Recombinant Measles virus Fusion glycoprotein F0 (F), partial, Biotinylated

1. Cell-to-Cell Measles Virus Spread between Human Neurons Is Dependent on Hemagglutinin and Hyperfusogenic Fusion Protein. PMID: 29298883
2. L454W F mutant is activated independently of H or the cell receptor that enabled the efficient spread in the central nervous system. PMID: 25670774
3. Acquisition of enhanced fusion activity through substitutions in the extracellular domain of the F protein may be crucial for measles virus to the extensive spread in the central nervous system and development of subacute sclerosing panencephalitis. PMID: 25520515
4. Complementation of F mutants with a monomeric, fusion-inactive F variant enriched the F oligomers for heterotrimers containing a single disulfide bond, without affecting fusion complementation profiles compared with standard F protein. PMID: 25157143
5. F maturation prepares for complex separation after triggering, and the H head domains in prereceptor-bound conformation prevent premature stalk rearrangements and F activation. PMID: 25392208
6. Thermodynamically stabilized by the N465H substitution, the F protein required elevated temperature as high as 40 degrees C to promote cell-cell fusion, whereas all five DIII mutations caused destabilization of the F protein PMID: 25479085
7. Authors demonstrate that the measles virus H stalk represents the effector domain for measles virus F triggering. PMID: 23966411
8. Taken together, these findings reveal that the morbillivirus H protein must lower the activation energy barrier of metastable prefusion F for fusion triggering. PMID: 23077316
9. The F genes of measles virus isolated in china had no significant genetic variation. PMID: 20084883
10. The F genes of measles virus in China during 1999-2003 had no sig-nificant changes. PMID: 20077667
11. residues located in the head domain of the F trimer and the HR-B region contribute jointly to controlling F conformational stability PMID: 16415028
12. findings show that both M (a fraction of which is modified by ubiquitination) & F proteins individually promote formation of virus-like particles, but they do not act in synergy; we propose that M & F act separately in particle morphogenesis and release PMID: 17374768
13. These findings suggest a common molecular mechanism and a key role of the F protein for syncytium formation in cells expressing an unidentified third receptor for MV. PMID: 17825451
14. Tyrosine-based targeting motifs in the H and F glycoproteins play a crucial role for MV replication and spread within lymphocytes, the main target cells of acute MV infection. PMID: 18272759
15. The partitioning of F, CD46 and CD55 molecules in different membrane microdomains could account for the ability of F to escape complement regulation by the CD55 and CD46 regulators. PMID: 18455798
16. Alanine-scanning mutagenesis revealed that an F protein with a single mutation of a central TM region leucine (L507A) was more fusogenic than the unmodified F protein while retaining similar kinetics of proteolytic processing. PMID: 18786999
17. The H-protein and the F-protein mediates the virus cell entry. PMID: 19198562
18. findings argue against specific protein-protein contacts between the H head & F head domains; support a docking model characterized by short-range contacts between prefusion F head & attachment protein stalk, possibly involving H residues 111, 114 & 118 PMID: 19656895

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KEGG: vg:1489800