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Article

The Antagonism of HIV-1 Nef to SERINC5 Particle Infectivity Restriction Involves the Counteraction of Virion-Associated Pools of the Restriction Factor.

Journal of virology - 1 Dec 2016

Trautz Birthe, Pierini Virginia, Wombacher Rebecka, Stolp Bettina, Chase Amanda J, Pizzato Massimo, Fackler Oliver T

Abstract excerpt

SERINC3 (serine incorporator 3) and SERINC5 are recently identified host cell inhibitors of HIV-1 particle infectivity that are counteracted by the viral pathogenesis factor Nef. Here we confirm that HIV-1 Nef, but not HIV-1 Vpu, antagonizes the particle infectivity restriction of SERINC5. SERINC5 antagonism occurred in parallel with other Nef activities, including cell surface receptor downregulation,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to HIV Infections

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Share to nef Gene Products, Human Immunodeficiency Virus

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Source

Open in PubMed Open full text

Identifiers

PMID: 27681140
DOI: 10.1128/JVI.01246-16
PMCID: PMC5110172

Genes

SERINC5
SERINC3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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The Antagonism of HIV-1 Nef to SERINC5 Particle Infectivity Restriction Involves the Counteraction of Virion-Associated Pools of the Restriction Factor.PMID 27681140Read ↗

Variation in HIV-1 Nef function within and among viral subtypes reveals genetically separable antagonism of SERINC3 and SERINC5Semantic proximity Read ↗

SERINC5 as a New Restriction Factor for Human Immunodeficiency Virus and Murine Leukemia VirusSemantic proximity Read ↗

SERINC5 Is the Primary Target of Retroviral Antagonists Among Human SERINC Paralogs and Requires a Tri-Cysteine Motif for Its Counteraction by HIV-1 NefSemantic proximity Read ↗

Proteasomal degradation of human SERINC4: a potent host anti-HIV-1 factor that is antagonized by NefSemantic proximity Read ↗

A Conserved Acidic-Cluster Motif in SERINC5 Confers Partial Resistance to Antagonism by HIV-1 Nef.Semantic proximity Read ↗

SERINC5 Potently Restricts Retrovirus Infection In VivoSemantic proximity Read ↗

An Amino Acid Polymorphism within the HIV-1 Nef Dileucine Motif Functionally Uncouples Cell Surface CD4 and SERINC5 Downregulation.Semantic proximity Read ↗

Potent Enhancement of HIV-1 Replication by Nef in the Absence of SERINC3 and SERINC5Semantic proximity Read ↗

SIVcol Nef counteracts SERINC5 by promoting its proteasomal degradation but does not efficiently enhance HIV-1 replication in human CD4+ T cells and lymphoid tissueSemantic proximity Read ↗

CD4 Expression and Env Conformation Are Critical for HIV-1 Restriction by SERINC5Semantic proximity Read ↗

The retroviral accessory proteins S2, Nef, and glycoMA use similar mechanisms for antagonizing the host restriction factor SERINC5Semantic proximity Read ↗

Influence of different glycoproteins and of the virion core on SERINC5 antiviral activitySemantic proximity Read ↗

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