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Mucosal immune responses to microbes in genital tract
Published in Phillip D. Smith, Richard S. Blumberg, Thomas T. MacDonald, Principles of Mucosal Immunology, 2020
Carcinoembryonic antigen-related cell adhesion molecule 3 (CEACAM3) mediates the opsonin-independent recognition and elimination of a restricted set of human-specific gram-negative bacterial pathogens including N. gonorrhoeae. CEACAM3 binds to the Opa protein expressed by N. gonorrhoeae and internalizes the bacteria for degradation. N. gonorrhoeae expresses lipooligosaccharide, lacking the O antigen. This structure is recognized by TLR2, TLR4, and triggering receptor expressed on myeloid cells-2A (TREM-2A). In addition, porins and Lip lipoproteins of N. gonorrhoeae are recognized through TLR2.
Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF
Published in Journal of Oral Microbiology, 2019
Matthew L. Brewer, David Dymock, R. Leo Brady, Bernhard B. Singer, Mumtaz Virji, Darryl J. Hill
The CEACAM family belongs to the Immunoglobulin superfamily and include epithelial and polymorphonuclear cell-expressed members such as CEACAM1, CEACAM3, CEA, CEACAM6, and CEACAM8 whose distribution in tissues and functions may be divergent [20,21]. Of the cell surface-expressed members of the family, CEACAM1 (previously known as BGP and CD66a) has the broadest tissue distribution and is expressed on the apical surfaces of epithelial cells of human mucosa, cells of myeloid lineage as well as on some endothelial cells [20–22]. Focussing specifically on oral/respiratory tissues, CEACAM expression on normal epithelial cells in oral, tonsillar, and lung tissues has been reported [22–24]. We have demonstrated the expression of the receptor on the apical surfaces of tonsillar epithelium [25], where the receptor may be available for microbial colonisation. Since increased receptor density demonstrably increases the chances of cellular invasion by bacteria [26], these observations suggest that CEACAMs may play a critical role in mucosal colonisation and pathogenesis. CEACAM1, CEA, and CEACAM6 are expressed in human junctional epithelium [27]. However, whether other oro-respiratory bacterial colonisers/pathogens besides Nm, Hi, and Mx target CEACAMs has not been fully investigated.
T cell-mediated elimination of cancer cells by blocking CEACAM6–CEACAM1 interaction
Published in OncoImmunology, 2022
Jessica Pinkert, Hans-Henning Boehm, Mark Trautwein, Wolf-Dietrich Doecke, Florian Wessel, Yingzi Ge, Eva Maria Gutierrez, Rafael Carretero, Christoph Freiberg, Uwe Gritzan, Merlin Luetke-Eversloh, Sven Golfier, Oliver Von Ahsen, Valentina Volpin, Antonio Sorrentino, Anchana Rathinasamy, Maria Xydia, Robert Lohmayer, Julian Sax, Ayse Nur-Menevse, Abir Hussein, Slava Stamova, Georg Beckmann, Julian Marius Glueck, Dorian Schoenfeld, Joerg Weiske, Dieter Zopf, Rienk Offringa, Bertolt Kreft, Philipp Beckhove, Joerg Willuda
Recombinant human CEACAM1, −5, −6 proteins were purchased from R&D Systems, human CEACAM3 was obtained from Sino Biological. Other recombinant human or cynomolgus CEACAM6 variants including Fc fusions and domain variants were produced as described in the Supplementary Methods.