Structure of the gene of tum− transplantation antigen P91A: The mutated exon encodes a peptide recognized with Ld by cytolytic T cells

Lurquin, Christophe; Pel, Aline Van; Mariamé, Bernard; Plaen, Etienne De; Szikora, Jean-Pierre; Janssens, C.; Reddehase, Matthias J.; Lejeune, Joseph; Boon, Thierry

doi:10.1016/0092-8674(89)90844-1

Cited by 286 publications

(148 citation statements)

References 39 publications

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“…The two genes were designated SUNI and SUN2 (suppressor of ninl-1). SUN2 is an essential gene and is a homologue of DoxA2 of Drosophila melanogaster (Pentz and Wright, 1991; Kawamura et al, 1996), a mouse transplantation antigen gene, P91A, (Lurquin et al, 1989), and the p58 gene encoding a component of the human 26S proteasome (DeMartino et al, 1994 and present study). In contrast, the SUN1 gene with an insertion at the mid-point of its open reading frame (ORF) does not confer a growth defect on the cells.…”

Section: Introductionmentioning

confidence: 99%

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.

Kominami

Okura

Kawamura

et al. 1997

MBoC

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Ninlp, a component of the 26S proteasome of Saccharomyces cerevisiae, is required for activation of Cdc28p kinase at the G1-S-phase and G2-M boundaries. By exploiting the temperature-sensitive phenotype of the ninl-l mutant, we have screened for genes encoding proteins with related functions to Ninlp and have cloned and characterized two new multicopy suppressors, SUNI and SlUN2, of the ninl-l mutation. SUNI can suppress a null ninl mutation, whereas SlUN2, an essential gene, does not. Sunlp is a 268-amino acid protein which shows strong similarity to MBP1 of Arabidopsis thaliana, a homologue of the S5a subunit of the human 26S proteasome. Sunlp binds ubiquitin-lysozyme conjugates as do S5a and MBP1. Sun2p (523 amino acids) was found to be homologous to the p58 subunit of the human 26S proteasome. cDNA encoding the p58 component was cloned. Furthermore, expression of a derivative of p58 from which the N-terminal 150 amino acids had been removed restored the function of a null allele of SUN2. During glycerol density gradient centrifugation, both Sunlp and Sun2p comigrated with the known proteasome components. These results, as well as other structural and functional studies, indicate that both Sunlp and Sun2p are components of the regulatory module of the yeast 26S proteasome.

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Section: Introductionmentioning

confidence: 99%

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.

Kominami

Okura

Kawamura

et al. 1997

MBoC

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“…The mechanism for this is unknown, although assessment of one of these regrowth tumors demonstrated a loss of the gene coding for the model antigen, a phenomenon that has been previously noted in antigen-loss tumor variants in human melanoma and murine P815 and SV40-transformed tumor models. [27][28][29][30] It is tempting to speculate that a vigorous antigen-specific antitumor CTL response in vivo might facilitate the generation of antigen-loss variants by eradicating tumor cells expressing the tumor antigen, permitting small numbers of tumor cells not expressing the targeted antigen to regrow. This observation supports the critical importance of T cell selective pressure against tumor progression and has important implications for the …”

Section: Discussionmentioning

confidence: 99%

Persistent, antigen-specific, therapeutic antitumor immunity by dendritic cells genetically modified with an adenoviral vector to express a model tumor antigen

et al. 2000

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Dendritic cells (DC) are potent antigen-presenting cells that play a critical role in the initiation of cellular immune responses. Using a BALB/c syngeneic colon carcinoma cell line expressing a model tumor antigen ␤-galactosidase (␤gal), we previously reported (Song et al, J Exp Med 1997; 186: 1247-1256) that immunization of mice with a single injection of DCs genetically modified with an adenovirus vector expressing ␤gal confers potent protection against a lethal intravenous tumor challenge, as well as suppression of preestablished lung tumors, resulting in a significant survival advantage. In the present study, we have addressed the question: how long does the memory of tumor antigenspecific immunity persists after DC priming in vivo using this genetically modified DC-based cancer vaccination strategy? To accomplish this, two groups of mice were evaluated: (1)

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“…These peptides became very real when they were first eluted from target cells by the group of H. G. Rammensee [65]. Peptides were also soon shown to be involved in anti-tumour CTL responses by T. Boon's group [66]. All became convincingly clear in the classical studies of P. Björkman, J. Strominger and D. Wiley in 1987, when the X-ray cristallography of a class I HLA-molecule revealed the peptide binding cleft [67,68].…”

Section: Further Analysismentioning

confidence: 99%

Cellular Immune Recognition and the Biological Role of Major Transplantation Antigens

Zinkernagel

1997

Scand J Immunol

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Structure of the gene of tum− transplantation antigen P91A: The mutated exon encodes a peptide recognized with Ld by cytolytic T cells

Cited by 286 publications

References 39 publications

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.

Persistent, antigen-specific, therapeutic antitumor immunity by dendritic cells genetically modified with an adenoviral vector to express a model tumor antigen

Cellular Immune Recognition and the Biological Role of Major Transplantation Antigens

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