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Showing 1–3 of 3 results
Advanced filters: Author: Oscar Q. Pich Clear advanced filters

  • The adhesion complex (Nap) in Mycoplasma genitalium is composed of the adhesin proteins P110 and P140 and essential for infectivity, motility and adhesion of this human pathogen. Here, the author present the structures of P140 alone and the P140/P110 complex in closed and open conformations and based on their structural data and further functional studies propose a mechanism for the attachment and release of M. genitalium to the host cell receptor.

    • David Aparicio
    • Margot P. Scheffer
    • Achilleas S. Frangakis
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • How the Mycoplasma genitalium cytadhesins P140 and P110 promote host cell invasion remains poorly understood. Here, combining structural analysis with functional assays, Aparicio et al. identify the P110 domain that binds to sialylated receptors essential for mycoplasma cytadherence.

    • David Aparicio
    • Sergi Torres-Puig
    • Ignacio Fita
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11

  • Adhesion of the human pathogen Mycoplasma pneumoniae to pulmonary epithelial cells is mediated by a transmembrane complex composed of proteins P1 and P40/P90. Here, the authors present the structures of M. pneumoniae P1 and P40/P90, show that P40/P90 binds sialylated oligosaccharides and have also determined the crystal structures of P40/P90 complexes with 3’-Sialyllactose and 6’-Sialyllactose, which provide insights into the mechanisms of adhesion and gliding on host cell surfaces.

    • David Vizarraga
    • Akihiro Kawamoto
    • David Aparicio
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16