The SARS-CoV-2 outbreak originated in China in late 2019 and has since spread to pandemic proportions . Diagnostics, therapeutics and vaccines are urgently needed . We model the trimeric Spike protein, including flexible loops and all N-glycosylation sites, in order to elucidate accessible epitopes for antibody-based diagnostics, therapeutics and vaccine development . Based on published experimental data, six homogeneous glycosylation patterns and two heterogeneous ones were used for the analysis . The glycan chains alter the accessible surface areas on the S-protein, impeding antibody-antigen recognition . In presence of glycan, epitopes on the S1 subunit, that notably contains the receptor binding domain, remain mostly accessible to antibodies while those present on the S2 subunit are predominantly inaccessible . We identify 28 B-cell epitopes in the Spike structure and group them as non-affected by the glycan cloud versus those which are strongly masked by the glycan cloud, resulting in a list of favourable epitopes as targets for vaccine development, antibody-based therapy and diagnostics.