| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
,
* Center for Pulmonary and Infectious Disease Control,
Department of Microbiology and Immunology,
Department of Medicine, and
Department of Biochemistry, Center for Biomedical Research, University of Texas Health Center, Tyler, TX 75708; and
¶ Department of Microbiology and Immunology, Faculty of Health Sciences, and Cancer Research Center, Ben Gurion University of the Negev, Beer Sheva, Israel
We previously showed that human NK cells used the NKp46 receptor to lyse Mycobacterium tuberculosis H37Ra-infected monocytes. To identify ligands on H37Ra-infected human mononuclear phagocytes, we used anti-NKp46 to immunoprecipitate NKp46 from NK cells bound to its ligand(s) on H37Ra-infected monocytes. Mass spectrometry analysis identified a 57-kDa molecule, vimentin, as a putative ligand for NKp46. Vimentin expression was significantly up-regulated on the surface of infected monocytes, compared with uninfected cells, and this was confirmed by fluorescence microscopy. Anti-vimentin antiserum inhibited NK cell lysis of infected monocytes, whereas antiserum to actin, another filamentous protein, did not. CHO-K1 cells transfected with a vimentin construct were lysed much more efficiently by NK cells than cells transfected with a control plasmid. This lysis was inhibited by mAb-mediated masking of NKp46 (on NK cells) or vimentin (on infected monocytes). ELISA and Far Western blotting showed that recombinant vimentin bound to a NKp46 fusion protein. These results indicate that vimentin is involved in binding of NKp46 to M. tuberculosis H37Ra-infected mononuclear phagocytes.
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.
1 This work was supported by National Institutes of Health Grants AI054629, AI044935, and A1063514, the Cain Foundation for Infectious Disease Research, and the Center for Pulmonary and Infectious Disease Control.
2 Address correspondence and reprint requests to Dr. Ramakrishna Vankayalapati, Center for Pulmonary and Infectious Disease Control, University of Texas Health Center, 11937 U.S. Highway 271, Tyler, TX 75708-3154. E-mail address: Krishna.vankayalapati{at}uthct.edu
3 Abbreviations used in this paper: HSPG, heparan sulfate proteoglycan; MOI, multiplicity of infection; MFI, mean fluorescence intensity.
This article has been cited by other articles:
|
|
 |
|
  S. Esin, G. Batoni, C. Counoupas, A. Stringaro, F. L. Brancatisano, M. Colone, G. Maisetta, W. Florio, G. Arancia, and M. Campa Direct Binding of Human NK Cell Natural Cytotoxicity Receptor NKp44 to the Surfaces of Mycobacteria and Other Bacteria Infect. Immun., April 1, 2008; 76(4): 1719 - 1727. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Lanemo Myhrinder, E. Hellqvist, E. Sidorova, A. Soderberg, H. Baxendale, C. Dahle, K. Willander, G. Tobin, E. Backman, O. Soderberg, et al. A new perspective: molecular motifs on oxidized LDL, apoptotic cells, and bacteria are targets for chronic lymphocytic leukemia antibodies Blood, April 1, 2008; 111(7): 3838 - 3848. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. B. Scott, J. L. Meade, and G. P. Cook Profiling killers; unravelling the pathways of human natural killer cell function Brief Funct Genomic Proteomic, January 21, 2008; (2008) elm037v1. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Draghi, A. Pashine, B. Sanjanwala, K. Gendzekhadze, C. Cantoni, D. Cosman, A. Moretta, N. M. Valiante, and P. Parham NKp46 and NKG2D Recognition of Infected Dendritic Cells Is Necessary for NK Cell Activation in the Human Response to Influenza Infection J. Immunol., March 1, 2007; 178(5): 2688 - 2698. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
