Expression of the major capsid protein of human papillomavirus type 16 in Escherichia coli

1995 ◽  
Vol 53 (1) ◽  
pp. 75-90 ◽  
Author(s):  
S.R. Kelsall ◽  
J.K. Kulski
Keyword(s):  
Escherichia Coli ◽  
Human Papillomavirus ◽  
Capsid Protein ◽  
Major Capsid Protein ◽  
Human Papillomavirus Type 16

Expression of Human Papillomavirus Type 16 Major Capsid Protein L1 in Transgenic Arabidopsis thaliana

2007 ◽  
Vol 25 (3-4) ◽  
pp. 133-144 ◽  
Author(s):  
Sonia M’hirsi El Adab ◽  
Aymen Ezzine ◽  
Iness Ben Khedija ◽  
Lotfi Chouchane ◽  
Mohamed Nejib Marzouki
Keyword(s):  
Arabidopsis Thaliana ◽  
Human Papillomavirus ◽  
Capsid Protein ◽  
Major Capsid Protein ◽  
Transgenic Arabidopsis ◽  
Human Papillomavirus Type 16 ◽  
Transgenic Arabidopsis Thaliana

scholarly journals Identification of a Human Papillomavirus Type 16-Specific Epitope on the C-Terminal Arm of the Major Capsid Protein L1

2003 ◽  
Vol 77 (21) ◽  
pp. 11625-11632 ◽  
Author(s):  
Joseph J. Carter ◽  
Greg C. Wipf ◽  
Sarah F. Benki ◽  
Neil D. Christensen ◽  
Denise A. Galloway
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibodies ◽  
Human Papillomavirus ◽  
Binding Site ◽  
Capsid Protein ◽  
Major Capsid Protein ◽  
Molecular Model ◽  
Hpv 16 ◽  
Human Papillomavirus Type 16 ◽  
Antibody Binding Site

ABSTRACT To characterize epitopes on human papillomavirus (HPV) virus-like particles (VLPs), a panel of mutated HPV-16 VLPs was created. Each mutated VLP had residues substituted from HPV-31 or HPV-52 L1 sequences to the HPV-16 L1 backbone. Mutations were created on the HPV-31 and −52 L1 proteins to determine if HPV-16 type-specific recognition could be transferred. Correct folding of the mutated proteins was verified by resistance to trypsin digestion and by binding to one or more conformation-dependent monoclonal antibodies. Several of the antibodies tested were found to bind to regions already identified as being important for HPV VLP recognition (loops DE, EF, FG, and HI). Sequences at both ends of the long FG loop (amino acids 260 to 290) were required for both H16.V5 and H16.E70 reactivity. A new antibody-binding site was discovered on the C-terminal arm of L1 between positions 427 and 445. Recognition of these residues by the H16.U4 antibody suggests that this region is surface exposed and supports a recently proposed molecular model of HPV VLPs.

Mapping the B cell epitopes within the major capsid protein L1 of human papillomavirus type 16

2018 ◽  
Vol 118 ◽  
pp. 1354-1361 ◽  
Author(s):  
Aiping Wang ◽  
Ning Li ◽  
Jingming Zhou ◽  
Yumei Chen ◽  
Min Jiang ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
B Cell ◽  
Capsid Protein ◽  
Major Capsid Protein ◽  
B Cell Epitopes ◽  
Human Papillomavirus Type 16
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