The peptide loop consisting of amino acids 139–157 of human granzyme B (fragmentin 2) contains an immunodominant epitope recognized by the mouse

Apostolidis, Vicki A.; Browne, Kylie A.; Smyth, Mark J.; Trapani, Joseph A.

doi:10.1016/0161-5890(95)00042-d

Cited by 7 publications

(2 citation statements)

References 24 publications

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“…However, we identified a peptide loop (residues 139-157) exteriorised in the surface of granzyme B and related proteases that could act as an immunodominant epitope in mice. 37 We have since used peptides synthesised according to the deduced amino acid sequences from this region to produce monoclonal antibodies that specifically recognise human granzymes B38, A and Met-ase. In a collaborative study with investigators at the Manitoba Institute for Cell Biology, we have used one such monoclonal antibody detecting granzyme B to demonstrate in immuno-electron microscopy studies that granzyme B is internalised within vacuoles in the target cell cytoplasm that form as the result of the simultaneous exposure to perforin (unpublished data).…”

Section: An Important Role In Cl-mediated Apoptosismentioning

confidence: 99%

Target cell apoptosis induced by cytotoxic T cells and natural killer cells involves synergy between the pore‐forming protein, perforin, and the serine protease, granzyme B

Trapani

1995

Australian and New Zealand Journal of Medicine

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Cytotoxic lymphocytes (CL) comprise two effector cell populations with the ability to eliminate unwanted or harmful cells. Cytotoxic T cells (CTLs) demonstrate both an exquisite specificity and memory in recognising target cell oligopeptides presented within the groove of major histocompatibility complex class I antigens. By contrast, natural killer (NK) cells mediate "innate' immunity against virus-infected cells and surveillance against neoplastic transformation, and do not require presensitisation. Despite recognising target cells in very different ways, CTLs and NK cells both utilise a pore-forming protein, perforin, and a battery of serine proteases as a principal means of inflicting cell death. The action of both types of CL results in death by apoptosis. Recently, we and others have accumulated evidence that perforin and serine proteases synergistically trigger an endogenous pathway of programmed cell death that results in dissolution of the nuclear membrane, chromatin condensation and DNA fragmentation. These changes are secondary to inappropriate activation of p34, a kinase whose activation and migration from the cytoplasm to the nucleus normally controls a cell's entry into mitosis. Therefore, CI, may exert their actions through the derangement of cell cycle control. The downstream molecular targets of perforin/granzyme-mediated apoptosis (especially the physiological ligand/substrate of granzyme B) are still unclear, though candidate molecules with homology to products of cell death genes found in primitive organisms such as the nematode, C. elegans, are currently under investigation.

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Section: An Important Role In Cl-mediated Apoptosismentioning

confidence: 99%

Target cell apoptosis induced by cytotoxic T cells and natural killer cells involves synergy between the pore‐forming protein, perforin, and the serine protease, granzyme B

Trapani

1995

Australian and New Zealand Journal of Medicine

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“…[6][7][8][9][10][11] Nevertheless, exceptions to this general view of discontinuous antibody epitopes have been published, suggesting that antibody epitopes may well consist of continuous sequences within, for example, surface-exposed peptide loops or at the ends of native proteins. 6,[12][13][14][15][16][17][18][19][20][21][22][23][24][25][26] Therefore, the SQ-peptide could be a candidate target for the immune system.…”

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confidence: 99%

Analysis of Samples from Patients Treated with ReFacto℗ for the Presence of Anti-SQ-Peptide Specific Antibodies

Wikén¹,

Sjöberg²

2002

Semin Thromb Hemost

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ReFacto lacks the major part of the B-domain, except for 14 amino acid residues from the N-terminal and C-terminal ends, which are linked into a 14 amino acid SQ-peptide tail in the C-terminal end of the 90 kD heavy chain, thereby introducing a new peptide sequence in the factor VIII (FVIII) molecule. Therefore, samples from some of the patients enrolled in the ReFacto clinical trials were analyzed for the emergence of anti-SQ-peptide antibodies in addition to determinations for inhibitors by Bethesda assay and for anti-FVIII antibodies by enzyme-linked immunosorbent assay (ELISA). An anti-peptide ELISA was developed using six partially overlapping 15-16 mer peptides covering the SQ-linker region. Results from ReFacto-treated anti-FVIII antibody-positive or -negative patients were compared with those for normal healthy adults and patients treated with other FVIII products. The pattern was compared with that for SQ-peptide specific monoclonal antibodies, each recognizing three or four overlapping SQ-peptides. Antibodies recognizing mainly one of the SQ-peptides were found in samples in some individuals from all investigated groups. This means that the anti-SQ reactivity found in patients treated with ReFacto is not induced by the SQ-sequence of the molecule but rather by some other agent, giving rise to antibodies cross-reactive with SQ-peptides.

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Generation of HER2 monoclonal antibodies using epitopes of a rabbit polyclonal antibody

Uhlén

Rockberg

2014

New Biotechnology

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The peptide loop consisting of amino acids 139–157 of human granzyme B (fragmentin 2) contains an immunodominant epitope recognized by the mouse

Cited by 7 publications

References 24 publications

Target cell apoptosis induced by cytotoxic T cells and natural killer cells involves synergy between the pore‐forming protein, perforin, and the serine protease, granzyme B

Target cell apoptosis induced by cytotoxic T cells and natural killer cells involves synergy between the pore‐forming protein, perforin, and the serine protease, granzyme B

Analysis of Samples from Patients Treated with ReFacto℗ for the Presence of Anti-SQ-Peptide Specific Antibodies

Generation of HER2 monoclonal antibodies using epitopes of a rabbit polyclonal antibody

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