The fusion protein core of measles virus forms stable coiled-coil trimer. Biochem Biophys Res Commun 2002 Dec 20;299(5):897-902
Date
12/10/2002Pubmed ID
12470664DOI
10.1016/s0006-291x(02)02761-4Scopus ID
2-s2.0-0036926562 (requires institutional sign-in at Scopus site) 26 CitationsAbstract
Recent studies have shown that paramyxovirus might adopt a similar molecular mechanism of virus entry and fusion in which the attachment glycoprotein binds receptor/s and triggers the conformational changes of the fusion protein. There are two conserved regions of heptad repeat (HR1 and HR2) in the fusion protein and they were shown with fusion-inhibition effects in many paramyxoviruses, including measles virus. They also appear to show characteristic structure in the fusion core: the HR1/HR2 forms stable six-helix coiled-coil centered by HR1 and is surrounded by HR2 (trimer of HR1/HR2), which represents the post-fusion conformational structure. In this study, we expressed the HR1 and HR2 of measles virus fusion protein as a single chain (named 2-Helix) and subsequently tested its formation of trimer. Indeed, the results do show that the HR1 and HR2 interact with each other and form stable six-helix coiled-coil bundle. This is the first member in genus Morbillivirus of family Paramyxoviridae to be confirmed with this characteristic structure and provides the basis for the HR2-inhibition effects on virus fusion/entry for measles virus.
Author List
Zhu J, Zhang CW, Qi Y, Tien P, Gao GFAuthor
Jieqing Zhu PhD Assistant Professor, Associate Investigator in the Biochemistry department at BloodCenter of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceCircular Dichroism
Measles virus
Membrane Fusion
Molecular Sequence Data
Protein Structure, Quaternary
Protein Structure, Secondary
Repetitive Sequences, Amino Acid
Sequence Alignment
Viral Fusion Proteins