Biotinylation of class I MHC molecules abrogates recognition by W6/32 antibody

P. Malik, Eishi Baba, Jack L. Strominger

研究成果: ジャーナルへの寄稿記事

9 引用 (Scopus)

抄録

W6/32 is one of the most common monoclonal antibodies (mAb) used to characterize human class I major histocompatibility complex (MHC) molecules. It recognizes a conformational epitope on the intact MHC molecule containing both β2-microglobulin (β2-m) and the heavy chain. Labelling proteins by biotinylation is a very useful technique of for their detection, purification and analysis. A common method for biotinylating proteins is through the use of N-hydroxysuccinimide (NHS) biotin or Sulfo-NHS-biotin where the free amino groups on the protein are used for coupling the biotin moiety. However, W6/32 was unable to effectively immunoprecipitate biotinylated human class I MHC molecules including the human non classical HLA-G molecule. FACScan analysis confirmed that biotinylating human class I MHC and HLA-G molecules prevents the recognition of these molecule by W6/32. In contrast, the recognition by another conformation-dependent monoclonal antibody, ME1, specific to HLA-B27 molecules, remained totally unaffected.

元の言語英語
ページ(範囲)576-579
ページ数4
ジャーナルTissue antigens
53
発行部数6
DOI
出版物ステータス出版済み - 6 14 1999

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Biotinylation
Major Histocompatibility Complex
HLA-G Antigens
Molecules
Antibodies
Monoclonal Antibodies
HLA-B27 Antigen
Proteins
Biotin
Epitopes
Labeling
Purification
Conformations

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology
  • Biochemistry
  • Genetics

これを引用

Biotinylation of class I MHC molecules abrogates recognition by W6/32 antibody. / Malik, P.; Baba, Eishi; Strominger, Jack L.

:: Tissue antigens, 巻 53, 番号 6, 14.06.1999, p. 576-579.

研究成果: ジャーナルへの寄稿記事

Malik, P. ; Baba, Eishi ; Strominger, Jack L. / Biotinylation of class I MHC molecules abrogates recognition by W6/32 antibody. :: Tissue antigens. 1999 ; 巻 53, 番号 6. pp. 576-579.
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abstract = "W6/32 is one of the most common monoclonal antibodies (mAb) used to characterize human class I major histocompatibility complex (MHC) molecules. It recognizes a conformational epitope on the intact MHC molecule containing both β2-microglobulin (β2-m) and the heavy chain. Labelling proteins by biotinylation is a very useful technique of for their detection, purification and analysis. A common method for biotinylating proteins is through the use of N-hydroxysuccinimide (NHS) biotin or Sulfo-NHS-biotin where the free amino groups on the protein are used for coupling the biotin moiety. However, W6/32 was unable to effectively immunoprecipitate biotinylated human class I MHC molecules including the human non classical HLA-G molecule. FACScan analysis confirmed that biotinylating human class I MHC and HLA-G molecules prevents the recognition of these molecule by W6/32. In contrast, the recognition by another conformation-dependent monoclonal antibody, ME1, specific to HLA-B27 molecules, remained totally unaffected.",
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N2 - W6/32 is one of the most common monoclonal antibodies (mAb) used to characterize human class I major histocompatibility complex (MHC) molecules. It recognizes a conformational epitope on the intact MHC molecule containing both β2-microglobulin (β2-m) and the heavy chain. Labelling proteins by biotinylation is a very useful technique of for their detection, purification and analysis. A common method for biotinylating proteins is through the use of N-hydroxysuccinimide (NHS) biotin or Sulfo-NHS-biotin where the free amino groups on the protein are used for coupling the biotin moiety. However, W6/32 was unable to effectively immunoprecipitate biotinylated human class I MHC molecules including the human non classical HLA-G molecule. FACScan analysis confirmed that biotinylating human class I MHC and HLA-G molecules prevents the recognition of these molecule by W6/32. In contrast, the recognition by another conformation-dependent monoclonal antibody, ME1, specific to HLA-B27 molecules, remained totally unaffected.

AB - W6/32 is one of the most common monoclonal antibodies (mAb) used to characterize human class I major histocompatibility complex (MHC) molecules. It recognizes a conformational epitope on the intact MHC molecule containing both β2-microglobulin (β2-m) and the heavy chain. Labelling proteins by biotinylation is a very useful technique of for their detection, purification and analysis. A common method for biotinylating proteins is through the use of N-hydroxysuccinimide (NHS) biotin or Sulfo-NHS-biotin where the free amino groups on the protein are used for coupling the biotin moiety. However, W6/32 was unable to effectively immunoprecipitate biotinylated human class I MHC molecules including the human non classical HLA-G molecule. FACScan analysis confirmed that biotinylating human class I MHC and HLA-G molecules prevents the recognition of these molecule by W6/32. In contrast, the recognition by another conformation-dependent monoclonal antibody, ME1, specific to HLA-B27 molecules, remained totally unaffected.

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