Molecular basis of bacterial lectin recognition of eukaryotic glycans : The case of Mycoplasma pneumoniae and Mycoplasma genitalium cytoadhesins
Marseglia, Angela (University of Naples Federico II)
Forgione, Maria Concetta (University of Naples Federico II)
Marcos Silva, Marina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Di Carluccio, Cristina (University of Naples Federico II)
Manabe, Yoshiyuki (Osaka University)
Vizarraga, David (Institut de Biologia Molecular de Barcelona)
Nieto-Fabregat, Ferran (University of Naples Federico II)
Lenza, Maria Pia (University of Naples Federico II)
Fukase, Koichi (Osaka University)
Molinaro, Antonio (Osaka University)
Quijada Pich, Oscar (Parc Taulí Hospital Universitari. Institut d'Investigació i Innovació Parc Taulí (I3PT))
Aparicio, David (Institute for Research in Biomedicine)
Silipo, Alba (Osaka University)
Marchetti, Roberta (University of Naples Federico II)
Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular

Date:	2024
Abstract:	Mycoplasma pneumoniae and Mycoplasma genitalium are two emerging bacterial pathogens that colonize the human respiratory and urogenital epithelia, respectively. Both pathogens express cell surface cytoadhesins that play a crucial role in the interaction with the host, mediating the attachment to sialylated glycan receptors and triggering infection. The design of competitive binding inhibitors of Mycoplasma cytoadhesins has potential to disrupt these interactions and lessen bacterial pathogenesis. To this end, we report here molecular insights into the adhesion mechanisms of M. pneumoniae and M. genitalium, which are largely mediated by sialylated glycans on the host cell surface. In detail, a combination of Nuclear Magnetic Resonance (NMR) spectroscopy, fluorescence analysis and computational studies allowed us to explore the recognition by the cytoadhesins P40/P90 in M. pneumoniae and P110 in M. genitalium of sialylated N- and O-glycans. We reveal that, unlike other bacterial adhesins, which are characterized by a wide binding pocket, Mycoplasma cytoadhesins principally accommodate the sialic acid residue, in a similar manner to mammalian Siglecs. These findings represent crucial insight into the future development of novel compounds to counteract Mycoplasma infections by inhibiting bacterial adherence to host tissues.
Grants:	European Commission 851356
Rights:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades.
Language:	Anglès
Document:	Article ; recerca ; Versió publicada
Subject:	Bacterial lectins ; Sialoglycans ; Molecular recognition ; STD NMR
Published in:	International journal of biological macromolecules, Vol. 279, Part 2 (November 2024) , art. 135277, ISSN 1879-0003

DOI: 10.1016/j.ijbiomac.2024.135277

13 p, 11.1 MB

The record appears in these collections:
Research literature > UAB research groups literature > Research Centres and Groups (research output) > Health sciences and biosciences > Parc Taulí Research and Innovation Institute (I3PT
Research literature > UAB research groups literature > Research Centres and Groups (research output) > Health sciences and biosciences > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Research articles
Articles > Published articles