasets retrieved from antiretroviral-na{\"i}ve patients; this study focuses on these polymorphisms. Methods: The analysis included 335 HIV-1 subtype-C IN sequences (one per patient). Multi-alignment of IN sequences was performed, and for the definition of a polymorphism, only amino acid changes with prevalence ≥3 % among treatment-na{\"i}ve patients were considered. Results: Seventy IN amino acid positions were fully conserved. Differently, forty-six IN amino acid polymorphic positions were observed, 12 within the N-terminal domain and 13 within the C-terminal domain. In the DDE-catalytic motif, only one mutation per site (D64G/D116G/E152K) was found, while a low variability (",

keywords = "Drug resistance, HIV, Integrase inhibitors, Polymorphism, Prevalence, Subtype-C",

author = "S. Dimonte and M. Babakir-Mina and S. Aquaro and Perno, {C. F.}",

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AU - Dimonte, S.

AU - Babakir-Mina, M.

AU - Aquaro, S.

AU - Perno, C. F.

PY - 2013/12

Y1 - 2013/12

N2 - Purpose: Integrase (IN) is an enzyme produced by human immunodeficiency virus (HIV)-1 that enables its genetic material to be integrated into the DNA of the infected cell. Still now, few data are available with detailed analysis of the natural IN polymorphisms of HIV-1 subtype-C in datasets retrieved from antiretroviral-naïve patients; this study focuses on these polymorphisms. Methods: The analysis included 335 HIV-1 subtype-C IN sequences (one per patient). Multi-alignment of IN sequences was performed, and for the definition of a polymorphism, only amino acid changes with prevalence ≥3 % among treatment-naïve patients were considered. Results: Seventy IN amino acid positions were fully conserved. Differently, forty-six IN amino acid polymorphic positions were observed, 12 within the N-terminal domain and 13 within the C-terminal domain. In the DDE-catalytic motif, only one mutation per site (D64G/D116G/E152K) was found, while a low variability (

AB - Purpose: Integrase (IN) is an enzyme produced by human immunodeficiency virus (HIV)-1 that enables its genetic material to be integrated into the DNA of the infected cell. Still now, few data are available with detailed analysis of the natural IN polymorphisms of HIV-1 subtype-C in datasets retrieved from antiretroviral-naïve patients; this study focuses on these polymorphisms. Methods: The analysis included 335 HIV-1 subtype-C IN sequences (one per patient). Multi-alignment of IN sequences was performed, and for the definition of a polymorphism, only amino acid changes with prevalence ≥3 % among treatment-naïve patients were considered. Results: Seventy IN amino acid positions were fully conserved. Differently, forty-six IN amino acid polymorphic positions were observed, 12 within the N-terminal domain and 13 within the C-terminal domain. In the DDE-catalytic motif, only one mutation per site (D64G/D116G/E152K) was found, while a low variability (

KW - Drug resistance

KW - HIV

KW - Integrase inhibitors

KW - Polymorphism

KW - Prevalence

KW - Subtype-C

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Natural polymorphisms of HIV-1 subtype-C integrase coding region in a large group of ARV-naïve infected individuals

Abstract

Keywords

ASJC Scopus subject areas

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