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Special Issue "Viral Entry Inhibitors"

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A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Animal Viruses".

Deadline for manuscript submissions: closed (31 January 2013)

Special Issue Editor

Guest Editor
Dr. Asim Kumar Debnath

Head, Laboratory of Molecular Modeling & Drug Design, Member, Lindsley F. Kimball Research Institute, New York Blood Center, 310 E 67th Street, New York, NY 10065, USA
Website | E-Mail
Fax: +(212) 570 3168

Special Issue Information

Dear Colleagues,

Virus entry into host cells is the earliest step in a productive infection process for both enveloped and non-enveloped viruses. The mechanism of virus entry of enveloped viruses has been studied quite extensively and two drugs targeted to the entry pathway of HIV-1 have been approved by the US FDA. Many more inhibitors are currently being studied to inhibit HIV-1 entry. However, the entry process of non-enveloped viruses is poorly understood. In this special issue, we hope to capture the recent developments in our understanding of the entry mechanism of both enveloped and non-enveloped viruses and their inhibition.

Dr. Asim Kumar Debnath
Guest Editor

Submission

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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a 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 1500 CHF (Swiss Francs).

Keywords

  • virus entry
  • enveloped and non-enveloped viruses
  • entry inhibitors
  • fusion inhibitors
  • mechanism of virus entry
  • pathogenesis
  • drug-resistance

Published Papers (6 papers)

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Review

Open AccessReview HIV-1 Diversity in the Envelope Glycoproteins: Implications for Viral Entry Inhibition
Viruses 2013, 5(2), 595-604; doi:10.3390/v5020595
Received: 12 December 2012 / Revised: 24 January 2013 / Accepted: 31 January 2013 / Published: 6 February 2013
Cited by 6 | PDF Full-text (568 KB) | HTML Full-text | XML Full-text
Abstract
Entry of HIV-1 into a host cell is a multi-step process, with the viral envelope gp120 and gp41 acting sequentially to mediate the viral attachment, CD4 binding, coreceptor binding, and fusion of the viral and host membranes. The emerging class of antiretroviral agents,
[...] Read more.
Entry of HIV-1 into a host cell is a multi-step process, with the viral envelope gp120 and gp41 acting sequentially to mediate the viral attachment, CD4 binding, coreceptor binding, and fusion of the viral and host membranes. The emerging class of antiretroviral agents, collectively known as entry inhibitors, interfere in some of these steps. However, viral diversity has implications for possible differential responses to entry inhibitors, since envelope is the most variable of all HIV genes. Different HIV genetic forms carry in their genomes genetic signatures and polymorphisms that could alter the structure of viral proteins which are targeted by drugs, thus impairing antiretroviral binding and efficacy. This review will examine current research that describes subtype differences in envelope at the genetic level and the effects of mutations on the efficacy of current entry inhibitors. Full article
(This article belongs to the Special Issue Viral Entry Inhibitors)
Open AccessReview Carbohydrate-Related Inhibitors of Dengue Virus Entry
Viruses 2013, 5(2), 605-618; doi:10.3390/v5020605
Received: 16 January 2013 / Revised: 1 February 2013 / Accepted: 4 February 2013 / Published: 6 February 2013
Cited by 11 | PDF Full-text (521 KB) | HTML Full-text | XML Full-text
Abstract
Dengue virus (DENV), which is transmitted by Aedes mosquitoes, causes fever and hemorrhagic disorders in humans. The virus entry process mediated through host receptor molecule(s) is crucial for virus propagation and the pathological progression of dengue disease. Therefore, elucidation of the molecular mechanisms
[...] Read more.
Dengue virus (DENV), which is transmitted by Aedes mosquitoes, causes fever and hemorrhagic disorders in humans. The virus entry process mediated through host receptor molecule(s) is crucial for virus propagation and the pathological progression of dengue disease. Therefore, elucidation of the molecular mechanisms underlying virus entry is essential for an understanding of dengue pathology and for the development of effective new anti-dengue agents. DENV binds to its receptor molecules mediated through a viral envelope (E) protein, followed by incorporation of the virus-receptor complex inside cells. The fusion between incorporated virus particles and host endosome membrane under acidic conditions is mediated through the function of DENV E protein. Carbohydrate molecules, such as sulfated glycosaminoglycans (GAG) and glycosphingolipids, and carbohydrate-recognition proteins, termed lectins, inhibit virus entry. This review focuses on carbohydrate-derived entry inhibitors, and also introduces functionally related compounds with similar inhibitory mechanisms against DENV entry. Full article
(This article belongs to the Special Issue Viral Entry Inhibitors)
Open AccessReview Influenza A Virus Entry Inhibitors Targeting the Hemagglutinin
Viruses 2013, 5(1), 352-373; doi:10.3390/v5010352
Received: 14 December 2012 / Revised: 17 January 2013 / Accepted: 21 January 2013 / Published: 22 January 2013
Cited by 31 | PDF Full-text (365 KB) | HTML Full-text | XML Full-text
Abstract
Influenza A virus (IAV) has caused seasonal influenza epidemics and influenza pandemics, which resulted in serious threat to public health and socioeconomic impacts. Until now, only 5 drugs belong to two categories are used for prophylaxis and treatment of IAV infection. Hemagglutinin (HA),
[...] Read more.
Influenza A virus (IAV) has caused seasonal influenza epidemics and influenza pandemics, which resulted in serious threat to public health and socioeconomic impacts. Until now, only 5 drugs belong to two categories are used for prophylaxis and treatment of IAV infection. Hemagglutinin (HA), the envelope glycoprotein of IAV, plays a critical role in viral binding, fusion and entry. Therefore, HA is an attractive target for developing anti‑IAV drugs to block the entry step of IAV infection. Here we reviewed the recent progress in the study of conformational changes of HA during viral fusion process and the development of HA-based IAV entry inhibitors, which may provide a new choice for controlling future influenza pandemics. Full article
(This article belongs to the Special Issue Viral Entry Inhibitors)
Open AccessReview Respiratory Syncytial Virus Entry Inhibitors Targeting the F Protein
Viruses 2013, 5(1), 211-225; doi:10.3390/v5010211
Received: 7 December 2012 / Revised: 17 December 2012 / Accepted: 11 January 2013 / Published: 16 January 2013
Cited by 21 | PDF Full-text (1058 KB) | HTML Full-text | XML Full-text
Abstract
Human respiratory syncytial virus (RSV) is the main viral cause of respiratory tract infection in infants as well as some elderly and high-risk adults with chronic pulmonary disease and the severely immunocompromised. So far, no specific anti-RSV therapeutics or effective anti-RSV vaccines
[...] Read more.
Human respiratory syncytial virus (RSV) is the main viral cause of respiratory tract infection in infants as well as some elderly and high-risk adults with chronic pulmonary disease and the severely immunocompromised. So far, no specific anti-RSV therapeutics or effective anti-RSV vaccines have been reported. Only one humanized monoclonal antibody, Palivizumab, has been approved for use in high-risk infants to prevent RSV infection. Ribavirin is the only drug licensed for therapy of RSV infection, but its clinical use is limited by its nonspecific anti-RSV activity, toxic effect, and relatively high cost. Therefore, development of novel effective anti-RSV therapeutics is urgently needed. The RSV envelope glycoprotein F plays an important role in RSV fusion with, and entry into, the host cell and, consequently, serves as an attractive target for developing RSV entry inhibitors. This article reviews advances made in studies of the structure and function of the F protein and the development of RSV entry inhibitors targeting it. Full article
(This article belongs to the Special Issue Viral Entry Inhibitors)
Open AccessReview Approaches for Identification of HIV-1 Entry Inhibitors Targeting gp41 Pocket
Viruses 2013, 5(1), 127-149; doi:10.3390/v5010127
Received: 3 December 2012 / Revised: 3 January 2013 / Accepted: 3 January 2013 / Published: 11 January 2013
Cited by 13 | PDF Full-text (600 KB) | HTML Full-text | XML Full-text
Abstract
The hydrophobic pocket in the HIV-1 gp41 N-terminal heptad repeat (NHR) domain plays an important role in viral fusion and entry into the host cell, and serves as an attractive target for development of HIV-1 fusion/entry inhibitors. The peptide anti-HIV drug targeting gp41
[...] Read more.
The hydrophobic pocket in the HIV-1 gp41 N-terminal heptad repeat (NHR) domain plays an important role in viral fusion and entry into the host cell, and serves as an attractive target for development of HIV-1 fusion/entry inhibitors. The peptide anti-HIV drug targeting gp41 NHR, T-20 (generic name: enfuvirtide; brand name: Fuzeon), was approved by the U.S. FDA in 2003 as the first HIV fusion/entry inhibitor for treatment of HIV/AIDS patients who fail to respond to the current antiretroviral drugs. However, because T20 lacks the pocket-binding domain (PBD), it exhibits low anti-HIV-1 activity and short half-life. Therefore, several next-generation HIV fusion inhibitory peptides with PBD have been developed. They possess longer half-life and more potent antiviral activity against a broad spectrum of HIV-1 strains, including the T-20-resistant variants. Nonetheless, the clinical application of these peptides is still limited by the lack of oral availability and the high cost of production. Thus, development of small molecule compounds targeting the gp41 pocket with oral availability has been promoted. This review describes the main approaches for identification of HIV fusion/entry inhibitors targeting the gp41 pocket and summarizes the latest progress in developing these inhibitors as a new class of anti-HIV drugs. Full article
(This article belongs to the Special Issue Viral Entry Inhibitors)
Open AccessReview Escape from Human Immunodeficiency Virus Type 1 (HIV-1) Entry Inhibitors
Viruses 2012, 4(12), 3859-3911; doi:10.3390/v4123859
Received: 6 November 2012 / Revised: 8 December 2012 / Accepted: 12 December 2012 / Published: 19 December 2012
Cited by 14 | PDF Full-text (806 KB) | HTML Full-text | XML Full-text
Abstract
The human immunodeficiency virus (HIV) enters cells through a series of molecular interactions between the HIV envelope protein and cellular receptors, thus providing many opportunities to block infection. Entry inhibitors are currently being used in the clinic, and many more are under development.
[...] Read more.
The human immunodeficiency virus (HIV) enters cells through a series of molecular interactions between the HIV envelope protein and cellular receptors, thus providing many opportunities to block infection. Entry inhibitors are currently being used in the clinic, and many more are under development. Unfortunately, as is the case for other classes of antiretroviral drugs that target later steps in the viral life cycle, HIV can become resistant to entry inhibitors. In contrast to inhibitors that block viral enzymes in intracellular compartments, entry inhibitors interfere with the function of the highly variable envelope glycoprotein as it continuously adapts to changing immune pressure and available target cells in the extracellular environment. Consequently, pathways and mechanisms of resistance for entry inhibitors are varied and often involve mutations across the envelope gene. This review provides a broad overview of entry inhibitor resistance mechanisms that inform our understanding of HIV entry and the design of new inhibitors and vaccines. Full article
(This article belongs to the Special Issue Viral Entry Inhibitors)

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