Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection
Abstract
Retinol plays a vital role in the immune response to infection, yet proteins that mediate retinol transport during infection have not been identified. Serum amyloid A (SAA) proteins are strongly induced in the liver by systemic infection and in the intestine by bacterial colonization, but their exact functions remain unclear. Here we show that mouse and human SAAs are retinol binding proteins. Mouse and human SAAs bound retinol with nanomolar affinity, were associated with retinol in vivo, and limited the bacterial burden in tissues after acute infection. We determined the crystal structure of mouse SAA3 at a resolution of 2 Å, finding that it forms a tetramer with a hydrophobic binding pocket that can accommodate retinol. Our results thus identify SAAs as a family of microbe-inducible retinol binding proteins, reveal a unique protein architecture involved in retinol binding, and suggest how retinol is circulated during infection.
- Authors:
-
- Univ. of Texas Southwestern Medical Center, Dallas, TX (United States). Dept. of Immunology
- New York Univ. (NYU), NY (United States). School of Medicine. The Kimmel Center for Biology and Medicine of the Skirball Inst. Molecular Pathogenesis Program
- Univ. of Texas Southwestern Medical Center, Dallas, TX (United States). Dept. of Biochemistry
- Univ. of Texas Southwestern Medical Center, Dallas, TX (United States). Dept. of Immunology; Univ. of Texas Southwestern Medical Center, Dallas, TX (United States). Howard Hughes Medical Inst.
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division; National Institutes of Health (NIH); National Cancer Institute (NCI)
- OSTI Identifier:
- 1628814
- Grant/Contract Number:
- AC02-06CH11357; R01 DK070855; T32 AI005284; Y1-CO-1020; Y1-GM-1104
- Resource Type:
- Accepted Manuscript
- Journal Name:
- eLife
- Additional Journal Information:
- Journal Volume: 3; Journal ID: ISSN 2050-084X
- Publisher:
- eLife Sciences Publications, Ltd.
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Life Sciences & Biomedicine - Other Topics
Citation Formats
Derebe, Mehabaw G., Zlatkov, Clare M., Gattu, Sureka, Ruhn, Kelly A., Vaishnava, Shipra, Diehl, Gretchen E., MacMillan, John B., Williams, Noelle S., and Hooper, Lora V. Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection. United States: N. p., 2014.
Web. doi:10.7554/elife.03206.
Derebe, Mehabaw G., Zlatkov, Clare M., Gattu, Sureka, Ruhn, Kelly A., Vaishnava, Shipra, Diehl, Gretchen E., MacMillan, John B., Williams, Noelle S., & Hooper, Lora V. Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection. United States. https://doi.org/10.7554/elife.03206
Derebe, Mehabaw G., Zlatkov, Clare M., Gattu, Sureka, Ruhn, Kelly A., Vaishnava, Shipra, Diehl, Gretchen E., MacMillan, John B., Williams, Noelle S., and Hooper, Lora V. Tue .
"Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection". United States. https://doi.org/10.7554/elife.03206. https://www.osti.gov/servlets/purl/1628814.
@article{osti_1628814,
title = {Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection},
author = {Derebe, Mehabaw G. and Zlatkov, Clare M. and Gattu, Sureka and Ruhn, Kelly A. and Vaishnava, Shipra and Diehl, Gretchen E. and MacMillan, John B. and Williams, Noelle S. and Hooper, Lora V.},
abstractNote = {Retinol plays a vital role in the immune response to infection, yet proteins that mediate retinol transport during infection have not been identified. Serum amyloid A (SAA) proteins are strongly induced in the liver by systemic infection and in the intestine by bacterial colonization, but their exact functions remain unclear. Here we show that mouse and human SAAs are retinol binding proteins. Mouse and human SAAs bound retinol with nanomolar affinity, were associated with retinol in vivo, and limited the bacterial burden in tissues after acute infection. We determined the crystal structure of mouse SAA3 at a resolution of 2 Å, finding that it forms a tetramer with a hydrophobic binding pocket that can accommodate retinol. Our results thus identify SAAs as a family of microbe-inducible retinol binding proteins, reveal a unique protein architecture involved in retinol binding, and suggest how retinol is circulated during infection.},
doi = {10.7554/elife.03206},
journal = {eLife},
number = ,
volume = 3,
place = {United States},
year = {Tue Jul 29 00:00:00 EDT 2014},
month = {Tue Jul 29 00:00:00 EDT 2014}
}
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