HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 19, 18562-18567, May 13, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/19/18562    most recent M500490200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hari-Dass, R. Articles by Raynes, J. G. Search for Related Content PubMed PubMed Citation Articles by Hari-Dass, R. Articles by Raynes, J. G. Social Bookmarking                      What's this?

Serum Amyloid A Protein Binds to Outer Membrane Protein A of Gram-negative Bacteria^*

Ranjeeta Hari-Dass, Chandrabala Shah, David J. Meyer, and John G. Raynes

From the Immunology Unit, Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom

Serum amyloid A (SAA) is the major acute phase protein in man and most mammals. We observed SAA binding to a surprisingly large number of Gram-negative bacteria, including Escherichia coli, Salmonella typhimurium, Shigella flexneri, Klebsiella pneumoniae, Vibrio cholerae, and Pseudomonas aeruginosa. The binding was found to be high affinity and rapid. Importantly, this binding was not inhibited by high density lipoprotein with which SAA is normally complexed in serum. Binding was also observed when bacteria were offered serum containing SAA. Ligand blots following SDS-PAGE or two-dimensional gels revealed two major ligands of 29 and 35 kDa that bound SAA when probing with radiolabeled SAA or SAA and monoclonal anti-SAA. Following fractionation the ligand was found in the outer membrane fraction of E. coli and was identified by matrix-assisted laser desorption ionization time-of-flight mass spectrometry to be outer membrane protein A (OmpA). OmpA-deficient E. coli did not bind SAA, and following purification of OmpA the protein retained binding activity. The ligands on other bacteria were likely to be homologues of OmpA because wild type, but not OprF-deficient, P. aeruginosa bound SAA.

Received for publication, January 14, 2005

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a Medical Research Council studentship.

To whom correspondence should be addressed. Tel.: 44-20-7927-2355; Fax: 44-20-7323-5687; E-mail: john.raynes{at}lshtm.ac.uk.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				W. Hu, S. Abe-Dohmae, M. Tsujita, N. Iwamoto, O. Ogikubo, T. Otsuka, Y. Kumon, and S. Yokoyama Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo J. Lipid Res., February 1, 2008; 49(2): 386 - 393. [Abstract] [Full Text] [PDF]

				L. Bjorkman, J. Karlsson, A. Karlsson, M.-J. Rabiet, F. Boulay, H. Fu, J. Bylund, and C. Dahlgren Serum amyloid A mediates human neutrophil production of reactive oxygen species through a receptor independent of formyl peptide receptor like-1 J. Leukoc. Biol., February 1, 2008; 83(2): 245 - 253. [Abstract] [Full Text] [PDF]

				N. Zhang, Q. A. Truong-Tran, B. Tancowny, K. E. Harris, and R. P. Schleimer Glucocorticoids Enhance or Spare Innate Immunity: Effects in Airway Epithelium Are Mediated by CCAAT/Enhancer Binding Proteins J. Immunol., July 1, 2007; 179(1): 578 - 589. [Abstract] [Full Text] [PDF]

				Z. Cai, L. Cai, J. Jiang, K.-S. Chang, D. R. van der Westhuyzen, and G. Luo Human Serum Amyloid A Protein Inhibits Hepatitis C Virus Entry into Cells J. Virol., June 1, 2007; 81(11): 6128 - 6133. [Abstract] [Full Text] [PDF]

				H. Cai, C. Song, I. Endoh, J. Goyette, W. Jessup, S. B. Freedman, H. P. McNeil, and C. L. Geczy Serum Amyloid A Induces Monocyte Tissue Factor J. Immunol., February 1, 2007; 178(3): 1852 - 1860. [Abstract] [Full Text] [PDF]

				M. Guillier, S. Gottesman, and G. Storz Modulating the outer membrane with small RNAs Genes & Dev., September 1, 2006; 20(17): 2338 - 2348. [Abstract] [Full Text] [PDF]

				C. Shah, R. Hari-Dass, and J. G. Raynes Serum amyloid A is an innate immune opsonin for Gram-negative bacteria Blood, September 1, 2006; 108(5): 1751 - 1757. [Abstract] [Full Text] [PDF]

				S. Abe-Dohmae, K. H. Kato, Y. Kumon, W. Hu, H. Ishigami, N. Iwamoto, M. Okazaki, C.-A. Wu, M. Tsujita, K. Ueda, et al. Serum amyloid A generates high density lipoprotein with cellular lipid in an ABCA1- or ABCA7-dependent manner J. Lipid Res., July 1, 2006; 47(7): 1542 - 1550. [Abstract] [Full Text] [PDF]

				P. D. Eckersall, F. J. Young, A. M. Nolan, C. H. Knight, C. McComb, M. M. Waterston, C. J. Hogarth, E. M. Scott, and J. L. Fitzpatrick Acute Phase Proteins in Bovine Milk in an Experimental Model of Staphylococcus aureus Subclinical Mastitis J Dairy Sci, May 1, 2006; 89(5): 1488 - 1501. [Abstract] [Full Text] [PDF]