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Hiv-1 Envelope Glycoproteins : Folding, Function and Vaccin Design.

Author: Ian Sanderson
Publisher: Leiden University Press [Imprint] Amsterdam : Amsterdam University Press. March 2004
Series: UvA Proefschriften Ser.
Edition/Format:   eBook : Document : English
Database:WorldCat
Summary:

The need for a vaccine against HIV is obvious, but the development of an effective vaccine has met with frustrations. The HIV envelope glycoproteins, residing in the viral membrane, are the sole  Read more...

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Genre/Form: Electronic books
Material Type: Document, Internet resource
Document Type: Internet Resource, Computer File
All Authors / Contributors: Ian Sanderson
ISBN: 9789053566671 9053566678
OCLC Number: 697667328
Description: 1 online resource.
Contents: Table of Contents - 6[-]1 Introduction - 8[-]2 Env and HIV transmission - 34[-] 2.1 Differential transmission of HIV-1 by distinct subsets of effector dendritic cells - 34[-]3 Env antigenicity - 52[-] 3.1 The mannose-dependent epitope for neutralizing antibody 2G12 on HIV-1 glycoprotein gp120 - 52[-]4 Env folding - 76[-] 4.1 Folding and functionality of HIV-1 envelope glycoprotein disulfide bond mutants: discrepancies between ER quality control verdicts and viral fitness requirements - 76[-] 4.2 A stable -sheet fold can substitute for a disulfide bond in HIV-1 gp120 - 98[-] 4.3 Local and distal compensatory changes upon evolution of the HIV-1 envelope glycoproteins lacking the N-terminal disulfide bond in gp120 - 118[-]5 Env modifications for vaccines - 128[-] 5.1 A recombinant HIV-1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure - 128[-] 5.2 Variable loop-deleted variants of the HIV-1 envelope glycoprotein can be stabilized by the introduction of an intermolecular disulfide bridge between the gp120 and gp41 subunits - 162[-] 5.3 Biophysical and antigenic properties of a proteolytically mature, disulfide stabilized HIV-1 gp140 envelope glycoprotein - 182[-] 5.4 Evolution of the HIV-1 envelope glycoproteins with a disulfide bond between gp120 and gp41 - 212[-] 5.5 Enhancing the proteolytic maturation of HIV-1 envelope glycoproteins - 226[-] 5.6 Stabilization of the soluble, trimeric form of the envelope glycoprotein complex of HIV-1 - 248[-] 5.7 Evolutionary repair of HIV-1 gp41 with a kink in the N-terminal helix leads to restoration of the six-helix bundle structure - 276[-]6 Concluding remarks - 290[-]Appendix Mutational analyses and natural variability of the gp41 ectodomain - 296[-]Summary - 322[-]Samenvatting (Dutch) - 328[-]Dankwoord (Dutch) - 334[-]Publications - 336
Series Title: UvA Proefschriften Ser.
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