Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1

Küspert, Katharina; Roth, Alexandra; Hauck, Christof R.

Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1

Dateien

Kuespert_168302.pdfGröße: 795.33 KBDownloads: 390

Datum

2011

Autor:innen

Küspert, Katharina

Roth, Alexandra

Hauck, Christof R.

Open Access-Veröffentlichung

Open Access Gold, Open Access Gold

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

PLoS ONE. 2011, 6(1), e14609. eISSN 1932-6203. Available under: doi: 10.1371/journal.pone.0014609

Zusammenfassung

Background
Several human-restricted Gram-negative bacteria exploit carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) for host colonization. For example, Neisseria meningitidis engages these human receptors via outer membrane proteins of the colony opacity-associated (Opa) protein family triggering internalization into non-phagocytic cells.

Principal Findings
We report that a non-opaque strain of N. meningitidis selectively interacts with CEACAM1, but not other CEACAM family members. Using functional assays of bacterial adhesion and internalisation, microscopic analysis, and a panel of CEACAM1 deletion mutants we demonstrate that the engagement of CEACAM1 by non-opaque meningococci occurs in a manner distinct from Opa protein-mediated association. In particular, the amino-terminal domain of CEACAM1 is necessary, but not sufficient for Opa protein-independent binding, which requires multiple extracellular domains of the human receptor in a cellular context. Knock-down of CEACAM1 interferes with binding to lung epithelial cells, whereas chemical or pharmacological disruption of host protein glycosylation does not abrogate CEACAM1 recognition by non-opaque meningococci. The previously characterized meningococcal invasins NadA or Opc do not operate in a CEACAM1-dependent manner.

Conclusions
The results demonstrate a mechanistically distinct, Opa protein-independent interaction between N. meningitidis and human CEACAM1. Our functional investigations suggest the presence of a second CEACAM1-binding invasin on the meningococcal surface that associates with the protein backbone and not the carbohydrate structures of CEACAM1. The redundancy in meningococcal CEACAM1-binding factors further highlights the important role of CEACAM recognition in the biology of this human-adapted pathogen.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

KÜSPERT, Katharina, Alexandra ROTH, Christof R. HAUCK, 2011. Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1. In: PLoS ONE. 2011, 6(1), e14609. eISSN 1932-6203. Available under: doi: 10.1371/journal.pone.0014609

BibTex

@article{Kuspert2011Neiss-16830,
  year={2011},
  doi={10.1371/journal.pone.0014609},
  title={Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1},
  number={1},
  volume={6},
  journal={PLoS ONE},
  author={Küspert, Katharina and Roth, Alexandra and Hauck, Christof R.},
  note={Article Number: e14609}
}

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    <dcterms:abstract xml:lang="eng">Background&lt;br /&gt;Several human-restricted Gram-negative bacteria exploit carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) for host colonization. For example, Neisseria meningitidis engages these human receptors via outer membrane proteins of the colony opacity-associated (Opa) protein family triggering internalization into non-phagocytic cells.&lt;br /&gt;&lt;br /&gt;Principal Findings&lt;br /&gt;We report that a non-opaque strain of N. meningitidis selectively interacts with CEACAM1, but not other CEACAM family members. Using functional assays of bacterial adhesion and internalisation, microscopic analysis, and a panel of CEACAM1 deletion mutants we demonstrate that the engagement of CEACAM1 by non-opaque meningococci occurs in a manner distinct from Opa protein-mediated association. In particular, the amino-terminal domain of CEACAM1 is necessary, but not sufficient for Opa protein-independent binding, which requires multiple extracellular domains of the human receptor in a cellular context. Knock-down of CEACAM1 interferes with binding to lung epithelial cells, whereas chemical or pharmacological disruption of host protein glycosylation does not abrogate CEACAM1 recognition by non-opaque meningococci. The previously characterized meningococcal invasins NadA or Opc do not operate in a CEACAM1-dependent manner.&lt;br /&gt;&lt;br /&gt;Conclusions&lt;br /&gt;The results demonstrate a mechanistically distinct, Opa protein-independent interaction between N. meningitidis and human CEACAM1. Our functional investigations suggest the presence of a second CEACAM1-binding invasin on the meningococcal surface that associates with the protein backbone and not the carbohydrate structures of CEACAM1. The redundancy in meningococcal CEACAM1-binding factors further highlights the important role of CEACAM recognition in the biology of this human-adapted pathogen.</dcterms:abstract>
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