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- Title
Structural analysis and molecular dynamics simulation studies of HIV-1 antisense protein predict its potential role in HIV replication and pathogenesis.
- Authors
Sathiyamani, Balakumaran; Daniel, Evangeline Ann; Ansar, Samdani; Esakialraj, Bennett Henzeler; Hassan, Sameer; Revanasiddappa, Prasanna D.; Keshavamurthy, Amrutha; Roy, Sujata; Vetrivel, Umashankar; Hanna, Luke Elizabeth
- Abstract
The functional significance of the HIV-1 Antisense Protein (ASP) has been a paradox since its discovery. The expression of this protein in HIV-1-infected cells and its involvement in autophagy, transcriptional regulation, and viral latency have sporadically been reported in various studies. Yet, the definite role of this protein in HIV-1 infection remains unclear. Deciphering the 3D structure of HIV-1 ASP would throw light on its potential role in HIV lifecycle and host-virus interaction. Hence, using extensive molecular modeling and dynamics simulation for 200 ns, we predicted the plausible 3D-structures of ASP from two reference strains of HIV-1 namely, Indie-C1 (subtype-C) and NL4-3 (subtype-B) so as to derive its functional implication through structural domain analysis. In spite of sequence and structural differences in subtype B and C ASP, both structures appear to share common domains like the Von Willebrand Factor Domain-A (VWFA), Integrin subunit alpha-X (ITGSX), and ETV6-Transcriptional repressor, thereby reiterating the potential role of HIV-1 ASP in transcriptional repression and autophagy, as reported in earlier studies. Gromos-based cluster analysis of the centroid structures also reassured the accuracy of the prediction. This is the first study to elucidate a highly plausible structure for HIV-1 ASP which could serve as a feeder for further experimental validation studies.
- Subjects
ANTISENSE peptides; MOLECULAR dynamics; HIV; VON Willebrand factor; INTEGRINS; GENETIC transcription regulation; PROTEIN expression
- Publication
Frontiers in Microbiology, 2023, Vol 14, p1
- ISSN
1664-302X
- Publication type
Article
- DOI
10.3389/fmicb.2023.1152206