Analysis of the glycoproteins of Seoul orthohantavirus strain B1 associated with fusion activity

Collection Location Koleksi E-book & E-Journal Perpustakaan Pusat Unila
Edition Vol. 163, Issue 2
Call Number
ISBN/ISSN 14328798
Author(s) Isegawa, Yuji
Okuno, Yoshinobu
Subject(s) Biomedicine
Classification NONE
Series Title
GMD E-Journal
Language English
Publisher Springer
Publishing Year 2018
Publishing Place Switzerland
Abstract/Notes Abstract We analyzed two virus variants (S1 and L1) from
Seoul orthohantavirus strain B1. Strain B1 produces large
opaque plaques when plated on Vero E6 cell monolayers.
However, although the L1 variant produced the large opaque
plaques common to the strain, the variant S1 produced small
clear ones on Vero E6 cells. Five days after Vero E6 cells
were infected with the S1 variant, polykaryons formed spontaneously.
However, the cells infected with the L1 variant
did not show the formation of syncytia. An analysis of the
pH dependency of the cell fusion demonstrated that the L1
variant could induce cell fusion, but only at a pH that was
0.2 units lower than the pH at which the S1 variant induced
it. Sequencing of the M genome segment of the two virus
variants revealed amino acid substitutions at 4 positions in
the Gn and Gc gene products of the S1 variant. Two of these
substitutions occurred in the extracellular domain of Gn and
changed the charge of the protein. Our findings suggest that
these amino acid substitutions caused the S1 variant Gn protein
to induce fusion at an elevated pH.
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