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@ARTICLE{Zhang:288564,
author = {Y. Zhang$^*$ and F. C. Mariz$^*$ and P. Sehr and G.
Spagnoli and K. M. Koenig$^*$ and S. Çelikyürekli$^*$ and
T. Kreuziger and X. Zhao$^*$ and A. Bolchi and S. Ottonello
and M. Müller$^*$},
title = {{I}nter-epitope spacer variation within polytopic
{L}2-based human papillomavirus antigens affects
immunogenicity.},
journal = {npj vaccines},
volume = {9},
number = {1},
issn = {2059-0105},
address = {[London]},
publisher = {Nature Publishing Group},
reportid = {DKFZ-2024-00410},
pages = {44},
year = {2024},
note = {#EA:F035#LA:F035# /NEU/ #EA:D335#LA:D335#},
abstract = {The human papillomavirus minor capsid protein L2 is being
extensively explored in pre-clinical studies as an
attractive vaccine antigen capable of inducing
broad-spectrum prophylactic antibody responses. Recently, we
have developed two HPV vaccine antigens - PANHPVAX and
CUT-PANHPVAX- both based on heptameric nanoparticle antigens
displaying polytopes of the L2 major cross-neutralizing
epitopes of eight mucosal and twelve cutaneous HPV types,
respectively. Prompted by the variable neutralizing antibody
responses against some of the HPV types targeted by the
antigens observed in previous studies, here we investigated
the influence on immunogenicity of six distinct
glycine-proline spacers inserted upstream to a specific L2
epitope. We show that spacer variants differentially
influence antigen immunogenicity in a mouse model, with the
antigen constructs M8merV6 and C12merV6 displaying a
superior ability in the induction of neutralizing antibodies
as determined by pseudovirus-based neutralization assays
(PBNAs). L2-peptide enzyme-linked immunosorbent assay
(ELISA) assessments determined the total anti-L2 antibody
level for each antigen variant, showing for the majority of
sera a correlation with their repective neutralizing
antibody level. Surface Plasmon Resonance revealed that L2
epitope-specific, neutralizing monoclonal antibodies (mAbs)
display distinct avidities to different antigen spacer
variants. Furthermore, mAb affinity toward individual spacer
variants was well correlated with their neutralizing
antibody induction capacity, indicating that the mAb
affinity assay predicts L2-based antigen immunogenicity.
These observations provide insights on the development and
optimization of L2-based HPV vaccines.},
cin = {F035 / D335},
ddc = {610},
cid = {I:(DE-He78)F035-20160331 / I:(DE-He78)D335-20160331},
pnm = {314 - Immunologie und Krebs (POF4-314)},
pid = {G:(DE-HGF)POF4-314},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:38402256},
doi = {10.1038/s41541-024-00832-0},
url = {https://inrepo02.dkfz.de/record/288564},
}