Source:http://linkedlifedata.com/resource/pubmed/id/18222422
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-2-4
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pubmed:abstractText |
Removal of the R peptide (residues 617-632) from the Moloney murine leukemia virus (MoMuLV) envelope protein (Env) cytoplasmic tail potentiates fusion. We examined the role of the membrane-proximal cytoplasmic domain (598-616) of the MoMuLV Env in the Env-mediated membrane fusion and incorporation. The Env truncated at 616 exhibits maximum fusogenicity in cell-to-cell fusion assay. By comparison, full tail Env (632) and the Env truncated to residue 601 mediated fusion at 40%. The Envs truncated to residues 598 or 595 are not fusogenic. Progressive cytoplasmic tail truncation correlated with decreased Env incorporation into virions. Substitution of the domain 598-616 with an amphiphilic alpha-helix from melittin results in maximally fusogenic Envs that efficiently incorporated into transduction competent virions. However, substitution of the domain 598-616 with random or hydrophilic sequences caused loss of the Env fusogenicity and titer while retaining incorporation. Further, a secondary structure prediction analysis of 27 unrelated Env cytoplasmic tails indicates a common (23/27) propensity for an amphiphilic alpha-helical domain at immediate proximity to the viral membrane. These results support the suggestion that viral fusion is enhanced by a membrane-proximal cytoplasmic amphiphilic alpha-helix in Env tail. The model of its action is proposed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-4800
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18-30
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pubmed:meshHeading |
pubmed-meshheading:18222422-Amino Acid Sequence,
pubmed-meshheading:18222422-Animals,
pubmed-meshheading:18222422-Cell Fusion,
pubmed-meshheading:18222422-Cell Line,
pubmed-meshheading:18222422-Cell Membrane,
pubmed-meshheading:18222422-Gene Products, env,
pubmed-meshheading:18222422-Humans,
pubmed-meshheading:18222422-Melitten,
pubmed-meshheading:18222422-Membrane Fusion,
pubmed-meshheading:18222422-Mice,
pubmed-meshheading:18222422-Models, Molecular,
pubmed-meshheading:18222422-Molecular Sequence Data,
pubmed-meshheading:18222422-Moloney murine leukemia virus,
pubmed-meshheading:18222422-Mutation,
pubmed-meshheading:18222422-Protein Structure, Secondary,
pubmed-meshheading:18222422-Protein Structure, Tertiary,
pubmed-meshheading:18222422-Recombinant Fusion Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Membrane-proximal cytoplasmic domain of Moloney murine leukemia virus envelope tail facilitates fusion.
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pubmed:affiliation |
San Diego Cancer Research Institute, 1200 Garden View, Suite 200, Encinitas, CA 92024, USA. YaninaAdler@cox.net
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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