Specialized functions of major histocompatibility complex class I molecules. II. Hmt binds N-formylated peptides of mitochondrial and prokaryotic origin

doi:10.1084/jem.174.4.941

This Article

	Full Text (PDF, 370K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JEM
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Shawar, S. M.
	Articles by Rich, R. R.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Shawar, S. M.
	Articles by Rich, R. R.


Social Bookmarking

	What's this?

ARTICLES

Specialized functions of major histocompatibility complex class I molecules. II. Hmt binds N-formylated peptides of mitochondrial and prokaryotic origin

SM Shawar, JM Vyas, JR Rodgers, RG Cook and RR Rich
Howard Hughes Medical Institute Laboratory, Baylor College of Medicine, Houston, Texas 77030.

The physiological functions of the mouse telomeric major histocompatibility complex (MHC) class I molecules, including Hmt, are unknown. Hmt presents a polymorphic, N-formylated peptide encoded by the mitochondrial gene ND1 forming the cell surface maternally transmitted antigen (Mta). Because the N-formyl moiety is required for Hmt binding, we proposed that Hmt may function generally in presentation of N-formylated antigens. This hypothesis was validated by a competitive binding assay, demonstrating that synthetic N-formyl peptides from other mitochondrial genes also bound Hmt. Bacteria similarly initiate protein synthesis with N-formylmethionine; indeed, we established that Hmt can also present prokaryotic peptides in an N- formyl-dependent manner. These results indicate biochemical specialization of this MHC-peptide interaction and suggest a unique role for Hmt in prokaryotic host defenses.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Xu, H., Chun, T., Choi, H.-J., Wang, B., Wang, C.-R. (2006). Impaired response to Listeria in H2-M3-deficient mice reveals a nonredundant role of MHC class Ib-specific T cells in host defense. JEM 203: 449-459 [Abstract] [Full Text]
Battersby, B. J., Redpath, M. E., Shoubridge, E. A. (2005). Mitochondrial DNA segregation in hematopoietic lineages does not depend on MHC presentation of mitochondrially encoded peptides. Hum Mol Genet 14: 2587-2594 [Abstract] [Full Text]
Ploss, A., Lauvau, G., Contos, B., Kerksiek, K. M., Guirnalda, P. D., Leiner, I., Lenz, L. L., Bevan, M. J., Pamer, E. G. (2003). Promiscuity of MHC Class Ib-Restricted T Cell Responses. J. Immunol. 171: 5948-5955 [Abstract] [Full Text]
Doyle, C. K., Davis, B. K., Cook, R. G., Rich, R. R., Rodgers, J. R. (2003). Hyperconservation of the N-Formyl Peptide Binding Site of M3: Evidence that M3 Is an Old Eutherian Molecule with Conserved Recognition of a Pathogen-Associated Molecular Pattern. J. Immunol. 171: 836-844 [Abstract] [Full Text]
Weber, D. A., Attinger, A., Kemball, C. C., Wigal, J. L., Pohl, J., Xiong, Y., Reinherz, E. L., Cheroutre, H., Kronenberg, M., Jensen, P. E. (2002). Peptide-Independent Folding and CD8{alpha}{alpha} Binding by the Nonclassical Class I Molecule, Thymic Leukemia Antigen. J. Immunol. 169: 5708-5714 [Abstract] [Full Text]
Chun, T., Grandea, A. G. III, Lybarger, L., Forman, J., Van Kaer, L., Wang, C.-R. (2001). Functional Roles of TAP and Tapasin in the Assembly of M3-N-Formylated Peptide Complexes. J. Immunol. 167: 1507-1514 [Abstract] [Full Text]
Chun, T., Serbina, N. V., Nolt, D., Wang, B., Chiu, N. M., Flynn, J. L., Wang, C.-R. (2001). Induction of M3-Restricted Cytotoxic T Lymphocyte Responses by N-Formylated Peptides Derived from Mycobacterium tuberculosis. JEM 193: 1213-1220 [Abstract] [Full Text]
Kerksiek, K. M., Busch, D. H., Pamer, E. G. (2001). Variable Immunodominance Hierarchies for H2-M3-Restricted N-Formyl Peptides Following Bacterial Infection. J. Immunol. 166: 1132-1140 [Abstract] [Full Text]
Yague, J., Alvarez, I., Rognan, D., Ramos, M., Vazquez, J., de Castro, J. A. L. (2000). An N-Acetylated Natural Ligand of Human Histocompatibility Leukocyte Antigen (Hla)-B39: Classical Major Histocompatibility Complex Class I Proteins Bind Peptides with a Blocked Nh2 Terminus in Vivo. JEM 191: 2083-2092 [Abstract] [Full Text]
Chiu, N. M., Chun, T., Fay, M., Mandal, M., Wang, C.-R. (1999). The Majority of H2-M3 Is Retained Intracellularly in a Peptide-Receptive State and Traffics to the Cell Surface in the Presence of N-Formylated Peptides. JEM 190: 423-434 [Abstract] [Full Text]
Dabhi, V. M., Hovik, R., Van Kaer, L., Fischer Lindahl, K. (1998). The Alloreactive T Cell Response Against the Class Ib Molecule H2-M3 Is Specific for High Affinity Peptides. J. Immunol. 161: 5171-5178 [Abstract] [Full Text]
Byers, D. E., Fischer Lindahl, K. (1998). H2-M3 Presents a Nonformylated Viral Epitope to CTLs Generated In Vitro. J. Immunol. 161: 90-96 [Abstract] [Full Text]
Princiotta, M. F., Lenz, L. L., Bevan, M. J., Staerz, U. D. (1998). H2-M3 Restricted Presentation of a Listeria-derived Leader Peptide. JEM 187: 1711-1719 [Abstract] [Full Text]
Castano, A., Tangri, S, Miller, J., Holcombe, H., Jackson, M., Huse, W., Kronenberg, M, Peterson, P. (1995). Peptide binding and presentation by mouse CD1. Science 269: 223-226 [Abstract]
Kurlander, R., Shawar, S., Brown, M., Rich, R. (1992). Specialized role for a murine class I-b MHC molecule in prokaryotic host defenses. Science 257: 678-679 [Abstract]