Fusobacterium nucleatum CbpF Mediates Inhibition of T Cell Function Through CEACAM1 Activation

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Fusobacterium nucleatum CbpF Mediates Inhibition of T Cell Function Through CEACAM1 Activation. / Galaski, Johanna; Shhadeh, Amjad; Umaña, Ariana; Yoo, Christopher C; Arpinati, Ludovica; Isaacson, Batya; Berhani, Orit; Singer, Bernhard B; Slade, Daniel J; Bachrach, Gilad; Mandelboim, Ofer.

in: FRONT CELL INFECT MI, Jahrgang 11, 07.2021, S. 692544.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Galaski, J, Shhadeh, A, Umaña, A, Yoo, CC, Arpinati, L, Isaacson, B, Berhani, O, Singer, BB, Slade, DJ, Bachrach, G & Mandelboim, O 2021, 'Fusobacterium nucleatum CbpF Mediates Inhibition of T Cell Function Through CEACAM1 Activation', FRONT CELL INFECT MI, Jg. 11, S. 692544. https://doi.org/10.3389/fcimb.2021.692544

APA

Galaski, J., Shhadeh, A., Umaña, A., Yoo, C. C., Arpinati, L., Isaacson, B., Berhani, O., Singer, B. B., Slade, D. J., Bachrach, G., & Mandelboim, O. (2021). Fusobacterium nucleatum CbpF Mediates Inhibition of T Cell Function Through CEACAM1 Activation. FRONT CELL INFECT MI, 11, 692544. https://doi.org/10.3389/fcimb.2021.692544

Vancouver

Bibtex

@article{82b6813cc01a466b9bda6702e539d331,
title = "Fusobacterium nucleatum CbpF Mediates Inhibition of T Cell Function Through CEACAM1 Activation",
abstract = "F. nucleatum is an anaerobic bacterium that is associated with several tumor entities and promotes tumorigenesis. Recent evidence suggests that F. nucleatum binds the inhibitory receptor carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1) via the trimeric autotransporter adhesin CbpF. However, whether this binding is functional or whether other fusobacterial trimeric autotransporter adhesins are involved in CEACAM1 activation is unknown. In this study, using F. nucleatum mutants lacking the type 5c trimeric autotransporter adhesins fvcA (CbpF), fvcB, fvcC, and fvcD, we show that F. nucleatum CbpF binds and activates CEACAM1 and also binds carcinoembryonic antigen (CEA), a tumor-associated protein. We further find that CEACAM antibodies directed against the CEACAM N-terminal domain block the CbpF-CEACAM1 interaction. In functional assays, we demonstrate CbpF-dependent inhibition of CD4+ T cell response. Thus, we characterize an immune evasion mechanism in which F. nucleatum uses its surface protein CbpF to inhibit T cell function by activating CEACAM1.",
author = "Johanna Galaski and Amjad Shhadeh and Ariana Uma{\~n}a and Yoo, {Christopher C} and Ludovica Arpinati and Batya Isaacson and Orit Berhani and Singer, {Bernhard B} and Slade, {Daniel J} and Gilad Bachrach and Ofer Mandelboim",
note = "Copyright {\textcopyright} 2021 Galaski, Shhadeh, Uma{\~n}a, Yoo, Arpinati, Isaacson, Berhani, Singer, Slade, Bachrach and Mandelboim.",
year = "2021",
month = jul,
doi = "10.3389/fcimb.2021.692544",
language = "English",
volume = "11",
pages = "692544",
journal = "FRONT CELL INFECT MI",
issn = "2235-2988",
publisher = "Frontiers Media S. A.",

}

RIS

TY - JOUR

T1 - Fusobacterium nucleatum CbpF Mediates Inhibition of T Cell Function Through CEACAM1 Activation

AU - Galaski, Johanna

AU - Shhadeh, Amjad

AU - Umaña, Ariana

AU - Yoo, Christopher C

AU - Arpinati, Ludovica

AU - Isaacson, Batya

AU - Berhani, Orit

AU - Singer, Bernhard B

AU - Slade, Daniel J

AU - Bachrach, Gilad

AU - Mandelboim, Ofer

N1 - Copyright © 2021 Galaski, Shhadeh, Umaña, Yoo, Arpinati, Isaacson, Berhani, Singer, Slade, Bachrach and Mandelboim.

PY - 2021/7

Y1 - 2021/7

N2 - F. nucleatum is an anaerobic bacterium that is associated with several tumor entities and promotes tumorigenesis. Recent evidence suggests that F. nucleatum binds the inhibitory receptor carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1) via the trimeric autotransporter adhesin CbpF. However, whether this binding is functional or whether other fusobacterial trimeric autotransporter adhesins are involved in CEACAM1 activation is unknown. In this study, using F. nucleatum mutants lacking the type 5c trimeric autotransporter adhesins fvcA (CbpF), fvcB, fvcC, and fvcD, we show that F. nucleatum CbpF binds and activates CEACAM1 and also binds carcinoembryonic antigen (CEA), a tumor-associated protein. We further find that CEACAM antibodies directed against the CEACAM N-terminal domain block the CbpF-CEACAM1 interaction. In functional assays, we demonstrate CbpF-dependent inhibition of CD4+ T cell response. Thus, we characterize an immune evasion mechanism in which F. nucleatum uses its surface protein CbpF to inhibit T cell function by activating CEACAM1.

AB - F. nucleatum is an anaerobic bacterium that is associated with several tumor entities and promotes tumorigenesis. Recent evidence suggests that F. nucleatum binds the inhibitory receptor carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1) via the trimeric autotransporter adhesin CbpF. However, whether this binding is functional or whether other fusobacterial trimeric autotransporter adhesins are involved in CEACAM1 activation is unknown. In this study, using F. nucleatum mutants lacking the type 5c trimeric autotransporter adhesins fvcA (CbpF), fvcB, fvcC, and fvcD, we show that F. nucleatum CbpF binds and activates CEACAM1 and also binds carcinoembryonic antigen (CEA), a tumor-associated protein. We further find that CEACAM antibodies directed against the CEACAM N-terminal domain block the CbpF-CEACAM1 interaction. In functional assays, we demonstrate CbpF-dependent inhibition of CD4+ T cell response. Thus, we characterize an immune evasion mechanism in which F. nucleatum uses its surface protein CbpF to inhibit T cell function by activating CEACAM1.

U2 - 10.3389/fcimb.2021.692544

DO - 10.3389/fcimb.2021.692544

M3 - SCORING: Journal article

C2 - 34336716

VL - 11

SP - 692544

JO - FRONT CELL INFECT MI

JF - FRONT CELL INFECT MI

SN - 2235-2988

ER -