Our work revealed that a high-mannose structure (Man5GlcNAc2) occupied the N1098 site of the postfusion S trimer and had a strong potency to facilitate viral trans/cis-infection via DC- and L-SIGN as co-receptors, indicating that a glycan decorated postfusion structure present on the surface of SARS-CoV-2 virus (Yao et al., 2020) is not redundant and may have a substantial function in receptor binding and mediating viral infection. Here, AQP1 is linked to viral infectious disease.