Paneth cells secrete lysozyme via secretory autophagy during bacterial infection of the intestine

Science

Volumn 357, Issue 6355, 2017, Pages 1047-1052

  Bel, Shai ^a   Pendse, Mihir ^a   Wang, Yuhao ^a   Li, Yun ^a   Ruhn, Kelly A ^a   Hassell, Brian ^a   Leal, Tess ^a   Winter, Sebastian E ^b   Xavier, Ramnik J ^c,d   Hooper, Lora V ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c BROAD INSTITUTE OF MIT AND HARVARD   (United States)

^d MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; ATG16L1 PROTEIN, MOUSE; CARRIER PROTEIN; MAP1LC3 PROTEIN, MOUSE; MICROTUBULE ASSOCIATED PROTEIN;

ANTIMICROBIAL ACTIVITY; BACTERIUM; CELLS AND CELL COMPONENTS; ENZYME; ENZYME ACTIVITY; GENE; MUTATION; PATHOGEN; PROTEIN; SECRETION;

ARTICLE; ATG16L1 GENE; AUTOPHAGOSOME; AUTOPHAGY; CELLULAR SECRETION; CROHN DISEASE; ENDOPLASMIC RETICULUM STRESS; GENE; GENE MUTATION; HUMAN; IMMUNOFLUORESCENCE; INNATE IMMUNITY; INTRACELLULAR SIGNALING; LYMPHOID CELL; NONHUMAN; PANETH CELL; PRIORITY JOURNAL; SALMONELLA ENTERICA SEROVAR TYPHIMURIUM; TRANSMISSION ELECTRON MICROSCOPY; ANIMAL; C57BL MOUSE; ENZYMOLOGY; GENETICS; IMMUNOLOGY; METABOLISM; MICROBIOLOGY; MOUSE; MUTATION; SALMONELLA ENTERICA; SALMONELLOSIS; SECRETION (PROCESS);

BACTERIA (MICROORGANISMS); MUS;

ANIMALS; AUTOPHAGY; CARRIER PROTEINS; CROHN DISEASE; ENDOPLASMIC RETICULUM STRESS; MICE; MICE, INBRED C57BL; MICROTUBULE-ASSOCIATED PROTEINS; MURAMIDASE; MUTATION; PANETH CELLS; SALMONELLA ENTERICA; SALMONELLA INFECTIONS;

EID: 85026463382     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aal4677     Document Type: Article

References (19)

1. D. Ramanan, K. Cadwell, Cell Host Microbe 19, 434-441 (2016).
2. K. Cadwell et al., Nature 456, 259-263 (2008).
3. K. Cadwell et al., Cell 141, 1135-1145 (2010).
4. A. Kaser et al., Cell 134, 743-756 (2008).
5. J. Celli, R. M. Tsolis, Nat. Rev. Microbiol. 13, 71-82 (2015).
6. A. M. Keestra-Gounder et al., Nature 532, 394-397 (2016).
7. J. L. Benjamin, R. Sumpter Jr., B. Levine, L. V. Hooper, Cell Host Microbe 13, 723-734 (2013).
8. N. Mizushima, T. Yoshimori, B. Levine, Cell 140, 313-326 (2010).
9. M. Ponpuak et al., Curr. Opin. Cell Biol. 35, 106-116 (2015).
10. N. Dupont et al., EMBO J. 30, 4701-4711 (2011).
11. B. Khor, A. Gardet, R. J. Xavier, Nature 474, 307-317 (2011).
12. K. G. Lassen et al., Proc. Natl. Acad. Sci. U.S.A. 111, 7741-7746 (2014).
13. P. Escoll, S. Mondino, M. Rolando, C. Buchrieser, Nat. Rev. Microbiol. 14, 5-19 (2016).
14. A. M. Preston, E. Gurisik, C. Bartley, D. R. Laybutt, T. J. Biden, Diabetologia 52, 2369-2373 (2009).
15. X. Z. Wang et al., Mol. Cell. Biol. 16, 4273-4280 (1996).
16. C. M. Oslowski, F. Urano, Methods Enzymol. 490, 71-92 (2011).
17. T. E. Adolph et al., Nature 503, 272-276 (2013).
18. M. Boyce et al., Science 307, 935-939 (2005).
19. C. A. Thaiss, N. Zmora, M. Levy, E. Elinav, Nature 535, 65-74 (2016).