KOPS - Das Institutionelle Repositorium der Universität Konstanz

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

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

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:0dbeac69e3995837bd37191a3665d458

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

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

Roth, Alexandra Roth, Alexandra 2012-01-03T17:19:23Z 2012-01-03T17:19:23Z Hauck, Christof 2011 Background<br />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.<br /><br />Principal Findings<br />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.<br /><br />Conclusions<br />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. Publ. in: PloS ONE ; 6 (2011), 1. - e14609 Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1 Küspert, Katharina eng deposit-license Küspert, Katharina Hauck, Christof

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

Kuespert_168302.pdf 152

Das Dokument erscheint in:

KOPS Suche


Stöbern

Mein Benutzerkonto