Mechanisms of viral membrane fusion and its inhibition.

  title={Mechanisms of viral membrane fusion and its inhibition.},
  author={Debra M. Eckert and Peter S. Kim},
  journal={Annual review of biochemistry},
Viral envelope glycoproteins promote viral infection by mediating the fusion of the viral membrane with the host-cell membrane. Structural and biochemical studies of two viral glycoproteins, influenza hemagglutinin and HIV-1 envelope protein, have led to a common model for viral entry. The fusion mechanism involves a transient conformational species that can be targeted by therapeutic strategies. This mechanism of infectivity is likely utilized by a wide variety of enveloped viruses for which… 

Figures from this paper

Cell entry of enveloped viruses.

Class II virus membrane fusion proteins.

Viral Membrane Fusion and the Transmembrane Domain

This work summarizes developments made in the past decade that have contributed to the understanding of the transmembrane region of viral fusion proteins, highlighting not only their critical role in the membrane fusion process, but further demonstrating their involvement in several aspects of the viral lifecycle.

[Entry process of enveloped viruses to host cells].

This review summarizes the entry process of enveloped viruses and focuses on the current topics of HIV entry.

Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?

A number of results obtained by the laboratory and by others suggest the existence of a third class of fusion proteins and support the idea that new insights should emerge from studies of membrane fusion mediated by the G protein of rhabdoviruses.

Alpharetrovirus envelope-receptor interactions.

Current research on ASLV Env-receptor interactions are reviewed and the specific molecular requirements of both the viral fusion protein and cognate receptors for ASLV entry are focused on.



Structural basis for membrane fusion by enveloped viruses.

This review focuses on the HIV-1 gp41 membrane fusion protein and discusses the structural similarities of viral membrane fusion proteins from diverse families, suggesting that they have all evolved to use a similar strategy to promote fusion of viral and cellular membranes.

The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens.

The human immunodeficiency virus-type 1 (HIV-1) envelope glycoproteins interact with receptors on the target cell and mediate virus entry by fusing the viral and cell membranes. The structure of the

Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism.

For alpha-, rhabdo- and orthomyxoviruses, a glycop protein is responsible for both virus attachment and fusion, and in the acidic environment of the endosome, the ectodomain portion of the glycoprotein undergoes a major structural rearrangement to generate a fusion-competent state.

New targets for inhibitors of HIV-1 replication

Despite the success of protease and reverse transcriptase inhibitors, new drugs to suppress HIV-1 replication are still needed. Several other early events in the viral life cycle (stages before the

The structure of a membrane fusion mutant of the influenza virus haemagglutinin.

The neutral pH crystal structure of one such mutant HAs from mutant viruses with raised fusion pH optima is determined, and it appears that four intra‐chain hydrogen bonds that stabilize the location of the N‐terminus of HA2 are lost in the mutant, resulting in a local destabilization that facilitates the extrusion of theN‐ terminus at higher pH.

Capture of an early fusion-active conformation of HIV-1 gp41

Using an inhibitory synthetic peptide from HIV-1 gp41, DP-178 binds gp41 and inhibits Env-mediated membrane fusion after gp120 interacts with cellular receptors, indicating that conformational changes involving the coiled coil domain of gp41 are required for entry.

Membrane fusion activity of influenza virus.

The finding that fusion occurs as efficiently with liposomes containing or lacking virus receptor structures, further emphasizes the remarkable division of labor in the HA molecule.