A spring-loaded mechanism for the conformational change of influenza hemagglutinin

Article Abstract:

A study to determine the fusion-active, or fusogenic, conformation of influenza hemagglutinin (HA) is reported. HA undergoes a conformational change which is required for membrane fusion, but its fusogenic structure has never been characterized. The study revealed a sequence in HA which has a high propensity for forming a coiled coil. A modelk for the fusogenic conformation is proposed in which the coiled coil stem of the native conformatoin extends to relocate the hydrophobic fusion peptide by 100 angstroms towards a target membrane.

Influenza viruses

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Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex

Article Abstract:

An examination of membrane fusion in the Semliki Forest virus through cryoelectron microscopy revealed spike proteins in the spike complex. Under low pH, the spike structure undergoes unexpected conformational change. Mapping the location of the proteins through icosahedral reconstruction showed that conformational change caused by the cleavage of p62 results to movement and fusion activity between the structural proteins in the complex.

Viruses, Morphology (Biology)

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Fibril conformation as the basis of species- and strain-dependent seeking specificity of mammalian prion amyloids

Article Abstract:

A demonstration that PrP23-144 amyloids from different species adopt distinct secondary structures and morphologies, and that one or two residues in a critical region control these structural differences is presented. Evidence is provided that protein conformations are transmitted in PrP amyloids strains, establishing a foundation for a structural basis of mammalian prion transmission barriers.

Analysis, Glycoproteins, Prion diseases

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