Capacity of intact proteins to bind to MHC class II molecules

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Standard

Capacity of intact proteins to bind to MHC class II molecules. / Sette, A; Adorini, L; Colon, S M; Buus, S; Grey, H M.

I: Journal of Immunology, Bind 143, Nr. 4, 1989, s. 1265-7.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sette, A, Adorini, L, Colon, SM, Buus, S & Grey, HM 1989, 'Capacity of intact proteins to bind to MHC class II molecules', Journal of Immunology, bind 143, nr. 4, s. 1265-7.

APA

Sette, A., Adorini, L., Colon, S. M., Buus, S., & Grey, H. M. (1989). Capacity of intact proteins to bind to MHC class II molecules. Journal of Immunology, 143(4), 1265-7.

Vancouver

Sette A, Adorini L, Colon SM, Buus S, Grey HM. Capacity of intact proteins to bind to MHC class II molecules. Journal of Immunology. 1989;143(4):1265-7.

Author

Sette, A ; Adorini, L ; Colon, S M ; Buus, S ; Grey, H M. / Capacity of intact proteins to bind to MHC class II molecules. I: Journal of Immunology. 1989 ; Bind 143, Nr. 4. s. 1265-7.

Bibtex

@article{179df0c0ebce11ddbf70000ea68e967b,
title = "Capacity of intact proteins to bind to MHC class II molecules",
abstract = "Here we have demonstrated that denatured, but not native protein antigens can interact with Ia molecules. Thus, the failure of native antigens to be recognized as such by T cells appears to be at least in part due to a deficient antigen/Ia interaction. These results also support previous observations that some T cells can recognize denatured antigens without a further processing requirement. Moreover, a striking correlation was observed between the in vitro binding pattern of denatured proteins and the pattern of restriction of T cell responses elicited by immunization with the native antigen, raising the possibility that an unfolding step may actually occur early during in vivo processing and influence the final outcome of Ia-restricted T cell responses.",
author = "A Sette and L Adorini and Colon, {S M} and S Buus and Grey, {H M}",
note = "Keywords: Animals; Cattle; Chickens; Histocompatibility Antigens Class II; Humans; Mice; Mice, Inbred DBA; Muramidase; Ovalbumin; Protein Binding; Protein Denaturation; Serum Albumin, Bovine; T-Lymphocytes; Transferrin",
year = "1989",
language = "English",
volume = "143",
pages = "1265--7",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "4",

}

RIS

TY - JOUR

T1 - Capacity of intact proteins to bind to MHC class II molecules

AU - Sette, A

AU - Adorini, L

AU - Colon, S M

AU - Buus, S

AU - Grey, H M

N1 - Keywords: Animals; Cattle; Chickens; Histocompatibility Antigens Class II; Humans; Mice; Mice, Inbred DBA; Muramidase; Ovalbumin; Protein Binding; Protein Denaturation; Serum Albumin, Bovine; T-Lymphocytes; Transferrin

PY - 1989

Y1 - 1989

N2 - Here we have demonstrated that denatured, but not native protein antigens can interact with Ia molecules. Thus, the failure of native antigens to be recognized as such by T cells appears to be at least in part due to a deficient antigen/Ia interaction. These results also support previous observations that some T cells can recognize denatured antigens without a further processing requirement. Moreover, a striking correlation was observed between the in vitro binding pattern of denatured proteins and the pattern of restriction of T cell responses elicited by immunization with the native antigen, raising the possibility that an unfolding step may actually occur early during in vivo processing and influence the final outcome of Ia-restricted T cell responses.

AB - Here we have demonstrated that denatured, but not native protein antigens can interact with Ia molecules. Thus, the failure of native antigens to be recognized as such by T cells appears to be at least in part due to a deficient antigen/Ia interaction. These results also support previous observations that some T cells can recognize denatured antigens without a further processing requirement. Moreover, a striking correlation was observed between the in vitro binding pattern of denatured proteins and the pattern of restriction of T cell responses elicited by immunization with the native antigen, raising the possibility that an unfolding step may actually occur early during in vivo processing and influence the final outcome of Ia-restricted T cell responses.

M3 - Journal article

C2 - 2787361

VL - 143

SP - 1265

EP - 1267

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 4

ER -

ID: 9946879