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Interferon-Induced Transmembrane Proteins at the Intersection of Virus Infection and...
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Interferon-Induced Transmembrane Proteins at the Intersection of Virus Infection and Immunity

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Viral Immunology, Vaccines, and Antivirals".

Deadline for manuscript submissions: closed (31 March 2024) | Viewed by 4625

Special Issue Editors

Prof. Chen Liang

E-Mail Website
Guest Editor
Lady Davis Institute, Jewish General Hospital, McGill University, Montreal, QC H3T 1E2, Canada
Interests: HIV; host restriction; CRISPR/Cas9; BST-2; IFITM; Mxb
Dr. Alex Compton

E-Mail Website
Guest Editor
HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA
Interests: retroviruses; RNA viruses; innate immunity; virus evolution; gene therapy

Special Issue Information

Dear Colleagues,

Interferon-induced transmembrane (IFITM) proteins provide key mechanisms in host antiviral innate immunity, particularly in the context of interferon responses to diverse viral infections. As membrane-bound proteins, they are located in the plasma membrane and endocytic compartments where they deter the entry of invading viruses including influenza viruses, West Nile virus, Ebola virus, human immunodeficiency virus, and many other pathogenic viruses. The known molecular mechanisms include the modulation of membrane curvature and fluidity in a manner that disfavors fusion between virus and cell. Their constitutive expression in certain cell types, such as stem cells, allows protection from virus assault, which can be further reinforced by interferons. Some viruses have evolved effective mechanisms to evade inhibition by IFITM, such as by mutating viral envelope proteins; some viruses even benefit from the presence of IFITM. The contribution of IFITM to antiviral immunity goes beyond guarding the cellular gate of virus entry, since they are expressed in immune cells such as T cells and B cells and regulate immune cell activation and, hence, adaptive immunity.

After more than one decade of research, we continue to be surprised by the versatile antiviral functions performed by IFITM proteins. In this Special Issue, we aim to publish exciting studies related to IFITM functions, including but not limited to the characterization and regulation of antiviral mechanisms, strategies for viral evasion and counteraction, and the functional interplay with other innate and adaptive antiviral mechanisms.

Prof. Chen Liang
Dr. Alex Compton
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 submissions that pass pre-check are 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 single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers (4 papers)

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Research

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17 pages, 3036 KiB  
Article
IFITM1 and IFITM3 Proteins Inhibit the Infectivity of Progeny HIV-1 without Disrupting Envelope Glycoprotein Clusters
by Smita Verma, Yen-Cheng Chen, Mariana Marin, Scott E. Gillespie and Gregory B. Melikyan
Viruses 2023, 15(12), 2390; https://doi.org/10.3390/v15122390 - 07 Dec 2023
Cited by 1 | Viewed by 938
Abstract
Human interferon-induced transmembrane (IFITM) proteins inhibit the fusion of a broad spectrum of enveloped viruses, both when expressed in target cells and when present in infected cells. Upon expression in infected cells, IFITMs incorporate into progeny virions and reduce their infectivity by a [...] Read more.
Human interferon-induced transmembrane (IFITM) proteins inhibit the fusion of a broad spectrum of enveloped viruses, both when expressed in target cells and when present in infected cells. Upon expression in infected cells, IFITMs incorporate into progeny virions and reduce their infectivity by a poorly understood mechanism. Since only a few envelope glycoproteins (Envs) are present on HIV-1 particles, and Env clustering has been proposed to be essential for optimal infectivity, we asked if IFITM protein incorporation modulates HIV-1 Env clustering. The incorporation of two members of the IFITM family, IFITM1 and IFITM3, into HIV-1 pseudoviruses correlated with a marked reduction of infectivity. Super-resolution imaging of Env distribution on single HIV-1 pseudoviruses did not reveal significant effects of IFITMs on Env clustering. However, IFITM3 reduced the Env processing and incorporation into virions relative to the control and IFITM1-containing viruses. These results show that, in addition to interfering with the Env function, IFITM3 restricts HIV-1 Env cleavage and incorporation into virions. The lack of notable effect of IFITMs on Env clustering supports alternative restriction mechanisms, such as modification of the properties of the viral membrane. Full article
(This article belongs to the Special Issue Interferon-Induced Transmembrane Proteins at the Intersection of Virus Infection and Immunity)
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16 pages, 2775 KiB  
Article
A Proteomics-Based Approach Identifies the NEDD4 Adaptor NDFIP2 as an Important Regulator of Ifitm3 Levels
by Federico Marziali, Yuxin Song, Xuan-Nhi Nguyen, Lucid Belmudes, Julien Burlaud-Gaillard, Philippe Roingeard, Yohann Couté and Andrea Cimarelli
Viruses 2023, 15(10), 1993; https://doi.org/10.3390/v15101993 - 26 Sep 2023
Viewed by 894
Abstract
IFITMs are a family of highly related interferon-induced transmembrane proteins that interfere with the processes of fusion between viral and cellular membranes and are thus endowed with broad antiviral properties. A number of studies have shown how the antiviral potency of IFITMs is [...] Read more.
IFITMs are a family of highly related interferon-induced transmembrane proteins that interfere with the processes of fusion between viral and cellular membranes and are thus endowed with broad antiviral properties. A number of studies have shown how the antiviral potency of IFITMs is highly dependent on their steady-state levels, their intracellular distribution and a complex pattern of post-translational modifications, parameters that are overall tributary of a number of cellular partners. In an effort to identify additional protein partners involved in the biology of IFITMs, we devised a proteomics-based approach based on the piggyback incorporation of IFITM3 partners into extracellular vesicles. MS analysis of the proteome of vesicles bearing or not bearing IFITM3 identified the NDFIP2 protein adaptor protein as an important regulator of IFITM3 levels. NDFIP2 is a membrane-anchored adaptor protein of the E3 ubiquitin ligases of the NEDD4 family that have already been found to be involved in IFITM3 regulation. We show here that NDFIP2 acts as a recruitment factor for both IFITM3 and NEDD4 and mediates their distribution in lysosomal vesicles. The genetic inactivation and overexpression of NDFIP2 drive, respectively, lower and higher levels of IFITM3 accumulation in the cell, overall suggesting that NDFIP2 locally competes with IFITM3 for NEDD4 binding. Given that NDFIP2 is itself tightly regulated and highly responsive to external cues, our study sheds light on a novel and likely dynamic layer of regulation of IFITM3. Full article
(This article belongs to the Special Issue Interferon-Induced Transmembrane Proteins at the Intersection of Virus Infection and Immunity)
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Review

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13 pages, 3141 KiB  
Review
Role of Viral Envelope Proteins in Determining Susceptibility of Viruses to IFITM Proteins
by Thomas Marceau and Martine Braibant
Viruses 2024, 16(2), 254; https://doi.org/10.3390/v16020254 - 05 Feb 2024
Viewed by 880
Abstract
Interferon-induced transmembrane proteins (IFITMs) are a family of proteins which inhibit infections of various enveloped viruses. While their general mechanism of inhibition seems to be non-specific, involving the tightening of membrane structures to prevent fusion between the viral envelope and cell membrane, numerous [...] Read more.
Interferon-induced transmembrane proteins (IFITMs) are a family of proteins which inhibit infections of various enveloped viruses. While their general mechanism of inhibition seems to be non-specific, involving the tightening of membrane structures to prevent fusion between the viral envelope and cell membrane, numerous studies have underscored the importance of viral envelope proteins in determining the susceptibility of viruses to IFITMs. Mutations in envelope proteins may lead to viral escape from direct interaction with IFITM proteins or result in indirect resistance by modifying the viral entry pathway, allowing the virus to modulate its exposure to IFITMs. In a broader context, the nature of viral envelope proteins and their interaction with IFITMs can play a crucial role in the context of adaptive immunity, leading to viral envelope proteins that are more susceptible to antibody neutralization. The precise mechanisms underlying these observations remain unclear, and further studies in this field could contribute to a better understanding of how IFITMs control viral infections. Full article
(This article belongs to the Special Issue Interferon-Induced Transmembrane Proteins at the Intersection of Virus Infection and Immunity)
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10 pages, 1697 KiB  
Review
Discovery and Characterization of IFITM S-Palmitoylation
by Tandrila Das and Howard C. Hang
Viruses 2023, 15(12), 2329; https://doi.org/10.3390/v15122329 - 28 Nov 2023
Viewed by 1283
Abstract
Interferon-induced transmembrane proteins (IFITM1, 2 and 3) are important host antiviral defense factors. They are active against viruses like the influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV) and severe acute respiratory syndrome coronavirus (SARS-CoV). In this review, [...] Read more.
Interferon-induced transmembrane proteins (IFITM1, 2 and 3) are important host antiviral defense factors. They are active against viruses like the influenza A virus (IAV), dengue virus (DENV), Ebola virus (EBOV), Zika virus (ZIKV) and severe acute respiratory syndrome coronavirus (SARS-CoV). In this review, we focus on IFITM3 S-palmitoylation, a reversible lipid modification, and describe its role in modulating IFITM3 antiviral activity. Our laboratory discovered S-palmitoylation of IFITMs using chemical proteomics and demonstrated the importance of highly conserved fatty acid-modified Cys residues in IFITM3 antiviral activity. Further studies showed that site-specific S-palmitoylation at Cys72 is important for IFITM3 trafficking to restricted viruses (IAV and EBOV) and membrane–sterol interactions. Thus, site-specific lipid modification of IFITM3 directly regulates its antiviral activity, cellular trafficking, and membrane-lipid interactions. Full article
(This article belongs to the Special Issue Interferon-Induced Transmembrane Proteins at the Intersection of Virus Infection and Immunity)
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