Open AccessSelf‐assembly of human papillomavirus type 16 capsids by expression of the L1 protein in insect cells
Author(s) -
Cann Pierre Le,
Coursaget Pierre,
Iochmann Sophie,
Touze Antoine
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06778.x
Subject(s) - recombinant dna , epitope , capsid , western blot , monoclonal antibody , microbiology and biotechnology , virology , dot blot , virus , biology , blot , antibody , chemistry , dna , gene , biochemistry , immunology
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 verions were identified by electron microscoy 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.