NDLI: Structural studies on membrane-embedded influenza hemagglutinin and its fragments.

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Structural studies on membrane-embedded influenza hemagglutinin and its fragments.

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Structural studies on membrane-embedded influenza hemagglutinin and its fragments.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gray, C. Tamm, L. K.
Description	Country affiliation: United States Author Affiliation: Gray C ( Department of Molecular Physiology and Biological Physics, University of Virginia Health Sciences Center, Charlottesville 22906-0011, USA.)
Abstract	The mechanism of influenza virus hemagglutinin (HA)-mediated membrane fusion has been inferred in part from studies examining pH-induced structural changes in soluble HA derivatives lacking the viral membrane anchor and, sometimes, the fusion peptide (the C- and N-terminal residues of the HA2 chain, respectively). To reconcile structure-based mechanisms of HA-mediated membrane fusion with structural implications of functional studies performed on membrane-embedded HA, we have undertaken attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopic analyses of membrane-embedded HA (strain X:31) and its fragments reconstituted into supported lipid bilayers. The fragments correspond to proteolytic products with the majority of the HA1 chain and, in some cases, the fusion peptide removed (THA2 and THA2F-, respectively). In combination with R18 fluorescence dequenching to monitor the functional implications of HA1 subunit removal, we have assessed the influence of pH and target membrane presentation on the secondary structures, orientations relative to the membrane, and dynamics of these molecules. We find that X:31 HA is more tilted towards the plane of the membrane under fusion than under resting conditions, that the fitting of HA depends on the presence of the HA1 chain, that the residues connecting the membrane-inserted fusion peptide with the crystallographically determined coiled coil probably adopt an alpha-helical conformation, and that several changes in the secondary structure and the amide H/D exchange kinetics occur as a result of acidification and target membrane presentation, which can be interpreted as small changes and a release of strain in the static and dynamic structure of membrane-bound HA. THA2 mediatcs fusion, but less efficiently and with less pH-selectivity than HA.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hemagglutinin Glycoproteins, Influenza Virus Chemistry Peptide Fragments Viral Envelope Proteins Amino Acid Sequence Animals Chick Embryo Metabolism Hydrogen-ion Concentration Kinetics Liposomes Membrane Fusion Molecular Sequence Data Protein Conformation Protein Structure, Secondary Recombinant Proteins Spectrometry, Fluorescence Spectroscopy, Fourier Transform Infrared Trypsin Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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