Recently (2019), a novel coronavirus (SARS-CoV-2) first reported in Wuhan, China has been declared a pandemic by the World Health Organization and is rapidly spreading throughout the globe which is associated with high morbidity and mortality, especially in the elderly and those with existing chronic conditions. SARS-CoV-2 infects cells through interaction of its surface glycoprotein with the human angiotensin converting enzyme 2 (ACE-2). This study conducted a analysis of mutation frequency in the surface glycoprotein of 796 sequenced SARS-CoV-2 isolates from different geographical locations in the GISAID and GenBank databases. Multiple sequence alignment analysis of the surface glycoprotein identified 64 different mutations at the protein level spanning multiple geographic locations globally. A cluster of mutations was identified in the receptor binding domain (RBD) of the surface glycoprotein. Significantly, the analysis showed that 68.5% of the isolates contain a D614 residue compared to 31.5% which contain a G614 suggesting virus is spreading in two forms. Furthermore, our investigation found that one isolate from Belgium had acquired 5 cumulative mutations in the surface glycoprotein indicating possible antigenic drift. The findings of this study are of critical importance for the design of vaccines and novel drugs against this severe acute respiratory syndrome coronavirus.