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Medical Sciences
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NeuroAIDS: Cognition, Immunology, Virology and Drug Abuse
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NeuroAIDS: Cognition, Immunology, Virology and Drug Abuse

A special issue of Medical Sciences (ISSN 2076-3271).

Deadline for manuscript submissions: closed (7 June 2019) | Viewed by 3454

Special Issue Editors

Assoc. Prof. Seetharaman Balaji, PhD

E-Mail Website
Guest Editor
Department of Biotechnology, Manipal Institute of Technology, Manipal Academy of Higher Education, Manipal-576104, Karnataka, India
Interests: Bioinformatics; Structural Biology; Biochemistry
Dr. Andrew Levine, PhD

E-Mail Website
Co-Guest Editor
Department of Neurology, David Geffen School of Medicine at the University of California Los Angeles, Los Angeles, CA, USA
Interests: clinical neuropsychology; NeuroAIDS; substance abuse; genetics/genomics
Dr. Pandjassarame Kangueane, PhD

E-Mail Website
Co-Guest Editor
Biomedical Informatics, Pondicherry, India
Interests: development of a peptide vaccine for HIV/AIDS; protein-protein interactions; peptide vaccine design

Special Issue Information

Dear Colleagues,

NeuroAIDS remains a major public health problem and is a major cause of death and disability globally. This Special Issue of Medical Sciences is being developed in order to provide an update on NeuroAIDS. We invite you to submit your research articles, short communications, or reviews, which include, but are not limited to the following NeuroAIDS topics: cognition, imaging, therapy, intervention, immunology, virology, opportunistic infections, drug abuse, pathophysiology, genetics, gene expression, animal models, and epidemiology.

Topics, authors, and brief abstracts should be submitted by the corresponding author at your earliest convenience. Manuscripts should be submitted before the deadline of 7 June 2019. 

We look forward to your contributions.

Sincerely,

Seetharaman Balaji, PhD
Mr. Andrew Levine, Ph.D.
Dr. Pandjassarame Kangueane, Ph.D.
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Medical Sciences is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) is waived for well-prepared manuscripts submitted to this issue in 2018. For manuscripts submitted in 2019, a fee of 350 CHF for accepted articles will apply. There will be no other associated publication charges for length, page number, graphics etc. English correction and/or formatting fees will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections. For further details see here.

Keywords

  • NeuroAIDS 
  • Cognition 
  • Imaging 
  • Therapy 
  • Interventions 
  • Immunology 
  • Virology 
  • Opportunistic infections 
  • Drug abuse 
  • Pathophysiology 
  • Genetics 
  • Gene expression 
  • Animal models 
  • Epidemiology

Published Papers (1 paper)

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Research

21 pages, 4283 KiB  
Article
In Silico Insights into HIV-1 Vpu-Tetherin Interactions and Its Mutational Counterparts
by Patil Sneha, Urmi Shah and Seetharaman Balaji
Med. Sci. 2019, 7(6), 74; https://doi.org/10.3390/medsci7060074 - 22 Jun 2019
Viewed by 3078
Abstract
Tetherin, an interferon-induced host protein encoded by the bone marrow stromal antigen 2 (BST2/CD317/HM1.24) gene, is involved in obstructing the release of many retroviruses and other enveloped viruses by cross-linking the budding virus particles to the cell surface. This activity is antagonized in [...] Read more.
Tetherin, an interferon-induced host protein encoded by the bone marrow stromal antigen 2 (BST2/CD317/HM1.24) gene, is involved in obstructing the release of many retroviruses and other enveloped viruses by cross-linking the budding virus particles to the cell surface. This activity is antagonized in the case of human immunodeficiency virus (HIV)-1 wherein its accessory protein Viral Protein U (Vpu) interacts with tetherin, causing its downregulation from the cell surface. Vpu and tetherin connect through their transmembrane (TM) domains, culminating into events leading to tetherin degradation by recruitment of β-TrCP2. However, mutations in the TM domains of both proteins are reported to act as a resistance mechanism to Vpu countermeasure impacting tetherin’s sensitivity towards Vpu but retaining its antiviral activity. Our study illustrates the binding aspects of blood-derived, brain-derived, and consensus HIV-1 Vpu with tetherin through protein–protein docking. The analysis of the bound complexes confirms the blood-derived Vpu–tetherin complex to have the best binding affinity as compared to other two. The mutations in tetherin and Vpu are devised computationally and are subjected to protein–protein interactions. The complexes are tested for their binding affinities, residue connections, hydrophobic forces, and, finally, the effect of mutation on their interactions. The single point mutations in tetherin at positions L23Y, L24T, and P40T, and triple mutations at {L22S, F44Y, L37I} and {L23T, L37T, T45I}, while single point mutations in Vpu at positions A19H and W23Y and triplet of mutations at {V10K, A11L, A19T}, {V14T, I18T, I26S}, and {A11T, V14L, A15T} have revealed no polar contacts with minimal hydrophobic interactions between Vpu and tetherin, resulting in reduced binding affinity. Additionally, we have explored the aggregation potential of tetherin and its association with the brain-derived Vpu protein. This work is a possible step toward an understanding of Vpu–tetherin interactions. Full article
(This article belongs to the Special Issue NeuroAIDS: Cognition, Immunology, Virology and Drug Abuse)
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