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Doherty, Ryan; Oliveira, Túlio de; Seebregts, Christopher J.; Danaviah, Sivapragashini; Gordon, Michelle; Cassol, Sharon

doi:10.1186/1742-4690-2-18

Cited by 18 publications

(11 citation statements)

References 25 publications

(19 reference statements)

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“…There is no direct evidence of p17-induced oxidative stress. However, p17 possesses specific structural motifs defined as “ coiled coil ” sequences, and has a high propensity to form multimers, mis-fold and aggregate, forming amyloidogenic assemblies [ 164 , 165 ]. This is typical to amyloidogenic proteins actively involved in the pathogenesis of many human diseases, such as Alzheimer’s disease and Parkinson’ disease.…”

Section: Oncogenic Hiv-1 Proteins Induce Oxidative Stressmentioning

confidence: 99%

Oncogenic Effects of HIV-1 Proteins, Mechanisms Behind

Isaguliants

Bayurova

Avdoshina

et al. 2021

Cancers

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People living with human immunodeficiency virus (HIV-1) are at increased risk of developing cancer, such as Kaposi sarcoma (KS), non-Hodgkin lymphoma (NHL), cervical cancer, and other cancers associated with chronic viral infections. Traditionally, this is linked to HIV-1-induced immune suppression with depletion of CD4+ T-helper cells, exhaustion of lymphopoiesis and lymphocyte dysfunction. However, the long-term successful implementation of antiretroviral therapy (ART) with an early start did not preclude the oncological complications, implying that HIV-1 and its antigens are directly involved in carcinogenesis and may exert their effects on the background of restored immune system even when present at extremely low levels. Experimental data indicate that HIV-1 virions and single viral antigens can enter a wide variety of cells, including epithelial. This review is focused on the effects of five viral proteins: envelope protein gp120, accessory protein negative factor Nef, matrix protein p17, transactivator of transcription Tat and reverse transcriptase RT. Gp120, Nef, p17, Tat, and RT cause oxidative stress, can be released from HIV-1-infected cells and are oncogenic. All five are in a position to affect “innocent” bystander cells, specifically, to cause the propagation of (pre)existing malignant and malignant transformation of normal epithelial cells, giving grounds to the direct carcinogenic effects of HIV-1.

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Section: Oncogenic Hiv-1 Proteins Induce Oxidative Stressmentioning

confidence: 99%

Oncogenic Effects of HIV-1 Proteins, Mechanisms Behind

Isaguliants

Bayurova

Avdoshina

et al. 2021

Cancers

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“…The three-dimensional structure of p17, determined by nuclear magnetic resonance and X-ray crystallography, reveals that individual folded p17 molecules are composed of five major α-helixes and a highly basic platform consisting of three β strands 26 , 27 . Due to the presence of specific structural motifs defined as “ coiled coil” sequences, p17 displays a high propensity to misfold and aggregate 28 . This HIV-1 matrix protein is known to possess self-interaction properties since it forms trimers 29 , 30 and hexamers 31 .…”

Section: Introductionmentioning

confidence: 99%

HIV-1 matrix protein p17 misfolding forms toxic amyloidogenic assemblies that induce neurocognitive disorders

Zeinolabediny

Caccuri

Colombo

et al. 2017

Sci Rep

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Human immunodeficiency virus type-1 (HIV-1)-associated neurocognitive disorder (HAND) remains an important neurological manifestation that adversely affects a patient’s quality of life. HIV-1 matrix protein p17 (p17) has been detected in autoptic brain tissue of HAND individuals who presented early with severe AIDS encephalopathy. We hypothesised that the ability of p17 to misfold may result in the generation of toxic assemblies in the brain and may be relevant for HAND pathogenesis. A multidisciplinary integrated approach has been applied to determine the ability of p17 to form soluble amyloidogenic assemblies in vitro. To provide new information into the potential pathogenic role of soluble p17 species in HAND, their toxicological capability was evaluated in vivo. In C. elegans, capable of recognising toxic assemblies of amyloidogenic proteins, p17 induces a specific toxic effect which can be counteracted by tetracyclines, drugs able to hinder the formation of large oligomers and consequently amyloid fibrils. The intrahippocampal injection of p17 in mice reduces their cognitive function and induces behavioral deficiencies. These findings offer a new way of thinking about the possible cause of neurodegeneration in HIV-1-seropositive patients, which engages the ability of p17 to form soluble toxic assemblies.

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“…As in the original version of the BioAfrica HIV-1 Proteomics Resource, the section on protein domains/folds/motifs includes information about the predicted motifs and structure of the protein as well as the protein functional domains ( 1 ). For example, the gp120 had five variable loops (V1–V5).…”

Section: Resultsmentioning

confidence: 99%

“…The objective of the BioAfrica HIV-1 Proteomics Resource is to provide accurate and comprehensive information on Human Immunodeficiency Virus (HIV) proteins. The first version of the resource was published in 2005 ( 1 ) and became popular across the scientific community. But, as with any resource, there is a need for information to be current and accurate.…”

Section: Introductionmentioning

confidence: 99%

Improving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource

et al. 2016

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The Human Immunodeficiency Virus (HIV) is one of the pathogens that cause the greatest global concern, with approximately 35 million people currently infected with HIV. Extensive HIV research has been performed, generating a large amount of HIV and host genomic data. However, no effective vaccine that protects the host from HIV infection is available and HIV is still spreading at an alarming rate, despite effective antiretroviral (ARV) treatment. In order to develop effective therapies, we need to expand our knowledge of the interaction between HIV and host proteins. In contrast to virus proteins, which often rapidly evolve drug resistance mutations, the host proteins are essentially invariant within all humans. Thus, if we can identify the host proteins needed for virus replication, such as those involved in transporting viral proteins to the cell surface, we have a chance of interrupting viral replication. There is no proteome resource that summarizes this interaction, making research on this subject a difficult enterprise. In order to fill this gap in knowledge, we curated a resource presents detailed annotation on the interaction between the HIV proteome and host proteins. Our resource was produced in collaboration with ViralZone and used manual curation techniques developed by UniProtKB/Swiss-Prot. Our new website also used previous annotations of the BioAfrica HIV-1 Proteome Resource, which has been accessed by approximately 10 000 unique users a year since its inception in 2005. The novel features include a dedicated new page for each HIV protein, a graphic display of its function and a section on its interaction with host proteins. Our new webpages also add information on the genomic location of each HIV protein and the position of ARV drug resistance mutations. Our improved BioAfrica HIV-1 Proteome Resource fills a gap in the current knowledge of biocuration.Database URL: http://www.bioafrica.net/proteomics/HIVproteome.html

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Abstract: Most Internet online resources for investigating HIV biology contain either bioinformatics tools, protein information or sequence data.

Cited by 18 publications

References 25 publications

Oncogenic Effects of HIV-1 Proteins, Mechanisms Behind

Oncogenic Effects of HIV-1 Proteins, Mechanisms Behind

HIV-1 matrix protein p17 misfolding forms toxic amyloidogenic assemblies that induce neurocognitive disorders

Improving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource

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