Post translational modifications of recombinant human Papillomavirus type 6b major capsid protein


Autoria(s): Fang, Ning-Xia; Frazer, Ian H.; Zhou, Jian; Fernando, Germain J. P.
Data(s)

01/04/1999

Resumo

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. (C) 1999 Elsevier Science B.V. All rights reserved.

Identificador

http://espace.library.uq.edu.au/view/UQ:35633

Idioma(s)

eng

Publicador

Elsevier Science B.V.

Palavras-Chave #Virology #Phosphorylation #Myristoylation #Palmitoylation #Glycosylation #Vaccine #Virus-like Particles #L1 Protein #Bovine Papillomavirus #Vaccinia Virus #Insect Cells #E7 Protein #B-epitopes #Expression #Antibodies #Phosphorylation #C1 #320305 Medical Biochemistry - Proteins and Peptides #321202 Epidemiology
Tipo

Journal Article