AUTHOR=Matsushima Yuki , Mizukoshi Fuminori , Sakon Naomi , Doan Yen Hai , Ueki Yo , Ogawa Yasutaka , Motoya Takumi , Tsukagoshi Hiroyuki , Nakamura Noriko , Shigemoto Naoki , Yoshitomi Hideaki , Okamoto-Nakagawa Reiko , Suzuki Rieko , Tsutsui Rika , Terasoma Fumio , Takahashi Tomoko , Sadamasu Kenji , Shimizu Hideaki , Okabe Nobuhiko , Nagasawa Koo , Aso Jumpei , Ishii Haruyuki , Kuroda Makoto , Ryo Akihide , Katayama Kazuhiko , Kimura Hirokazu TITLE=Evolutionary Analysis of the VP1 and RNA-Dependent RNA Polymerase Regions of Human Norovirus GII.P17-GII.17 in 2013–2017 JOURNAL=Frontiers in Microbiology VOLUME=10 YEAR=2019 URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2019.02189 DOI=10.3389/fmicb.2019.02189 ISSN=1664-302X ABSTRACT=

Human norovirus (HuNoV) GII.P17-GII.17 (Kawasaki2014 variant) reportedly emerged in 2014 and caused gastroenteritis outbreaks worldwide. To clarify the evolution of both VP1 and RNA-dependent RNA polymerase (RdRp) regions of GII.P17-GII.17, we analyzed both global and novel Japanese strains detected during 2013–2017. Time-scaled phylogenetic trees revealed that the ancestral GII.17 VP1 region diverged around 1949, while the ancestral GII.P17 RdRp region diverged around 2010. The evolutionary rates of the VP1 and RdRp regions were estimated at ~2.7 × 10−3 and ~2.3 × 10−3 substitutions/site/year, respectively. The phylogenetic distances of the VP1 region exhibited no overlaps between intra-cluster and inter-cluster peaks in the GII.17 strains, whereas those of the RdRp region exhibited a unimodal distribution in the GII.P17 strains. Conformational epitope positions in the VP1 protein of the GII.P17-GII.17 strains were similar, although some substitutions, insertions and deletions had occurred. Strains belonging to the same cluster also harbored substitutions around the binding sites for the histo-blood group antigens of the VP1 protein. Moreover, some amino acid substitutions were estimated to be near the interface between monomers and the active site of the RdRp protein. These results suggest that the GII.P17-GII.17 virus has produced variants with the potential to alter viral antigenicity, host-binding capability, and replication property over the past 10 years.