PDF(Pubmed)
Abstract：
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.
摘要：
我们先前的发现表明，与20°C相比，许多呼吸道合胞病毒（RSV）分离株在4°C下不稳定。一些菌株在4°C下24小时后完全失去感染性。这项研究使用代表性菌株分析了4°C下的失活过程，RSV/仙台/851/13。在4°C下储存24小时后，该病毒被完全灭活，但保留了其附着并被带入宿主细胞的能力。这表明病毒和细胞膜之间的融合能力降低。在4°C储存期间，RSV融合(F)蛋白发生构象变化,不再被融合前形式特异性抗体识别.当RSV/Sendai/851/13菌株在4℃传代时，具有氨基酸取代的变体，I148T,在F蛋白中选择融合肽。此外，获得了在低温下证明稳定性的G蛋白中的氨基酸变化。这些结果表明，RSV在4°C时的失活是由于F蛋白中膜融合活性的丧失，在4°C下不能保持其融合前状态。
