Vpu Protein: The Viroporin Encoded by HIV-1

González, María Eugenia Pérez

doi:10.3390/v7082824

Cited by 39 publications

(33 citation statements)

References 113 publications

(119 reference statements)

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“…For example, a role in viral release was demonstrated for the human immunodeficiency virus (HIV) vpu protein. Vpu is a ∼80 aa viroporins that oligomerizes to form a selective ion channel that may enhance viral release through its ion channel activity and/or by inhibiting tetherin, a cellular factor which inhibits viral release . Another extensively characterized viroporin is the 97 aa M2 influenza A virus (IAV) protein which oligomerizes to form an ion channel .…”

Section: Virally Encoded Short Proteinsmentioning

confidence: 99%

Viral Short ORFs and Their Possible Functions

2018

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Definition of functional genomic elements is one of the greater challenges of the genomic era. Traditionally, putative short open reading frames (sORFs) coding for less than 100 amino acids were disregarded due to computational and experimental limitations; however, it has become clear over the past several years that translation of sORFs is pervasive and serves diverse functions. The development of ribosome profiling, allowing identification of translated sequences genome wide, revealed wide spread, previously unidentified translation events. New computational methodologies as well as improved mass spectrometry approaches also contributed to the task of annotating translated sORFs in different organisms. Viruses are of special interest due to the selective pressure on their genome size, their rapid and confining evolution, and the potential contribution of novel peptides to the host immune response. Indeed, many functional viral sORFs were characterized to date, and ribosome profiling analyses suggest that this may be the tip of the iceberg. Our computational analyses of sORFs identified by ribosome profiling in DNA viruses demonstrate that they may be enriched in specific features implying that at least some of them are functional. Combination of systematic genome editing strategies with synthetic tagging will take us into the next step-elucidation of the biological relevance and function of this intriguing class of molecules.

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Section: Virally Encoded Short Proteinsmentioning

confidence: 99%

Viral Short ORFs and Their Possible Functions

2018

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“…In addition to the abovementioned target proteins, other intracellular proteins such as HIV-1 reverse transcriptase (RT)/p66, integrase (IN)/p32, protease (PR)/p11, nucleocapsid (NC)/p7, and matrix protein (MA)/p17 are among the promising candidate targets for antiviral treatment as reported in previous reviews [ 2 , 96 ]. Limited studies have also shown antiviral effects by targeting other accessory proteins such as Vif, Vpr, and Vpu [ 97 , 98 , 99 ]. While targeting these HIV-1 proteins resulted in marked HIV-1 inhibition, the viruses have a tendency to resist or escape the drug or inhibitor treatments, including HAART targets such as RT, IN, PR, etc.…”

Section: Targeting Hiv-1 Intracellular Proteins As Therapeutic Tarmentioning

confidence: 99%

Review of Current Cell-Penetrating Antibody Developments for HIV-1 Therapy

Nordin¹,

Teow

2018

Molecules

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The discovery of highly active antiretroviral therapy (HAART) in 1996 has significantly reduced the global mortality and morbidity caused by the acquired immunodeficiency syndrome (AIDS). However, the therapeutic strategy of HAART that targets multiple viral proteins may render off-target toxicity and more importantly results in drug-resistant escape mutants. These have been the main challenges for HAART and refinement of this therapeutic strategy is urgently needed. Antibody-mediated treatments are emerging therapeutic modalities for various diseases. Most therapeutic antibodies have been approved by Food and Drug Administration (FDA) mainly for targeting cancers. Previous studies have also demonstrated the promising effect of therapeutic antibodies against HIV-1, but there are several limitations in this therapy, particularly when the viral targets are intracellular proteins. The conventional antibodies do not cross the cell membrane, hence, the pathogenic intracellular proteins cannot be targeted with this classical therapeutic approach. Over the years, the advancement of antibody engineering has permitted the therapeutic antibodies to comprehensively target both extra- and intra-cellular proteins in various infections and diseases. This review aims to update on the current progress in the development of antibody-based treatment against intracellular targets in HIV-1 infection. We also attempt to highlight the challenges and limitations in the development of antibody-based therapeutic modalities against HIV-1.

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“…The so-called group of accessory proteins from HIV-1, which includes Nef, Vif, Vpu, and Vpr, has long been considered a promising target for developing therapeutic strategies against acquired immunodeficiency syndrome (AIDS) [ 176 ]. The development of effective antiretroviral drugs specifically targeted to Nef, Vif, or Vpu proteins has been attempted using in vitro-selected compounds, although none of these have yet progressed to final approval [ 177 , 178 , 179 , 180 ]. Among the accessory proteins, Vpr ranks second only to Nef in terms of the attention generated to halt virus spread.…”

Section: Progress In Searching For Vpr-targeted Drugsmentioning

confidence: 99%

The HIV-1 Vpr Protein: A Multifaceted Target for Therapeutic Intervention

González

2017

IJMS

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The human immunodeficiency virus type 1 (HIV-1) Vpr protein is an attractive target for antiretroviral drug development. The conservation both of the structure along virus evolution and the amino acid sequence in viral isolates from patients underlines the importance of Vpr for the establishment and progression of HIV-1 disease. While its contribution to virus replication in dividing and non-dividing cells and to the pathogenesis of HIV-1 in many different cell types, both extracellular and intracellular forms, have been extensively studied, its precise mechanism of action nevertheless remains enigmatic. The present review discusses how the apparently multifaceted interplay between Vpr and host cells may be due to the impairment of basic metabolic pathways. Vpr protein modifies host cell energy metabolism, oxidative status, and proteasome function, all of which are likely conditioned by the concentration and multimerization of the protein. The characterization of Vpr domains along with new laboratory tools for the assessment of their function has become increasingly relevant in recent years. With these advances, it is conceivable that drug discovery efforts involving Vpr-targeted antiretrovirals will experience substantial growth in the coming years.

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Vpu Protein: The Viroporin Encoded by HIV-1

Cited by 39 publications

References 113 publications

Viral Short ORFs and Their Possible Functions

Viral Short ORFs and Their Possible Functions

Review of Current Cell-Penetrating Antibody Developments for HIV-1 Therapy

The HIV-1 Vpr Protein: A Multifaceted Target for Therapeutic Intervention

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