Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium

David Aparicio, Margot P. Scheffer, Marina Marcos-Silva, David Vizarraga, Lasse Sprankel, Mercè Ratera, Miriam S. Weber, Anja Seybert, Sergi Torres-Puig, Luis Gonzalez-Gonzalez, Julian Reitz, Enrique Querol, Jaume Piñol, Oscar Q. Pich (), Ignacio Fita () and Achilleas S. Frangakis ()
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David Aparicio: Parc Científic de Barcelona
Margot P. Scheffer: Buchmann Institute for Molecular Life Sciences
Marina Marcos-Silva: Universitat Autònoma de Barcelona
David Vizarraga: Parc Científic de Barcelona
Lasse Sprankel: Buchmann Institute for Molecular Life Sciences
Mercè Ratera: Parc Científic de Barcelona
Miriam S. Weber: Buchmann Institute for Molecular Life Sciences
Anja Seybert: Buchmann Institute for Molecular Life Sciences
Sergi Torres-Puig: Universitat Autònoma de Barcelona
Luis Gonzalez-Gonzalez: Universitat Autònoma de Barcelona
Julian Reitz: Buchmann Institute for Molecular Life Sciences
Enrique Querol: Universitat Autònoma de Barcelona
Jaume Piñol: Universitat Autònoma de Barcelona
Oscar Q. Pich: Universitat Autònoma de Barcelona
Ignacio Fita: Parc Científic de Barcelona
Achilleas S. Frangakis: Buchmann Institute for Molecular Life Sciences

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Mycoplasma genitalium is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110. By cryo-electron microscopy (cryo-EM) and tomography (cryo-ET) we find closed and open Nap conformations, determined at 9.8 and 15 Å, respectively. Both crystal structures and the cryo-EM structure are found in a closed conformation, where the sialic acid binding site in P110 is occluded. By contrast, the cryo-ET structure shows an open conformation, where the binding site is accessible. Structural information, in combination with functional studies, suggests a mechanism for attachment and release of M. genitalium to and from the host cell receptor, in which Nap conformations alternate to sustain motility and guarantee infectivity.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16511-2

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DOI: 10.1038/s41467-020-16511-2

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