Dimerization of Hepatitis E Virus Capsid Protein E2s Domain Is Essential for Virus–Host Interaction
Figure 5
Mutational studies on the dimer interface.
(A) The schematic representation of wild-type E2 and eleven point mutations targeting the dimer interface region. Secondary structural elements are shown for the E2s region. The mutated residues located on the β-strands and coils are shown in red and black, respectively. (B) These mutants and wild-type E2 were subjected to non-reducing SDS-PAGE and Western Blotting with the neutralizing mAb 8C11 and 8H3 to study the effects of these mutations on dimerization and neutralization, respectively. [+] denotes dimerization or reactivity with 8C11 or 8H3, [−] denotes loss of the respective property. Note that both the capacity to form dimers and the reactivity with mAb 8C11 and 8H3 were abolished simultaneously in six of these mutants: Y557A, T564A, V598E, A599E, L601E and A602E.