A new coronavirus (SARS-CoV-2) outbreak began in Wuhan in the province of Hubei at the end of 2019. Despite many similarities to the 2002 outbreak of SARS-CoV, the new SARS-CoV-2 outbreak had higher morbidity and mortality. Most infected individuals show no or mild symptoms, but some present general complications such as acute respiratory distress syndrome, pneumonia, and septic shock, potentially leading to the patient's death. Drawing on established knowledge about the original virus, research groups worldwide have focused their efforts on two viral proteins: i) the spike (s)-glycoprotein, with the aim of disrupting its recognition of the membrane-bound angiotensin-converting enzyme 2 (ACE-2); and ii) the main viral protease (Mpro, 3CLpro), with the aim of disrupting viral replication by hindering the processing of several polyproteins that are translated from the viral RNA. Another approach for tackling the spread of the new virus builds on work on the original SARS virus, which resulted in the development of a vaccine designed to induce the production of antibodies against the viral sglycoprotein, preventing it from recognising and binding to ACE-2. Unfortunately, work on this vaccine was discontinued because it had side effects in animal models that prevented its testing in humans. Currently, there are over 300 therapies in development that are intended to prevent the spread of the virus and end the pandemic (). These efforts to create a vaccine or a potent inhibitor that can be used as an a posteriori medical treatment with acceptable side-effects are being undertaken by both private companies and academic institutions. Both viral and host proteins are being targeted. While most efforts are focused on disrupting the viral protease or viral polymerase, the viral genome is also being targeted with the aim of disrupting its replication. In particular, the host enzymes involved in nucleotide synthesis are being studied with the aim of halting the final step in viral genome replication. However, most therapies in development target proteins acting upstream of replication; there are almost 40 preclinical and over 30 clinical trials targeting viral surface proteins including the s-glycoprotein. Several host cell membrane proteins are also being targeted, including CD147 and TMPRSS2 and, most importantly, ACE-2. When the SARS-CoV-2 enters the body, s-glycoprotein units on the surface of the virus act as "hooks", triggering attachment to a host cell. The s-glycoprotein is homo-trimer with three domainsthe cytoplasmic tail, the transmembrane region, and most importantly, the ectodomain. The ectodomain is further divided into three areas: the proximal membrane region, the S2 subunit, and at the top, the S1 subunit. The receptor-binding domain is located in the S1 subunit. ACE-2 recognises the S1 subunit, and between 1 and 3 s-glycoprotein monomers can bind to ACE-2 by opening and moving upwards. Before the s-glycoprotein/ACE-2 binding event, the covalent bond between subunits S1 and S2 is primed for cleavage to permit the displacement of the S1 subunit. The viral membrane then fuses with that of the host cell via a series of substantial conformational changes.