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Role of lipids in virus assembly

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889195824 Year: Pages: 91 DOI: 10.3389/978-2-88919-582-4 Language: English
Publisher: Frontiers Media SA
Subject: Science (General) --- Microbiology --- Botany
Added to DOAB on : 2016-03-10 08:14:32
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Abstract

RNA enveloped viruses comprise several families belonging to plus and minus strand RNA viruses, such as retroviruses, flavoviruses and orthomyxoviruses. Viruses utilize cellular lipids during critical steps of replication like entry, assembly and egress. Growing evidence indicate important roles for lipids and lipid nanodomains in virus assembly. This special topic covers key aspects of virus-membrane interactions during assembly and egress, especially those of retroviruses and Ebola virus (EBOV). Virus assembly and release involve specific and nonspecific interactions between viral proteins and membrane compartments. Retroviral Gag proteins assemble predominantly on the PM. Despite the great progress in identifying the factors that modulate retroviral Gag assembly on the PM, there are still gaps in our understanding of precise mechanisms of Gag-membrane interactions. Studies over the last two decades have focused on the mechanisms by which other retroviral Gag proteins interact with membranes during assembly. These include human immunodeficiency virus (HIV), Rous sarcoma virus (RSV), equine infectious anemia virus (EIAV), Mason-Pfizer monkey virus (M-PMV), murine leukemia virus (MLV), and human T-lymphotropic virus type (HTLV-1). Additionally, assembly of filoviruses such as EBOV also occurs on the inner leaflet of the PM. The articles published under this special topic highlight the latest understanding of the role of membrane lipids during virus assembly, egress and release.

Keywords

retroviruses --- HIV 1 --- Gag --- Matrix --- membrane --- NMR --- Ebola --- VP40

HIV-Induced Damage of B Cells and Production of HIV Neutralizing Antibodies

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889454617 Year: Pages: 171 DOI: 10.3389/978-2-88945-461-7 Language: English
Publisher: Frontiers Media SA
Subject: Medicine (General) --- Allergy and Immunology
Added to DOAB on : 2018-11-16 17:17:57
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Multiple dysfunctions take place in the B cell compartment during HIV-1 infection, comprising depletion of resting memory B cells carrying serological memory to vaccines and previously met pathogens. In addition, population of B cells characterized by the expression of exhaustion markers are enlarged during HIV-1 infection. Antibodies with the capacity to neutralize a broad range of HIV-1 isolates can be detected only in a minority of infected patients, after a year or more from acute infection. An open question is whether the inability of producing neutralizing HIV-1 antibodies is somehow linked to the B cell immunopathology observed in patients. In this research topic we invited scientists to summarize the current state of knowledge on regulation and development of B cells and antibody responses during HIV-1 infection; fifteen contributions were received comprising both reviews and original articles. The articles are related to B cell dysfunctions identified in HIV-1 infected individuals, production of different types of antibodies (neutralizing versus non neutralizing, and of different isotypes) in vivo during HIV-1 infection and the biological factors which may impact on this process, clinical potential and applications of anti-HIV antibodies and how to achieve neutralizing antibody responses to HIV-1 epitopes upon vaccination. The topic has gathered articles on front-line research undertaken in the field of B cells and antibodies in HIV-1 infection. It is our hope that the collection of articles presented in this book may be useful for new and experienced scholars in the field and add a piece to the complex puzzle of knowledge needed for the development of an HIV-1 vaccine.

Macromolecular Structure Underlying Recognition in Innate Immunity

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889455270 Year: Pages: 151 DOI: 10.3389/978-2-88945-527-0 Language: English
Publisher: Frontiers Media SA
Subject: Medicine (General) --- Allergy and Immunology
Added to DOAB on : 2019-01-23 14:53:42
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Abstract

Immune molecules have evolved to distinguish “self “molecules from “non-self”, “altered self” and “danger” molecules. Recognition is mediated via interactions between pattern recognition receptor molecules (PPRs) and their ligands, which include hydrophobic and electrostatic interactions between amino acid residues on the PPRs and uncharged or charged groups on amino acid residues, sugar rings or DNA/RNA molecules. Recognition in innate immunity range from cases (C1q, mannin-binding protein etc) where recognition is orchestrated by interaction between many ligands with one receptor molecule, and density of interaction is necessary for strong specific recognition, distinct from weak non-specific binding, and cases such as TLRs and NLRs where recognition involves complexation of single receptor and ligand, followed by oligomerisation of the receptor molecule. The majority of PPR molecules bind and recognise a wide variety of ligands, e.g TLR4 recognises LPS (gram negative bacteria), Lipotechoic acid (gram positive bacteria), heat shock protein hsp60, respiratory syncytial virus fusion protein etc, molecules that are structurally dissimilar to each other. This indicates considerable flexibility in their binding domains (amino acid residue variations) and modes (hydrophobic and charged, direct or mediated via an adaptor molecule). However, in many cases there is a dearth of structural and molecular data available, required to delineate the mechanism of ligand binding underlining recognition in pathogen receptors in innate immunity. Insights into requirements of conformation, charge, surface etc in the recognition and function of innate immunity receptors and their activation pathways, based on current data can suggest valuable avenues for future work.

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