Many viruses, beside binding to their main cell target, interact with other molecules that promote virus adhesion tothe cell; often, these additional targets are glycans. The main receptor for SARSCoV2 is a peptide motif in the ACE2 protein. We studied interaction of the recombinant SARSCoV2 spike (S) protein with an array of glycoconjugates, includ ing various sialylated, sulfated, and other glycans, and found that the S protein binds some (but not all) glycans of the lac tosamine family. We suggest that parallel influenza infection will promote SARSCoV2 adhesion to the respiratory epithe lial cells due to the unmasking of lactosamine chains by the influenza virus neuraminidase.