SARS-CoV-2 is part of the Coronaviridae family, whose members are named after their crown-like appearance under the electron microscope caused by the surface glycoproteins that decorate the virus. Coronaviruses have a large (30+ kb) single-stranded positivesense RNA genome encoding for several open reading frames. One frame encodes the spike protein (S protein), a class I fusion protein that mediates attachment of the virus to cell surface receptors followed by uptake into endosomes (for most coronaviruses). Proteolytic cleavage of the S protein and fusion of viral and endosomal membranes trigger release of viral RNA into the cytosol. We know now from studies on SARS-CoV-1 and the related MERS-CoV vaccines that the S protein on the surface of the virus is an ideal target for a vaccine. In SARS-CoV-1 and SARS-CoV-2, this protein interacts with the receptor ACE2, and antibodies targeting the spike can interfere with this binding, thereby neutralizing the virus. The structure of the S protein of SARS-CoV-2 was solved in record time at high resolution, contributing to our understanding of this vaccine target. More than 90 vaccines are being developed against SARS-CoV-2 by research teams in companies and universities across the world.