Membrane Trafficking in Viral Replication by S. B. Sieczkarski, G. R. Whittaker (auth.), Dr. Mark Marsh

By S. B. Sieczkarski, G. R. Whittaker (auth.), Dr. Mark Marsh (eds.)

The skill of viruses to take advantage of mobile features for his or her personal ends makes them powerful pathogens and beautiful experimental instruments. paintings with viruses underpins a lot of our present figuring out of molecular mobile biology and similar fields. all of the 8 chapters during this quantity offers with a selected point of viral interactions with mobile membranes. those contain chapters on viral access, viral membrane fusion, viral membrane protein synthesis and delivery, viral replication, viral interactions with cytoskeletal structures and the nucleus, the trafficking of viral membrane proteins and viral perturbation of host phone protein trafficking. those chapters may still supply either an outline of mobile membrane trafficking mechanisms and viral interactions with those platforms, in addition to studies of the present nation of every of the fields.

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B Known class II fusion proteins are activated by proteolytic cleavage of an accessory protein. c The postfusion forms of all known class I fusion proteins are a-helical. The fusion subunit of metastable influenza HA is also highly a-helical, and this appears to be the case for a paramyxovirus F protein [Chen et al. (2001a) Structure 9:255–66]. Comparable information is not available for the metastable forms of other class I fusion proteins. d In the case of paramyxoviruses, the receptor binding protein relays the information of receptor binding to the fusion subunit [Lamb 1993; Colman and Lawrence 2003] followed by an extended chain (Fig.

C-terminal helices are green. For influenza HA2, the C-terminal extended region is yellow. N and C indicate the points where the fusion peptide and the transmembrane domain, respectively, attach ture, a host cell protease cleaves prM, resulting in reorganization of proteins on the viral surface (Allison et al. 1995). After prM cleavage, the E proteins exist as metastable homodimers. The ectodomains of the dimer are oriented antiparallel to one another. In further contrast to the trimeric class I fusion protein spikes, the ectodomains of the E homodimer lie parallel to the viral membrane and close to the surface.

Paramyxovirus F Proteins (Class I Fusion Protein, Neutral pH, Attachment Protein Assisted) . . . . . . . . . . TBE E and SFV E1 (Class II Fusion Proteins, Low pH) . . . . . . . . 36 38 5 Membrane Dynamics During Fusion . . . . . . . . . . 4 Membrane-Interacting Regions of Viral Fusion Proteins. The Fusion Peptide . . . . . . . . . . . Structure of N-terminal Fusion Peptides . . . . . Structure of Internal Fusion Peptides . . . . . . Roles of Fusion Peptides .

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