COVID-19, caused by SARS-CoV-2 coronavirus, has become a grave threat to global public health in 2020, causing over a million deaths and prompting governments worldwide to enter lockdowns to control the pandemic. The SARS-CoV-2 spike protein acts as the ligand to bind with human ACE2 to mediate viral entry into host cells. Thus, specific antibodies that interfere with this process are useful in halting the infection. To identify SARS-CoV-2 specific epitopes, we collected the sera of 25 convalescent patients during the first wave of COVID-19 infection in Singapore and 13 donors who recovered from SARS-CoV (SARS) infection in 2003 for analysis. Sera from COVID-19 patients, but not recalled SARS patients, contain antibodies that neutralize pseudotyped lentivirus expressing the SARS-CoV-2 spike protein. Furthermore, we screened these sera against the peptide libraries spanning the spike protein of SARS-CoV-2 and uncovered two specific linear B cell epitopes, S14P5 and S21P2, that were recognized only by COVID-19 patient sera. S14P5 is situated close to the receptor-binding domain (RBD) while S21P2 overlaps with the fusion peptide sequence, suggesting that specific antibodies against these regions may be able to interfere with viral entry into host cells. Indeed, depleting antibodies that recognize S14P5 and S21P2 decreased neutralization capacity of sera against pseudotyped lentivirus expressing the SARS-CoV-2 spike protein. In conclusion, antibodies against S14P5 and S21P2 can interfere with viral entry into host cells and prevent infection, indicating that they have considerable therapeutic potential to be used in COVID-19 treatments.