% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Luczak:827031,
      author       = {Luczak, Sören E. T. and Smits, Sander H. J. and Decker,
                      Christina and Nagel-Steger, Luitgard and Schmitt, Lutz and
                      Hegemann, Johannes H.},
      title        = {{T}he {C}hlamydia pneumoniae {A}dhesin {P}mp21 {F}orms
                      {O}ligomers with {A}dhesive {P}roperties},
      journal      = {The journal of biological chemistry},
      volume       = {291},
      number       = {43},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2017-01237},
      pages        = {22806-22818},
      year         = {2016},
      abstract     = {Chlamydiae sp. are obligate intracellular pathogens that
                      cause a variety of diseases in humans. The adhesion of
                      Chlamydiae to the eukaryotic host cell is a pivotal step in
                      pathogenesis. The adhesin family of polymorphic membrane
                      proteins (Pmp) in Chlamydia pneumoniae consists of 21
                      members. Pmp21 binds to the epidermal growth factor receptor
                      (EGFR). Pmps contain large numbers of FXXN (where X is any
                      amino acid) and GGA(I/L/V) motifs. At least two of these
                      motifs are crucial for adhesion by certain Pmp21 fragments.
                      Here we describe how the two FXXN motifs in Pmp21-D (D-Wt),
                      a domain of Pmp21, influence its self-interaction, folding,
                      and adhesive capacities. Refolded D-Wt molecules form
                      oligomers with high sedimentation values (8–85 S). These
                      oligomers take the form of elongated protofibrils, which
                      exhibit Thioflavin T fluorescence, like the amyloid protein
                      fragment β42. A mutant version of Pmp21-D (D-Mt), with FXXN
                      motifs replaced by SXXV, shows a markedly reduced capacity
                      to form oligomers. Secondary-structure assays revealed that
                      monomers of both variants exist predominantly as random
                      coils, whereas the oligomers form predominantly β-sheets.
                      Adhesion studies revealed that oligomers of D-Wt (D-Wt-O)
                      mediate significantly enhanced binding to human epithelial
                      cells relative to D-Mt-O and monomeric protein species.
                      Moreover, D-Wt-O binds EGFR more efficiently than D-Wt
                      monomers. Importantly, pretreatment of human cells with
                      D-Wt-O reduces infectivity upon subsequent challenge with C.
                      pneumoniae more effectively than all other protein species.
                      Hence, the FXXN motif in D-Wt induces the formation of
                      β-sheet-rich oligomeric protofibrils, which are important
                      for adhesion to, and subsequent infection of human cells.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000386760600037},
      pubmed       = {pmid:27551038},
      doi          = {10.1074/jbc.M116.728915},
      url          = {https://juser.fz-juelich.de/record/827031},
}