Abstract
BackgroundThe 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.MethodsIn 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).ResultsThe 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).ConclusionsThe differences of the binding affinities suggested that HRB is involved in functionally important intermolecular interaction in the fusion process.
Highlights
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
Expression and identification of the recombinant proteins The amplified gene encoding Peste des petits ruminants virus (PPRV) H, F, HRA and HRB were digested by restriction enzymes, and directional cloned into pCMV-HA-Tp IGFR-LD (HA) plasmid to generate successfully the HA fusion expression vectors HA-H, HA-F, HA-HRA and HA-HRB, respectively
The positive proportions and median of fluorescence intensity of plasmids-transfected CHO cells treated with anti-HA monoclonal antibody (MAb) were far higher than that of cells treated with isotype control antibody (Fig. 2)
Summary
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. Entry processes of enveloped viruses are complex and involve a variety of proteins of virus itself and host. Two viral glycoproteins plays the key role in the infection process: the hemagglutinin (H) and fusion (F) proteins [1]. The H protein is responsible for binding to the target cell, while the F protein mediates membrane fusion, inducing the virus-cell and cell-cell fusion [2, 3]. Peste des petits ruminants virus (PPRV), a member of the genus Morbillivirus in the Paramyxoviridae family causes an acutecontagious disease. Peste des petits ruminants (PPR) has recently been targeted as the candidate for global eradication
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