Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry

Donald F. Hunt; Robert A. Henderson; Jeffrey Shabanowitz; Kazuyasu Sakaguchi; Hanspeter Michel; Noelle Sevilir; Andrea L. Cox; Ettore Appella; Victor H. Engelhard

Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry

Donald F. Hunt, Robert A. Henderson, Jeffrey Shabanowitz, Kazuyasu Sakaguchi, Hanspeter Michel, Noelle Sevilir, Andrea L. Cox, Ettore Appella, Victor H. Engelhard

Research output: Contribution to journal › Article › peer-review

1137 Scopus citations

Abstract

Antigens recognized by T cells are expressed as peptides bound to major histocompatibility complex (MHC) molecules. Microcapillary high-performance liquid chromatography-electrospray ionization-tandem mass spectrometry was used to fractionate and sequence subpicomolar amounts of peptides isolated from the MHC molecule HLA-A2.1. Of 200 different species quantitated, eight were sequenced and four were found in cellular proteins. All were nine residues long and shared a distinct structural motif. The sensitivity and speed of this approach should enhance the analysis of peptides from small quantities of virally infected and transformed cells as well as those associated with autoimmune disease states.

Original language	English (US)
Pages (from-to)	1261-1263
Number of pages	3
Journal	Science
Volume	255
Issue number	5049
State	Published - Mar 6 1992

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title = "Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry",

abstract = "Antigens recognized by T cells are expressed as peptides bound to major histocompatibility complex (MHC) molecules. Microcapillary high-performance liquid chromatography-electrospray ionization-tandem mass spectrometry was used to fractionate and sequence subpicomolar amounts of peptides isolated from the MHC molecule HLA-A2.1. Of 200 different species quantitated, eight were sequenced and four were found in cellular proteins. All were nine residues long and shared a distinct structural motif. The sensitivity and speed of this approach should enhance the analysis of peptides from small quantities of virally infected and transformed cells as well as those associated with autoimmune disease states.",

author = "Hunt, {Donald F.} and Henderson, {Robert A.} and Jeffrey Shabanowitz and Kazuyasu Sakaguchi and Hanspeter Michel and Noelle Sevilir and Cox, {Andrea L.} and Ettore Appella and Engelhard, {Victor H.}",

year = "1992",

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language = "English (US)",

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T1 - Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry

AU - Hunt, Donald F.

AU - Henderson, Robert A.

AU - Shabanowitz, Jeffrey

AU - Sakaguchi, Kazuyasu

AU - Michel, Hanspeter

AU - Sevilir, Noelle

AU - Cox, Andrea L.

AU - Appella, Ettore

AU - Engelhard, Victor H.

PY - 1992/3/6

Y1 - 1992/3/6

N2 - Antigens recognized by T cells are expressed as peptides bound to major histocompatibility complex (MHC) molecules. Microcapillary high-performance liquid chromatography-electrospray ionization-tandem mass spectrometry was used to fractionate and sequence subpicomolar amounts of peptides isolated from the MHC molecule HLA-A2.1. Of 200 different species quantitated, eight were sequenced and four were found in cellular proteins. All were nine residues long and shared a distinct structural motif. The sensitivity and speed of this approach should enhance the analysis of peptides from small quantities of virally infected and transformed cells as well as those associated with autoimmune disease states.

AB - Antigens recognized by T cells are expressed as peptides bound to major histocompatibility complex (MHC) molecules. Microcapillary high-performance liquid chromatography-electrospray ionization-tandem mass spectrometry was used to fractionate and sequence subpicomolar amounts of peptides isolated from the MHC molecule HLA-A2.1. Of 200 different species quantitated, eight were sequenced and four were found in cellular proteins. All were nine residues long and shared a distinct structural motif. The sensitivity and speed of this approach should enhance the analysis of peptides from small quantities of virally infected and transformed cells as well as those associated with autoimmune disease states.

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M3 - Article

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AN - SCOPUS:0026507564

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ER -

Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry

Abstract

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