Journal Article

PUBDB-2024-05760

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The Chlamydia pneumoniae effector SemD exploits its host’s endocytic machinery by structural and functional mimicry

Kocher, F. ; Applegate, V. ; Reiners, J. ; Port, A. ; Spona, D. ; Hänsch, S. ; Mirzaiebadizi, A. ; Ahmadian, M. R. ; Smits, S. H. J. ; Hegemann, J. H. (Corresponding author) ; Mölleken, K.

2024
Nature Publishing Group UK [London]

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Please use a persistent id in citations: doi:10.1038/s41467-024-51681-3  doi:10.3204/PUBDB-2024-05760

Abstract: To enter epithelial cells, the obligate intracellular pathogen Chlamydia pneumoniae secretes early effector proteins, which bind to and modulate the host-cell’s plasma membrane and recruit several pivotal endocytic host proteins. Here, we present the high-resolution structure of an entry-related chlamydial effector protein, SemD. Co-crystallisation of SemD with its host binding partners demonstrates that SemD co-opts the Cdc42 binding site to activate the actin cytoskeleton regulator N-WASP, making active, GTP-bound Cdc42 superfluous. While SemD binds N-WASP much more strongly than Cdc42 does, it does not bind the Cdc42 effector protein FMNL2, indicating effector protein specificity. Furthermore, by identifying flexible and structured domains, we show that SemD can simultaneously interact with the membrane, the endocytic protein SNX9, and N-WASP. Here, we show at the structural level how a single effector protein can hijack central components of the host’s endocytic system for efficient internalization.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)
2. DFG project 417919780 - Zentrum für strukturelle Studien (417919780) (417919780)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)
2. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2024

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