Background
The specific and dynamic interaction between the hemagglutinin (H) and fusion (F) proteins of morbilliviruses is a prerequisite for the conformational rearrangements and membrane fusion during infection process. The two heptad repeat regions (HRA and HRB) of F protein are both important for the triggering of F protein.
Conclusions
The differences of the binding affinities suggested that HRB is involved in functionally important intermolecular interaction in the fusion process.
Methods
In this study, the direct interactions of Peste des petits ruminants virus (PPRV) H with F, HRA and HRB were quantitatively evaluated using biosensor surface plasmon resonance (SPR).
Results
The binding affinities of immobilized pCMV-HA-H (HA-H) interacted with proteins pCMV-HA-F (HA-F) and pCMV-HA-HRB (HA-HRB) (KD = 1.91 × 10- 8 M and 2.60 × 10- 7 M, respectively) reacted an order of magnitude more strongly than that of pCMV-HA-HRA (HA-HRA) and pCMV-HA-Tp IGFR-LD (HA) (KD = 1.08 × 10- 4 M and 1.43 × 10- 4 M, respectively). Conclusions: The differences of the binding affinities suggested that HRB is involved in functionally important intermolecular interaction in the fusion process.