Structure of parainfluenza virus receptor binding region and control of the virus infection

点击翻译按钮获取中文摘要

We demonstrated that 4-Ο-thiocarbamoylmethyl-Neu5Ac2en had strong inhibitory activity toward human parainfluenza type 1 (hPIV-1) sialidase. 4-Ο-thiocarbamoylmethyl-Neu5Ac2en was effective in inhibiting receptor binding and the growth of hPIV-1. To identify the region of the receptor binding pocket between hPIV-1 and hPIV-3, we generated the plasmid expression vector containing each hemagglutinin-neuraminidase gene. We found that hPIV-1 and hPIV-3 NHs had different receptor specificities. We evaluated the abilities of hPIV-1 and hPIV-3 to bind to different types of sialylglycoproteins, and we compared their binding abilities with that of SV. hPIV-1 and hPIV-3 preferentially bound to GP-2 with a terminal Neu5Ac linked to branched N-acetyllactosaminoglycans by the α2-3 linkage. hPIV-3 also weakly bound to glycoconjugates with a terminal Neu5Ac linked to branched N-acetyllactosaminoglycans by the α2-6 linkage. We also designed novel Neu5Ac2en analogs modified at the C-4 containing the different length of thioamido groups. We will analyze the effects of the analogs for hPIV-1 and hPIV-3 sialidase activities and the viral replication.