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@ARTICLE{Tamburini:285067,
      author       = {S. Tamburini and Y. Zhang$^*$ and A. Gagliardi and G. Di
                      Lascio and E. Caproni and M. Benedet and M. Tomasi and R.
                      Corbellari and I. Zanella and L. Croia and G. Grandi and M.
                      Müller$^*$ and A. Grandi},
      title        = {{B}acterial {O}uter {M}embrane {V}esicles as a {P}latform
                      for the {D}evelopment of a {B}roadly {P}rotective {H}uman
                      {P}apillomavirus {V}accine {B}ased on the {M}inor {C}apsid
                      {P}rotein {L}2.},
      journal      = {Vaccines},
      volume       = {11},
      number       = {10},
      issn         = {2076-393X},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {DKFZ-2023-02210},
      pages        = {1582},
      year         = {2023},
      abstract     = {Human papillomaviruses (HPVs) are a large family of viruses
                      with a capsid composed of the L1 and L2 proteins, which bind
                      to receptors of the basal epithelial cells and promote virus
                      entry. The majority of sexually active people become exposed
                      to HPV and the virus is the most common cause of cervical
                      cancer. Vaccines are available based on the L1 protein,
                      which self-assembles and forms virus-like particles (VLPs)
                      when expressed in yeast and insect cells. Although very
                      effective, these vaccines are HPV type-restricted and their
                      costs limit broad vaccination campaigns. Recently, vaccine
                      candidates based on the conserved L2 epitope from serotypes
                      16, 18, 31, 33, 35, 6, 51, and 59 were shown to elicit
                      broadly neutralizing anti-HPV antibodies. In this study, we
                      tested whether E. coli outer membrane vesicles (OMVs) could
                      be successfully decorated with L2 polytopes and whether the
                      engineered OMVs could induce neutralizing antibodies. OMVs
                      represent an attractive vaccine platform owing to their
                      intrinsic adjuvanticity and their low production costs. We
                      show that strings of L2 epitopes could be efficiently
                      expressed on the surface of the OMVs and a polypeptide
                      composed of the L2 epitopes from serotypes 18, 33, 35, and
                      59 provided a broad cross-protective activity against a
                      large panel of HPV serotypes as determined using pseudovirus
                      neutralization assay. Considering the simplicity of the OMV
                      production process, our work provides a highly effective and
                      inexpensive solution to produce universal anti-HPV
                      vaccines.},
      keywords     = {HPV OMV based vaccine (Other) / OMV engineering (Other) /
                      broadly protective vaccine (Other) / human papillomavirus
                      (HPV) (Other) / minor capsid protein L2 (Other) / outer
                      membrane vesicle (OMV) (Other) / proteome minimized E. coli
                      (Other)},
      cin          = {F035},
      ddc          = {610},
      cid          = {I:(DE-He78)F035-20160331},
      pnm          = {316 - Infektionen, Entzündung und Krebs (POF4-316)},
      pid          = {G:(DE-HGF)POF4-316},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37896984},
      pmc          = {pmc:PMC10611245},
      doi          = {10.3390/vaccines11101582},
      url          = {https://inrepo02.dkfz.de/record/285067},
}