The NSP8 forms a hexadecamer or heterotetramer with NSP7 that the NSP7-NSP8 complex may participate in viral replication by acting as a primase for Nsp12, the RNA-dependent RNA polymerase (RdRp). Interaction of NSP8 with NSP7appears to be conserved across the coronavirus family, making these proteins interesting drug targets. Alternatively, the NSP7-NSP8 complex may synthesize substantially longer products than oligonucleotide primers.

AIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQ

198 aa; 150 kDa