Structural basis for membrane fusion by enveloped viruses. NLM AIDSLINE Important note: Information in this article was accurate in 1999. The state of the art may have changed since the publication date.

Click here to return to AIDSLINE main menu
DonateNow
Print this Article


Structural basis for membrane fusion by enveloped viruses.

Mol Membr Biol. 1999 Jan-Mar;16(1):3-9. Unique Identifier : AIDSLINE MED/99265136
Weissenhorn W; Dessen A; Calder LJ; Harrison SC; Skehel JJ; Wiley DC; Laboratory of Molecular Medicine, Children's Hospital, Boston, MA; 02215, USA. weissen@embl-grenoble.fr


Abstract: Enveloped viruses such as HIV-1, influenza virus, and Ebola virus express a surface glycoprotein that mediates both cell attachment and fusion of viral and cellular membranes. The membrane fusion process leads to the release of viral proteins and the RNA genome into the host cell, initiating an infectious cycle. This review focuses on the HIV-1 gp41 membrane fusion protein and discusses the structural similarities of viral membrane fusion proteins from diverse families such as Retroviridae (HIV-1), Orthomyxoviridae (influenza virus), and Filoviridae (Ebola virus). Their structural organization suggests that they have all evolved to use a similar strategy to promote fusion of viral and cellular membranes. This observation led to the proposal of a general model for viral membrane fusion, which will be discussed in detail.
Keywords: JOURNAL ARTICLE REVIEW REVIEW, TUTORIAL Animal Ebola Virus/CHEMISTRY Human HIV Envelope Protein gp41/CHEMISTRY Membrane Fusion/*PHYSIOLOGY Membrane Proteins/PHYSIOLOGY Models, Biological Models, Molecular Moloney Leukemia Virus/CHEMISTRY Orthomyxoviridae/CHEMISTRY Protein Conformation Viral Envelope Proteins/*PHYSIOLOGYKWDjournalarticlereviewreview,tutorialanimalebolavirus/chemistryhumanhivenvelopeproteingp41/chemistrymembranefusion/KWDphysiologymembraneproteins/physiologymodels,biologicalmodels,molecularmoloneyleukemiavirus/chemistryorthomyxoviridae/chemistryproteinconformationviralenvelopeproteins/KWDphysiology
991030
A99A0936

Copyright © 1999 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

AEGiS is a 501(c)3, not-for-profit, tax-exempt, educational corporation. AEGiS is made possible through unrestricted funding from Boehringer Ingelheim, Bridgestone/Firestone Charitable Trust, Bristol-Myers Squibb Company, Elton John AIDS Foundation, Gill Foundation, the National Library of Medicine, Quest Diagnostics, Roche and Trimeris, and donations from users like you. Always watch for outdated information. This article first appeared in 1999. This material is designed to support, not replace, the relationship that exists between you and your doctor.

AEGiS presents published material, reprinted with permission and neither endorses nor opposes any material. All information contained on this website, including information relating to health conditions, products, and treatments, is for informational purposes only. It is often presented in summary or aggregate form. It is not meant to be a substitute for the advice provided by your own physician or other medical professionals. Always discuss treatment options with a doctor who specializes in treating HIV.

Copyright ©1980, 1999. AEGiS. All materials appearing on AEGiS are protected by copyright as a collective work or compilation under U.S. copyright and other laws and are the property of AEGiS, or the party credited as the provider of the content. .