An H-2L(d) hybrid molecule with a QA-2 α-3 domain and phosphatidyl-inositol anchor is not recognized by H-2L(d)-specific cytotoxic T lymphocytes

D. W. Mann, I. Stroynowski, L. Hood, J. Forman

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14 Citations (Scopus)

Abstract

L(d)/Q7(d), a hybrid molecule consisting of α-1 and α-2 domains from H-2L(d) and α-3 and carboxy-end components from Q7(d), was expressed on the surface of CRL-3A rat liver cells. This molecule retained serologic H-2L(d) epitopes. The Ag is attached to the cell membrane through a phosphatidyl-inositol linkage, characteristic of Qa-2 molecules. Both bulk cultured and cloned H-2L(d) alloreactive CTL as well as H-2L(d) restricted vesicular stomatitis virus-specific CTL lyse CRL-3A cells which express H-2L(d) but show little or no lytic activity on cells which express the L(d)/Q7(d) hybrid. These cells also fail to act as cold target competitors for alloreactive anti-H-2L(d) CTL. However, cells expressing L(d)/Q7(d) are not resistant to CTL mediated lysis because they can be killed in the presence of lectin. These data indicate that recognition of polymorphic class I CTL epitopes in the α-1 and α-2 domains are influenced by the structure of the carboxy-end of the molecule.

Original languageEnglish (US)
Pages (from-to)318-322
Number of pages5
JournalJournal of Immunology
Volume142
Issue number1
StatePublished - 1989

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Cytotoxic T-Lymphocytes
Phosphatidylinositols
Epitopes
Vesicular Stomatitis
Lectins
Cell Membrane
Viruses
Liver

ASJC Scopus subject areas

  • Immunology

Cite this

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title = "An H-2L(d) hybrid molecule with a QA-2 α-3 domain and phosphatidyl-inositol anchor is not recognized by H-2L(d)-specific cytotoxic T lymphocytes",
abstract = "L(d)/Q7(d), a hybrid molecule consisting of α-1 and α-2 domains from H-2L(d) and α-3 and carboxy-end components from Q7(d), was expressed on the surface of CRL-3A rat liver cells. This molecule retained serologic H-2L(d) epitopes. The Ag is attached to the cell membrane through a phosphatidyl-inositol linkage, characteristic of Qa-2 molecules. Both bulk cultured and cloned H-2L(d) alloreactive CTL as well as H-2L(d) restricted vesicular stomatitis virus-specific CTL lyse CRL-3A cells which express H-2L(d) but show little or no lytic activity on cells which express the L(d)/Q7(d) hybrid. These cells also fail to act as cold target competitors for alloreactive anti-H-2L(d) CTL. However, cells expressing L(d)/Q7(d) are not resistant to CTL mediated lysis because they can be killed in the presence of lectin. These data indicate that recognition of polymorphic class I CTL epitopes in the α-1 and α-2 domains are influenced by the structure of the carboxy-end of the molecule.",
author = "Mann, {D. W.} and I. Stroynowski and L. Hood and J. Forman",
year = "1989",
language = "English (US)",
volume = "142",
pages = "318--322",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
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TY - JOUR

T1 - An H-2L(d) hybrid molecule with a QA-2 α-3 domain and phosphatidyl-inositol anchor is not recognized by H-2L(d)-specific cytotoxic T lymphocytes

AU - Mann, D. W.

AU - Stroynowski, I.

AU - Hood, L.

AU - Forman, J.

PY - 1989

Y1 - 1989

N2 - L(d)/Q7(d), a hybrid molecule consisting of α-1 and α-2 domains from H-2L(d) and α-3 and carboxy-end components from Q7(d), was expressed on the surface of CRL-3A rat liver cells. This molecule retained serologic H-2L(d) epitopes. The Ag is attached to the cell membrane through a phosphatidyl-inositol linkage, characteristic of Qa-2 molecules. Both bulk cultured and cloned H-2L(d) alloreactive CTL as well as H-2L(d) restricted vesicular stomatitis virus-specific CTL lyse CRL-3A cells which express H-2L(d) but show little or no lytic activity on cells which express the L(d)/Q7(d) hybrid. These cells also fail to act as cold target competitors for alloreactive anti-H-2L(d) CTL. However, cells expressing L(d)/Q7(d) are not resistant to CTL mediated lysis because they can be killed in the presence of lectin. These data indicate that recognition of polymorphic class I CTL epitopes in the α-1 and α-2 domains are influenced by the structure of the carboxy-end of the molecule.

AB - L(d)/Q7(d), a hybrid molecule consisting of α-1 and α-2 domains from H-2L(d) and α-3 and carboxy-end components from Q7(d), was expressed on the surface of CRL-3A rat liver cells. This molecule retained serologic H-2L(d) epitopes. The Ag is attached to the cell membrane through a phosphatidyl-inositol linkage, characteristic of Qa-2 molecules. Both bulk cultured and cloned H-2L(d) alloreactive CTL as well as H-2L(d) restricted vesicular stomatitis virus-specific CTL lyse CRL-3A cells which express H-2L(d) but show little or no lytic activity on cells which express the L(d)/Q7(d) hybrid. These cells also fail to act as cold target competitors for alloreactive anti-H-2L(d) CTL. However, cells expressing L(d)/Q7(d) are not resistant to CTL mediated lysis because they can be killed in the presence of lectin. These data indicate that recognition of polymorphic class I CTL epitopes in the α-1 and α-2 domains are influenced by the structure of the carboxy-end of the molecule.

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