%0 Journal Article
%T Detailed analysis of low temperature inactivation of respiratory syncytial virus.
%A Kitai Y
%A Watanabe O
%A Ohmiya S
%A Kisu T
%A Ota R
%A Kawakami K
%A Katoh H
%A Fukuzawa K
%A Takeda M
%A Nishimura H
%J Sci Rep
%V 14
%N 1
%D 2024 05 23
%M 38783052
%F 4.996
%R 10.1038/s41598-024-62658-z
%X Our previous findings indicated that many respiratory syncytial virus (RSV) isolates are unstable at 4 °C compared to 20 °C. Some of the strains completely lose infectivity after 24 h at 4 °C. This study analyzed the inactivation process at 4 °C using a representative strain, RSV/Sendai/851/13. After 24 h of storage at 4 °C, the virus was completely inactivated but retained its ability to attach to and to be taken into host cells. It suggested a reduced fusion ability between the viral and cellular membranes. During storage at 4 °C, the RSV fusion (F) protein underwent a conformational change and was no longer recognized by pre-fusion form-specific antibodies. When the RSV/Sendai/851/13 strain was passaged at 4 °C, a variant with an amino acid substitution, I148T, in the F protein fusion peptide was selected. Also, an amino acid change in G protein demonstrating stability at low temperatures was obtained. These results show that the inactivation of RSV at 4 °C is due to the loss of membrane fusion activity in the F protein, which cannot maintain its pre-fusion state at 4 °C.