Abstract
In order to determine how T cell-presented peptides associate with the antigen binding sites (desetopes) of class I major histocompatibility complex (MHC) molecules and how they might be scavenged from an endogenous processing pathway for transfer to those molecules, we characterized the binding of two synthetic peptides restricted by HLA-B37 or HLA-A2 to class I MHC molecules and to cellular proteins of histotyped cell lines, by gel filtration and photo-affinity labeling techniques. In gel filtration binding studies, each peptide associated with immunopurified class I MHC molecules from cells with its restricting histotype, but little was bound to class I MHC molecules from cells without the restricting histotype and none was bound to bovine serum albumin. After crosslinkage of a radioiodinated photoreactive derivative of influenza virus nucleoprotein peptide NP(336-355Y) and immunoprecipitations with antibodies to class I MHC molecules, that peptide was found to bind to immunopurified class I MHC molecules from HLA-B37 + but not HLA-B37- cells. Binding of the [125I]NP peptide increased from 6 to 12 hr of incubation and was competed by unlabeled, NP peptide but not by HLA-A2-restricted, influenza virus matrix MA(57-73). The principal microsomal membrane proteins binding [125I]NP were about 65, 45 and 33 kD.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 341-348 |
| Number of pages | 8 |
| Journal | Molecular Immunology |
| Volume | 28 |
| Issue number | 4-5 |
| DOIs | |
| State | Published - 1991 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Molecular Biology
- Immunology
Cite this
Binding of radioiodinated influenza virus peptides to class I MHC molecules and to other cellular proteins as analyzed by gel filtration and photoaffinity labeling. / Reyes, Victor; Lu, Shan; Humphreys, Robert E.
In: Molecular Immunology, Vol. 28, No. 4-5, 1991, p. 341-348.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding of radioiodinated influenza virus peptides to class I MHC molecules and to other cellular proteins as analyzed by gel filtration and photoaffinity labeling
AU - Reyes, Victor
AU - Lu, Shan
AU - Humphreys, Robert E.
PY - 1991
Y1 - 1991
N2 - In order to determine how T cell-presented peptides associate with the antigen binding sites (desetopes) of class I major histocompatibility complex (MHC) molecules and how they might be scavenged from an endogenous processing pathway for transfer to those molecules, we characterized the binding of two synthetic peptides restricted by HLA-B37 or HLA-A2 to class I MHC molecules and to cellular proteins of histotyped cell lines, by gel filtration and photo-affinity labeling techniques. In gel filtration binding studies, each peptide associated with immunopurified class I MHC molecules from cells with its restricting histotype, but little was bound to class I MHC molecules from cells without the restricting histotype and none was bound to bovine serum albumin. After crosslinkage of a radioiodinated photoreactive derivative of influenza virus nucleoprotein peptide NP(336-355Y) and immunoprecipitations with antibodies to class I MHC molecules, that peptide was found to bind to immunopurified class I MHC molecules from HLA-B37 + but not HLA-B37- cells. Binding of the [125I]NP peptide increased from 6 to 12 hr of incubation and was competed by unlabeled, NP peptide but not by HLA-A2-restricted, influenza virus matrix MA(57-73). The principal microsomal membrane proteins binding [125I]NP were about 65, 45 and 33 kD.
AB - In order to determine how T cell-presented peptides associate with the antigen binding sites (desetopes) of class I major histocompatibility complex (MHC) molecules and how they might be scavenged from an endogenous processing pathway for transfer to those molecules, we characterized the binding of two synthetic peptides restricted by HLA-B37 or HLA-A2 to class I MHC molecules and to cellular proteins of histotyped cell lines, by gel filtration and photo-affinity labeling techniques. In gel filtration binding studies, each peptide associated with immunopurified class I MHC molecules from cells with its restricting histotype, but little was bound to class I MHC molecules from cells without the restricting histotype and none was bound to bovine serum albumin. After crosslinkage of a radioiodinated photoreactive derivative of influenza virus nucleoprotein peptide NP(336-355Y) and immunoprecipitations with antibodies to class I MHC molecules, that peptide was found to bind to immunopurified class I MHC molecules from HLA-B37 + but not HLA-B37- cells. Binding of the [125I]NP peptide increased from 6 to 12 hr of incubation and was competed by unlabeled, NP peptide but not by HLA-A2-restricted, influenza virus matrix MA(57-73). The principal microsomal membrane proteins binding [125I]NP were about 65, 45 and 33 kD.
UR - http://www.scopus.com/inward/record.url?scp=0025756435&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025756435&partnerID=8YFLogxK
U2 - 10.1016/0161-5890(91)90146-B
DO - 10.1016/0161-5890(91)90146-B
M3 - Article
VL - 28
SP - 341
EP - 348
JO - Molecular Immunology
JF - Molecular Immunology
SN - 0161-5890
IS - 4-5
ER -