Interaction of human immunodeficiency virus-1 and human immunodeficiency virus-2 capsid amino acid variants with human tripartite motif 5α protein SPRY domain and its association with pathogenesis

Autor: Susanne Pulimood, Balaji Nandagopal, G. John Fletcher, Priscilla Rupali, George M. Varghese, Lakshmanan Jeyaseelan, Rajesh Kannangai, Veena Vadhini Ramalingam, Gopalan Sridharan, Suganya Subramanian
Jazyk: angličtina
Rok vydání: 2019
Předmět:
0301 basic medicine
Microbiology (medical)
Sequence analysis
viruses
Ubiquitin-Protein Ligases
030106 microbiology
Immunology
Human immunodeficiency virus (HIV)
lcsh:QR1-502
Single-nucleotide polymorphism
HIV Infections
Biology
medicine.disease_cause
Microbiology
Polymorphism
Single Nucleotide
lcsh:Microbiology
Pathogenesis
Antiviral Restriction Factors
Tripartite Motif Proteins
03 medical and health sciences
0302 clinical medicine
human tripartite motif 5α protein
Immunology and Microbiology (miscellaneous)
medicine
Immunology and Allergy
Humans
030212 general & internal medicine
Amino Acids
chemistry.chemical_classification
General Immunology and Microbiology
virus diseases
human immunodeficiency virus-2
Group-specific antigen
Virology
human immunodeficiency virus-1
Amino acid
molecular modelling
Molecular Docking Simulation
Infectious Diseases
Cross-Sectional Studies
chemistry
Capsid
Docking (molecular)
HIV-2
docking
HIV-1
Capsid Proteins
Zdroj: Indian Journal of Medical Microbiology, Vol 37, Iss 4, Pp 574-583 (2019)
ISSN: 1998-3646
0255-0857
Popis: Purpose: The sequence variation of human immunodeficiency virus (HIV) capsid region may influence and alter the susceptibility to human tripartite motif 5α protein (huTRIM5α). Materials and Methods: Molecular docking was carried out with huTRIM5α SPRY domain by the use of ClusPro and Hex docking program for HIV-1 and HIV-2 capsid sequences. Results: The sequence analysis on HIV-1 and HIV-2 capsid gag gene identified 35 (19.7%) single-nucleotide polymorphisms (SNPs) in HIV-1 and 8 (4.5%) SNPs in HIV-2. The variations observed in the HIV-2 capsid region were significantly lower than HIV-1 (P < 0.001). The molecular docking analysis showed that HIV-1 wild type used V1 loop, while HIV-2 used V3 loop of huTRIM5α for interaction. HIV-1 with A116T SNP and HIV-2 with V81A SNP use V3 and V1 loop of huTRIM5α for interaction respectively. The reduced huTRIM5α inhibition may lead to a faster progression of disease among HIV-1-infected individuals. However, in case of HIV-2, increased inhibition by huTRIM5α slows down the disease progression. Conclusion: Polymorphisms in the capsid protein with both HIV-1- and HIV-2-monoinfected individuals showed the difference in the docking energy from the wild type. This is the first study which documents the difference in the usage of loop between the two HIV types for interaction with huTRIM5α. Variations in the capsid protein result in alteration in the binding to the restriction factor huTRIM5α.
Databáze: OpenAIRE
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