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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.    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)  (K  D  = 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)  (K  D  = 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.

virology journal

Quantitative investigation of the direct interaction between Hemagglutinin and fusion proteins of Peste des petits ruminant virus using surface Plasmon resonance