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Journal of Clinical Microbiology, July 1998, p. 2046-2051, Vol. 36, No. 7
0095-1137/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The L1 Major Capsid Protein of Human Papillomavirus Type 16 Variants Affects Yield of Virus-Like Particles Produced in an
Insect Cell Expression System
Antoine
Touze,1
Slimane
El Mehdaoui,1,2
Pierre-Yves
Sizaret,3
Christine
Mougin,4
Nubia
Muñoz,5 and
Pierre
Coursaget1,*
Institut de Virologie de Tours and CJF INSERM
93/09 Immunologie des Maladies Infectieuses, UFR des Sciences
Pharmaceutiques "Philippe Maupas," 37200 Tours,1
Laboratoire de Microscopie
Electronique, Faculté de Médecine de Tours, 37000 Tours,3
Laboratoire de Virologie,
Faculté de Médecine et de Pharmacie, 25000 Besançon,4 and
International
Agency for Research on Cancer, 69372 Lyon Cedex
2,5 France, and
Laboratoire de
Biologie Moléculaire, Université des Sciences et de la
Technologie "H. Boumedienne," BP 32, El-Alia,
Algeria2
Received 16 October 1997/Returned for modification 9 March
1998/Accepted 2 April 1998
The L1 major capsid proteins of six human papillomavirus type 16 (HPV-16) strains were expressed in insect cells by using recombinant
baculoviruses. Virus-like particles (VLPs) which appeared similar to
empty virions were identified by electron microscopy for all HPV
strains investigated. However, the yield of VLPs produced varied in a
range from 1 to 79 depending on the HPV-16 strain. The L1 proteins of
these strains differed by up to 15 amino acids from the L1 protein of
the prototype HPV-16 strain. Mutations in the amino acid region from
residues 83 to 97 seemed to affect the level of expression of the L1
protein. These results are important when considering the development
of HPV vaccines and serological tests. They indicate that strains
inducing high levels of VLP production must be selected for the
development of vaccines. Moreover, the L1 proteins of all strains
investigated were able to bind with DNA. We also investigated the
seroreactivities of VLPs derived from three different HPV-16 strains
from Algeria, Senegal, and the Philippines by testing sera from women
from 11 countries in immunoglobulin G-specific enzyme-linked
immunosorbent assays. We observed a strong correlation between the
reactivities of the three different VLP variants, independent of the
geographical origin of the sera investigated. These results indicate
that the three strains investigated are serologically cross-reactive
despite the fact that their L1 proteins differ in 14 amino acids and
suggest that VLPs derived from only one HPV-16 strain could be
sufficient for the development of an HPV-16 vaccine and anti-HPV-16
tests.
*
Corresponding author. Mailing address: Faculté
des Sciences Pharmaceutiques, 31 avenue Monge, 37200 Tours, France.
Phone: 33.247.36.71.89. Fax: 33.247.36.71.88. E-mail:
coursaget{at}univ-tours.fr.
Journal of Clinical Microbiology, July 1998, p. 2046-2051, Vol. 36, No. 7
0095-1137/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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