Self-assembly of human papillomavirus type 16 capsids by expression of the L1 protein in insect cells.
The L1 major protein of human papillomavirus type 16 was expressed in Sf-21 insect cells with a recombinant baculovirus vector. Virus-like particles similar in appearance to empty virions were identified by electron microscopy at densities of 1.29-1.30. Purified particles reacted with monoclonal anti-HPV-16-L1 antibody in Western blot and immuno dot blot suggesting that conformational epitopes are present in the recombinant particles. Immunodot blot assays using human sera correlated with the detection of HPV-16 DNA by the polymerase chain reaction. The results suggest that HPV-16-L1 virions produced by the baculovirus system might be useful for developing serologic tests to measure antibodies to conformational epitopes and may offer potential for vaccine development.
Le Cann
P
P
Institut de Virologie de Tours, Faculté de Pharmacie, France.
Coursaget
P
P
Iochmann
S
S
Touze
A
A
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D016367:Baculoviridae / Q000235:genetics; D001483:Base Sequence; D002213:Capsid / Q000032:analysis / Q000096:biosynthesis* / Q000276:immunology; D006801:Humans; D008969:Molecular Sequence Data; D009036:Moths; D027383:Papillomaviridae / Q000737:chemistry*; D011994:Recombinant Proteins / Q000096:biosynthesis*
D000911:Antibodies, Monoclonal; D011994:Recombinant Proteins