BREAKING🔔 The 19th paper from G2P-Japan🇯🇵 is out at Lancet Infectious Diseases @TheLancetInfDis . We elucidated the virological characteristics of new SARS-CoV-2 variant of interest, XBB.1.16 (aka #Arcturus) Please RT🔥 1/ thelancet.com/journals/lanin…
XBB.1.16 = XBB.1 + #F486P, #E180V, and #T478K in spike.
cf. XBB.1.5 = XBB.1 + #F486P in spike (i.e., XBB.1.16 = XBB.1.5 + #E180V and #T478K in spike). 2/
A phylogenetic tree shows that XBB.1.16 is a descendant of XBB.1, not of XBB.1.5. 3/
The relative basic reproduction number (Re) of XBB.1.16 is greater than that of XBB.1.5 in 🇮🇳🇺🇸🇸🇬🇦🇺, suggesting that XBB.1.16 will outcompete XBB.1.5 in the future. 4/
Pseudovirus experiments showed the increased infectivity by #T478K mutation. In contrast, #E180V decreased the infectivity. In total, the infectivity of XBB.1.16 was comparable to that of XBB.1.5. 5/
Neutralization assay showed that XBB.1.16 is robustly resistant to BA.2 breakthru infection sera (18-fold vs B.1.1) and BA.5 breakthru infection sera (37-fold vs B.1.1). 6/
Antigenic cartography shows that the antigenicity of XBB.1.16 is slightly different from that of XBB.1.5. 7/
Importantly, XBB.1.16 as well as the other XBB subvariants are sensitive to #sotrovimab, a therapeutic monoclonal antibody. 8/
In sum, our results suggest the increased fitness of XBB.1.16 may be due to (1) different antigenicity from XBB.1.5; and/or (2) the mutations in the non-S viral protein(s) that may contribute to increased viral growth efficiency. 9/9
PS - Yunlong @yunlong_cao explains more about XBB.1.16 and other new variants based on his data. This should add to and increase our knowledge🔥
Correction!
XBB.1.16 = XBB.1 + #F486P, #E180V, and #T478R in spike. cf. XBB.1.5 = XBB.1 + #F486P in spike (i.e., XBB.1.16 = XBB.1.5 + #E180V and #T478R in spike).
XBB.1 and XBB.1.5 harbor T478'K', while XBB.1.16 harbors T478'R'.
Correction (again)!
Pseudovirus experiments showed the increased infectivity by #T478R (not T478’K’!) mutation. In contrast, #E180V decreased the infectivity. In total, the infectivity of XBB.1.16 was comparable to that of XBB.1.5. 5/
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BREAKING🔔 We introduce the latest work from G2P-Japan🇯🇵 focusing on the virological characteristics of new SARS-CoV-2 lineage of concern, XBB.1.5 (aka #Kraken), which is rapidly spreading in the US🇺🇸 Please RT! Preprint/peer-review paper will come soon🔥 1/
XBB.1.5 = XBB.1 + #F486P in spike. We also found that a part of XBB.1.5 has reversion mutation in Y144del (=XBB.1.5 + #ins144Y) in spike. Because #Y144del evades antiviral immunity and decreases pseudovirus infectivity, its reversion might be also critical. 2/
First, a brilliant young talent, @jampei2, showed that the relative basic reproduction number (Re) of XBB.1.5 is >1.2-fold greater than the parental XBB.1 (❗️). Importantly the "1.2-fold difference" is similar to the differences between BA.1 versus BA.2 and BA.2 versus BA.5. 3/
BREAKING🔔 The 15th preprint from G2P-Japan🇯🇵 is out @biorxivpreprint. We illuminated the virological characteristics of one of the latest SARS-CoV-2 lineages of concern, XBB, which was generated by recombination of two #Omicron subvariants. Please RT. 1/ biorxiv.org/content/10.110…
In late 2022, the Omicron subvariants have highly diversified. An example is BQ.1.1, which has convergently acquired amino acid substitutions at five critical residues in the spike protein: R346T, K444T, L452R, N460K & F486V. We reported it as below⬇️ 2/
Another variant of concern is XBB (aka #gryphon). First, two young talents, @jampei2 & @SpyrosLytras, showed that XBB emerged by recombination of two co-circulating BA.2 lineages, BJ.1 & BM.1.1.1 (a progeny of BA.2.75), during 2022 summer in India or its neighboring countries. 3/
BREAKING🔔 The 14th preprint from G2P-Japan🇯🇵 is out @biorxivpreprint. We illuminated the evolutionary rule underlying the convergent evolution of #Omicron and the virological characteristics of one of the latest lineages of concern, BQ.1.1. Please RT. 1/ biorxiv.org/content/10.110…
In late 2022, the Omicron subvariants have highly diversified. However, some lineages have convergently acquired amino acid substitutions at five critical residues in the spike protein: R346, K444, L452, N460 and F486. 2/