Since January 2020, Elsevier has created a COVID-19 resource center with free information in English and Mandarin on the novel coronavirus. The resource center is hosted on Elsevier Connect, the company's public news and information website. Elsevier grants permission to make all its COVID-19-related research available in PubMed Central and other publicly funded repositories, including the WHO COVID database, with unrestricted research reuse and analyses, provided that the original source is acknowledged. These permissions are granted for free as long as the COVID-19 resource center remains active. The study investigates the impact of mutations in the SARS-CoV-2 spike protein on viral infectivity and antigenicity. Over 100 mutations were selected for analysis, including the dominant D614G mutation and its combinations with other amino acid changes. The results show that D614G and its combinations are more infectious, while most variants with amino acid changes at the receptor binding domain (RBD) are less infectious. However, variants containing A475V, L452R, V483A, and F490L became resistant to some neutralizing antibodies. Glycosylation site mutations, such as the deletion of both N331 and N343 glycosylation sites, also significantly reduced infectivity. Additionally, some mutations, such as N234Q, L452R, A475V, and V483A, were found to be resistant to certain monoclonal antibodies. These findings have implications for vaccine and therapeutic antibody development.Since January 2020, Elsevier has created a COVID-19 resource center with free information in English and Mandarin on the novel coronavirus. The resource center is hosted on Elsevier Connect, the company's public news and information website. Elsevier grants permission to make all its COVID-19-related research available in PubMed Central and other publicly funded repositories, including the WHO COVID database, with unrestricted research reuse and analyses, provided that the original source is acknowledged. These permissions are granted for free as long as the COVID-19 resource center remains active. The study investigates the impact of mutations in the SARS-CoV-2 spike protein on viral infectivity and antigenicity. Over 100 mutations were selected for analysis, including the dominant D614G mutation and its combinations with other amino acid changes. The results show that D614G and its combinations are more infectious, while most variants with amino acid changes at the receptor binding domain (RBD) are less infectious. However, variants containing A475V, L452R, V483A, and F490L became resistant to some neutralizing antibodies. Glycosylation site mutations, such as the deletion of both N331 and N343 glycosylation sites, also significantly reduced infectivity. Additionally, some mutations, such as N234Q, L452R, A475V, and V483A, were found to be resistant to certain monoclonal antibodies. These findings have implications for vaccine and therapeutic antibody development.