Post translational modifications of recombinant human papillomavirus type 6b major capsid protein.
We have determined the post-translational modifications of the major capsid protein, L1 of human papillomavirus (HPV) type 6b. Since this virus cannot be cultured in the laboratory to obtain sufficient material for a study, a recombinant L1 protein produced in a vaccinia virus expression system was used in this investigation. Our results show that this protein is phosphorylated at serine residues and is also glycosylated. No myristoylation or palmitoylation was detected. The fraction of L1 protein incorporated into virus-like particles was not glycosylated. Since recombinant L1 protein is a potential human vaccine candidate, knowledge of the post-translation modifications of this protein may prove useful for the design of anti-HPV vaccines.
Fang
N X
NX
Centre for Immunology and Cancer Research, University of Queensland Department of Medicine, Princess Alexandra Hospital, Brisbane, Australia.
Frazer
I H
IH
Zhou
J
J
Fernando
G J
GJ
D000818:Animals; D002213:Capsid / Q000235:genetics* / Q000378:metabolism; D002460:Cell Line; D006031:Glycosylation; D006801:Humans; D019814:Myristic Acid / Q000378:metabolism; D019308:Palmitic Acid / Q000378:metabolism; D027383:Papillomaviridae / Q000235:genetics*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014616:Vaccinia virus / Q000235:genetics; D014771:Virion / Q000378:metabolism
D011994:Recombinant Proteins; D019814:Myristic Acid; D019308:Palmitic Acid