Disassembly and reassembly improves morphology and thermal stability of human papillomavirus type 16 virus-like particles

2012 ◽  
Vol 8 (7) ◽  
pp. 1182-1189 ◽  
Author(s):  
Qinjian Zhao ◽  
Michael J. Allen ◽  
Yang Wang ◽  
Bei Wang ◽  
Ning Wang ◽  
...  
1993 ◽  
Vol 67 (12) ◽  
pp. 6929-6936 ◽  
Author(s):  
R Kirnbauer ◽  
J Taub ◽  
H Greenstone ◽  
R Roden ◽  
M Dürst ◽  
...  

2018 ◽  
Vol 10 (7) ◽  
pp. 6137-6145 ◽  
Author(s):  
Ding-Yi Fu ◽  
Simin Zhang ◽  
Zhiyu Qu ◽  
Xianghui Yu ◽  
Yuqing Wu ◽  
...  

2006 ◽  
Vol 72 (1) ◽  
pp. 745-752 ◽  
Author(s):  
Karina Araujo Aires ◽  
Aurora Marques Cianciarullo ◽  
Sylvia Mendes Carneiro ◽  
Luisa Lina Villa ◽  
Enrique Boccardo ◽  
...  

ABSTRACT Infections with human papillomavirus type 16 (HPV-16) are closely associated with the development of human cervical carcinoma, which is one of the most common causes of cancer death in women worldwide. At present, the most promising vaccine against HPV-16 infection is based on the L1 major capsid protein, which self-assembles in virus-like particles (VLPs). In this work, we used a lactose-inducible system based on the Lactobacillus casei lactose operon promoter (plac) for expression of the HPV-16 L1 protein in L. casei. Expression was confirmed by Western blotting, and an electron microscopy analysis of L. casei expressing L1 showed that the protein was able to self-assemble into VLPs intracellularly. The presence of conformational epitopes on the L. casei-produced VLPs was confirmed by immunofluorescence using the anti-HPV-16 VLP conformational antibody H16.V5. Moreover, sera from mice that were subcutaneously immunized with L. casei expressing L1 reacted with Spodoptera frugiperda-produced HPV-16 L1 VLPs, as determined by an enzyme-linked immunosorbent assay. The production of L1 VLPs by Lactobacillus opens the possibility for development of new live mucosal prophylactic vaccines.


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