Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.

Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. Research Abstract Details 

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Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. Abstract Text:

Laura E Luque,Charles J Russell,

During viral entry, the paramyxovirus fusion (F) protein fuses the viral envelope to a cellular membrane. Similar to other class I viral fusion glycoproteins, the F protein has two heptad repeat regions (HRA and HRB) that are important in membrane fusion and can be targeted by antiviral inhibitors. Upon activation of the F protein, HRA refolds from a spring-loaded, crumpled structure into a coiled coil that inserts a hydrophobic fusion peptide into the target membrane and binds to the HRB helices to form a fusogenic hairpin. To investigate how F protein conformational changes are regulated, we mutated in the Sendai virus F protein a highly conserved 10-residue sequence in HRA that undergoes major structural changes during protein refolding. Nine of the 15 mutations studied caused significant defects in F protein expression, processing, and fusogenicity. Conversely, the remaining six mutations enhanced the fusogenicity of the F protein, most likely by helping spring the HRA coil. Two of the residues that were neither located at "a" or "d" positions in the heptad repeat nor conserved among the paramyxoviruses were key regulators of the folding and fusion activity of the F protein, showing that residues not expected to be important in coiled-coil formation may play important roles in regulating membrane fusion. Overall, the data support the hypothesis that regions in the F protein that undergo dramatic changes in secondary and tertiary structure between the prefusion and hairpin conformations regulate F protein expression and activation.

Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. Publishing Authors By Initials

LE Luque,CJ Russell,

For similar biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus internalization research abstracts see: biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus internalization research

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Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of virology

VOLUME: 81

Page Numbers: 3130-41

Journal Abbreviation: J. Virol.

ISSN: 0022-538X

DAY: 24

MONTH: 01

YEAR: 2007

Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 113724

Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. Keywords Mesh Terms:

KEYWORDS: Virus Internalization

MESH TERMS: metabolism

Chemical & Substance for Abstract: Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. Information

Substance Name: Trypsin

Registry Number: EC 3.4.21.4

Grant and Affiliation Information for Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.

AFFILIATION: Department of Infectious Diseases, MS 320, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105-2794, USA.

Country: United States

AGENCY: United States NCI

GRANT: CA 21765

ACRONYM: CA

MEDLINETA: J Virol

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