Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division

Martín Alcorlo, David A. Dik, Stefania Benedetti, Kiran V. Mahasenan, Mijoon Lee, Teresa Domínguez-Gil, Dusan Hesek, Elena Lastochkin, Daniel López, Bill Boggess, Shahriar Mobashery () and Juan A. Hermoso ()
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Martín Alcorlo: Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas
David A. Dik: University of Notre Dame, Notre Dame
Stefania Benedetti: University of Notre Dame, Notre Dame
Kiran V. Mahasenan: University of Notre Dame, Notre Dame
Mijoon Lee: University of Notre Dame, Notre Dame
Teresa Domínguez-Gil: Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas
Dusan Hesek: University of Notre Dame, Notre Dame
Elena Lastochkin: University of Notre Dame, Notre Dame
Daniel López: Spanish National Research Council (CNB-CSIC)
Bill Boggess: University of Notre Dame, Notre Dame
Shahriar Mobashery: University of Notre Dame, Notre Dame
Juan A. Hermoso: Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan is enriched in the septal ring as a product of catalysis by cell-wall amidases that participate in the separation of daughter cells during cell division. Here, we document binding of synthetic denuded glycan ligands to the SPOR domain of the lytic transglycosylase RlpA from Pseudomonas aeruginosa (SPOR-RlpA) by mass spectrometry and structural analyses, and demonstrate that indeed the presence of peptide stems in the peptidoglycan abrogates binding. The crystal structures of the SPOR domain, in the apo state and in complex with different synthetic glycan ligands, provide insights into the molecular basis for recognition and delineate a conserved pattern in other SPOR domains. The biological and structural observations presented here are followed up by molecular-dynamics simulations and by exploration of the effect on binding of distinct peptidoglycan modifications.

Date: 2019
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DOI: 10.1038/s41467-019-13354-4

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