Elsevier established a free COVID-19 resource center in January 2020, offering information in English and Mandarin. The center grants permission for free access to research on PubMed Central and other repositories. A study analyzed 80 SARS-CoV-2 variants and 26 glycosylation mutants to assess their infectivity and antigenicity. Key findings include that the D614G mutation, along with other mutations, increases infectivity. Mutations like N331 and N343 glycosylation deletions reduce infectivity, while mutations such as N234Q and L452R increase resistance to neutralizing antibodies. Glycosylation sites are crucial for viral infectivity, and changes in the receptor-binding domain (RBD) affect antibody sensitivity. The study highlights the importance of monitoring viral mutations for vaccine and therapeutic development. The results suggest that glycosylation and RBD mutations significantly influence viral behavior and immune responses.Elsevier established a free COVID-19 resource center in January 2020, offering information in English and Mandarin. The center grants permission for free access to research on PubMed Central and other repositories. A study analyzed 80 SARS-CoV-2 variants and 26 glycosylation mutants to assess their infectivity and antigenicity. Key findings include that the D614G mutation, along with other mutations, increases infectivity. Mutations like N331 and N343 glycosylation deletions reduce infectivity, while mutations such as N234Q and L452R increase resistance to neutralizing antibodies. Glycosylation sites are crucial for viral infectivity, and changes in the receptor-binding domain (RBD) affect antibody sensitivity. The study highlights the importance of monitoring viral mutations for vaccine and therapeutic development. The results suggest that glycosylation and RBD mutations significantly influence viral behavior and immune responses.