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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2004-5-11
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pubmed:abstractText |
The influenza virus uses hemagglutinin (HA) to fuse the viral and cellular membranes. As part of an effort to study the membrane-interacting elements of HA, the fusion peptide, and the C-terminal transmembrane anchor, we have expressed in Escherichia coli the full-length HA(2) chain with maltose-binding protein fused at its N-terminus. The chimeric protein can be refolded in vitro in the presence of specific detergents to yield stable, homogeneous trimers, as determined by analytical ultracentrifugation. The trimers have the so-called "low pH" conformation-the rearranged HA(2) conformation obtained when intact HA(1)/HA(2) is induced to refold by exposure to low pH-as detected by electron microscopy and monoclonalantibody reactivity. These results provide further evidence for the notion that the neutral-pH structure of intact HA is metastable and that binding of protons lowers the kinetic barriers that prevent rearrangement to the minimum-free-energy conformation. The refolded chimeric protein described here is a suitable species for undertaking studies of how the fusion peptide inserts into membranes and assessing the nature of possible intermediates in the fusion process.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5902-11
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15134464-Amino Acid Sequence,
pubmed-meshheading:15134464-Carrier Proteins,
pubmed-meshheading:15134464-Detergents,
pubmed-meshheading:15134464-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:15134464-Escherichia coli Proteins,
pubmed-meshheading:15134464-Genetic Vectors,
pubmed-meshheading:15134464-Hemagglutinin Glycoproteins, Influenza Virus,
pubmed-meshheading:15134464-Hemagglutinins, Viral,
pubmed-meshheading:15134464-Hydrogen-Ion Concentration,
pubmed-meshheading:15134464-Maltose-Binding Proteins,
pubmed-meshheading:15134464-Molecular Sequence Data,
pubmed-meshheading:15134464-Protein Conformation,
pubmed-meshheading:15134464-Protein Folding,
pubmed-meshheading:15134464-Recombinant Fusion Proteins,
pubmed-meshheading:15134464-Solubility,
pubmed-meshheading:15134464-Structure-Activity Relationship,
pubmed-meshheading:15134464-Ultracentrifugation
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pubmed:year |
2004
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pubmed:articleTitle |
Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation.
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pubmed:affiliation |
Department of Biological Chemistry and Molecular Pharmacology, Howard Hughes Medical Institute, Harvard Medical School, 250 Longwood Avenue, Boston, Massachusetts 02115, USA. swalley@crystal.harvard.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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