SERINC5: One antiviral factor to bind them all

Timilsina, Uddhav; Stavrou, Spyridon

doi:10.1371/journal.ppat.1011076

Cited by 3 publications

(2 citation statements)

References 33 publications

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“…The Serinc family is composed of five paralogues. Initially identified as retroviral restriction factors, they are now known to inhibit diverse enveloped viruses including influenza A, SARS-CoV-2, and hepatitis B viruses (162)(163)(164)(165)(166). Serinc3 and Serinc5 localize to the plasma membrane.…”

Section: Serincsmentioning

confidence: 99%

Viral Membrane Fusion: A Dance Between Proteins and Lipids

White,

Ward,

Odongo

et al. 2023

Annu. Rev. Virol.

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There are at least 21 families of enveloped viruses that infect mammals, and many contain members of high concern for global human health. All enveloped viruses have a dedicated fusion protein or fusion complex that enacts the critical genome-releasing membrane fusion event that is essential before viral replication within the host cell interior can begin. Because all enveloped viruses enter cells by fusion, it behooves us to know how viral fusion proteins function. Viral fusion proteins are also major targets of neutralizing antibodies, and hence they serve as key vaccine immunogens. Here we review current concepts about viral membrane fusion proteins focusing on how they are triggered, structural intermediates between pre- and postfusion forms, and their interplay with the lipid bilayers they engage. We also discuss cellular and therapeutic interventions that thwart virus-cell membrane fusion.

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Section: Serincsmentioning

confidence: 99%

Viral Membrane Fusion: A Dance Between Proteins and Lipids

White,

Ward,

Odongo

et al. 2023

Annu. Rev. Virol.

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“…The demonstration that S3 and S5 reduce the glycosylation of hepatitis B virus (HBV) glycoproteins to inhibit the secretion of virus particles [ 27 ] revealed that SERINC proteins can interfere with virus replication using multiple strategies. Most viruses that are sensitive to SERINC restriction express viral proteins for its antagonism (e.g., Nef for HIV-1; GlycoGag for MLV and FeLV-B; Orf7a for SARS-CoV-2; S2 for EIAV; small, large and mid-size surface proteins for HBV) [ 28 ]. Together, these findings suggest SERINC’s antiviral function as an important player in the tug-of-war between viruses and their hosts and have triggered intense research efforts aimed at dissecting the mechanisms of restriction and antagonism, as well as their physiological relevance.…”

Section: Introduction: Serinc Proteins As Antiviral Restriction Factorsmentioning

confidence: 99%

Beyond Impairment of Virion Infectivity: New Activities of the Anti-HIV Host Cell Factor SERINC5

Sid Ahmed,

Bajak,

Fackler

2024

Viruses

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Members of the serine incorporator (SERINC) protein family exert broad antiviral activity, and many viruses encode SERINC antagonists to circumvent these restrictions. Significant new insight was recently gained into the mechanisms that mediate restriction and antagonism. In this review, we summarize our current understanding of the mode of action and relevance of SERINC proteins in HIV-1 infection. Particular focus will be placed on recent findings that provided important new mechanistic insights into the restriction of HIV-1 virion infectivity, including the discovery of SERINC’s lipid scramblase activity and its antagonism by the HIV-1 pathogenesis factor Nef. We also discuss the identification and implications of several additional antiviral activities by which SERINC proteins enhance pro-inflammatory signaling and reduce viral gene expression in myeloid cells. SERINC proteins emerge as versatile and multifunctional regulators of cell-intrinsic immunity against HIV-1 infection.

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