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Academic literature on the topic 'Peptide loading'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Peptide loading"

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Liu, Bai, Lijing You, Kaiping Han, Hyung-il Lee, Peter Rhode, Sarah Henrickson, Ulrich H. von Andrian, and Hing C. Wong. "Peptide-loading enhancement for antigen presenting cells (93.6)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S167. http://dx.doi.org/10.4049/jimmunol.178.supp.93.6.

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Abstract Exogenous β2-microglobulin has been shown to enhance the loading of antigenic peptides into MHC class I complexes of antigen presenting cells (APCs). In this study, we employed the multimeric soluble singe-chain T cell receptors and flow cytometry analysis to confirm the activity of exogenous β2 -microglobulin in enhancing the loading of various peptides onto APCs. To our surprise, we found that the enhancement of peptide loading on APCs was restricted to a fraction of the peptides tested. However, a chemical component, commonly used in biological research, exhibits similar peptide loading enhancement activity as that of exogenous β2-microglobulin. The peptide loading enhancement profiles of exogenous β2-microglobulin and the chemical are different and seem to be peptide-dependent. Although the underling mechanism of the chemical for peptide loading enhancement is unknown, the chemical is also found to significantly enhance the endogenous peptide presentation of the gp33 protein of lymphocytic choriomeningitis virus in 5T33 mouse myeloma cells. Thus, a mixture of β2-microglobulin and the chemical could have broad utility in increasing antigen presentation in a variety of experimental applications including vaccine-based approaches.
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Zernich, Danielle, Anthony W. Purcell, Whitney A. Macdonald, Lars Kjer-Nielsen, Lauren K. Ely, Nihay Laham, Tanya Crockford, et al. "Natural HLA Class I Polymorphism Controls the Pathway of Antigen Presentation and Susceptibility to Viral Evasion." Journal of Experimental Medicine 200, no. 1 (June 28, 2004): 13–24. http://dx.doi.org/10.1084/jem.20031680.

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HLA class I polymorphism creates diversity in epitope specificity and T cell repertoire. We show that HLA polymorphism also controls the choice of Ag presentation pathway. A single amino acid polymorphism that distinguishes HLA-B*4402 (Asp116) from B*4405 (Tyr116) permits B*4405 to constitutively acquire peptides without any detectable incorporation into the transporter associated with Ag presentation (TAP)-associated peptide loading complex even under conditions of extreme peptide starvation. This mode of peptide capture is less susceptible to viral interference than the conventional loading pathway used by HLA-B*4402 that involves assembly of class I molecules within the peptide loading complex. Thus, B*4402 and B*4405 are at opposite extremes of a natural spectrum in HLA class I dependence on the PLC for Ag presentation. These findings unveil a new layer of MHC polymorphism that affects the generic pathway of Ag loading, revealing an unsuspected evolutionary trade-off in selection for optimal HLA class I loading versus effective pathogen evasion.
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Morozov, Giora I., Huaying Zhao, Michael G. Mage, Lisa F. Boyd, Jiansheng Jiang, Michael A. Dolan, Ramesh Venna, et al. "Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing." Proceedings of the National Academy of Sciences 113, no. 8 (February 11, 2016): E1006—E1015. http://dx.doi.org/10.1073/pnas.1519894113.

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Peptide loading of major histocompatibility complex class I (MHC-I) molecules is central to antigen presentation, self-tolerance, and CD8+ T-cell activation. TAP binding protein, related (TAPBPR), a widely expressed tapasin homolog, is not part of the classical MHC-I peptide-loading complex (PLC). Using recombinant MHC-I molecules, we show that TAPBPR binds HLA-A*02:01 and several other MHC-I molecules that are either peptide-free or loaded with low-affinity peptides. Fluorescence polarization experiments establish that TAPBPR augments peptide binding by MHC-I. The TAPBPR/MHC-I interaction is reversed by specific peptides, related to their affinity. Mutational and small-angle X-ray scattering (SAXS) studies confirm the structural similarities of TAPBPR with tapasin. These results support a role of TAPBPR in stabilizing peptide-receptive conformation(s) of MHC-I, permitting peptide editing.
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Vatner, Ralph Eric, and Pramod K. Srivastava. "The TCP-1 Ring Complex (TRiC) binds antigenic peptides and facilitates their cross-presentation by APCs (93.5)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S166. http://dx.doi.org/10.4049/jimmunol.178.supp.93.5.

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Abstract The multimeric chaperonin TCP-1 Ring Complex (TRiC), an hsp60 homologue, was recently found to associate with the precursors of the ovalbumin-derived SIINFEKL epitope during processing and loading onto MHC I. The TRiC-peptide association is essential for loading of MHC I. Here, we have sought to characterize the peptide-binding properties of TRiC in vitro, and study the behavior of TRiC-peptide complexes in cross-presentation assays. TRiC is shown to bind a variety of peptides in vitro in much the same manner as previously described peptide chaperones of the hsp90 family. TRiC-peptide complexes are efficiently taken up by APCs and the peptides are processed and represented on MHC class I for recognition by specific CD8+ T cells. These results as well as the immunological properties of TRiC-peptide complexes formed in vivo shall be reported.
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Hafstrand, Ida, Ece Canan Sayitoglu, Anca Apavaloaei, Benjamin John Josey, Renhua Sun, Xiao Han, Sara Pellegrino, et al. "Successive crystal structure snapshots suggest the basis for MHC class I peptide loading and editing by tapasin." Proceedings of the National Academy of Sciences 116, no. 11 (February 26, 2019): 5055–60. http://dx.doi.org/10.1073/pnas.1807656116.

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MHC-I epitope presentation to CD8+ T cells is directly dependent on peptide loading and selection during antigen processing. However, the exact molecular bases underlying peptide selection and binding by MHC-I remain largely unknown. Within the peptide-loading complex, the peptide editor tapasin is key to the selection of MHC-I–bound peptides. Here, we have determined an ensemble of crystal structures of MHC-I in complex with the peptide exchange-associated dipeptide GL, as well as the tapasin-associated scoop loop, alone or in combination with candidate epitopes. These results combined with mutation analyses allow us to propose a molecular model underlying MHC-I peptide selection by tapasin. The N termini of bound peptides most probably bind first in the N-terminal and middle region of the MHC-I peptide binding cleft, upon which the peptide C termini are tested for their capacity to dislodge the tapasin scoop loop from the F pocket of the MHC-I cleft. Our results also indicate important differences in peptide selection between different MHC-I alleles.
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Badrinath, Soumya, Heike Kunze-Schumacher, Rainer Blasczyk, Trevor Huyton, and Christina Bade-Doeding. "A Micropolymorphism Altering the Residue Triad 97/114/156 Determines the Relative Levels of Tapasin Independence and Distinct Peptide Profiles for HLA-A*24 Allotypes." Journal of Immunology Research 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/298145.

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While many HLA class I molecules interact directly with the peptide loading complex (PLC) for conventional loading of peptides certain class I molecules are able to present peptides in a way that circumvents the PLC components. We investigated micropolymorphisms at position 156 of HLA-A*24 allotypes and their effects on PLC dependence for assembly and peptide binding specificities. HLA-A*24:06156Trpand HLA-A*24:13156Leushowed high levels of cell surface expression while HLA-A*24:02156Glnwas expressed at low levels in tapasin deficient cells. Peptides presented by these allelic variants showed distinct differences in features and repertoire. Immunoprecipitation experiments demonstrated all the HLA-A*24/156 variants to associate at similar levels with tapasin when present. Structurally, HLA-A*24:02 contains the residue triad Met97/His114/Gln156 and a Trp156 or Leu156 polymorphism provides tapasin independence by stabilizing these triad residues, thus generating an energetically stable and a more peptide receptive environment. Micropolymorphisms at position 156 can influence the generic peptide loading pathway for HLA-A*24 by altering their tapasin dependence for peptide selection. The trade-off for this tapasin independence could be the presentation of unusual ligands by these alleles, imposing significant risk following hematopoietic stem cell transplantation (HSCT).
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Yuan, Xin, Yingzhou Qin, Qingmei Tian, Cuijuan Liu, Xiangzhou Meng, Bo Qie, Fan Gao, et al. "Smart delivery of poly-peptide composite for effective cancer therapy." Biomedical Materials 17, no. 2 (January 24, 2022): 024103. http://dx.doi.org/10.1088/1748-605x/ac494c.

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Abstract In the past decade, multifunctional peptides have attracted increasing attention in the biomedical field. Peptides possess many impressive advantages, such as high penetration ability, low cost, and etc. However, the short half-life and instability of peptides limit their application. In this study, a poly-peptide drug loading system (called HKMA composite) was designed based on the different functionalities of four peptides. The peptide compositions of HKMA composite from N-terminal to C-terminal were HCBP1, KLA, matrix metalloproteinase-2 (MMP-2)-cleavable peptide and albumin-binding domain. The targeting and lethality of HKMA to NSCLC cell line H460 sphere cells and the half-life of the system were measured in vivo. The results showed that the HKMA composite had a long half-life and specific killing effect on H460 sphere cells in vitro and in vivo. Our result proposed smart peptide drug loading system and provided a potential methodology for effective cancer treatment.
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Ilca, F. Tudor, Andreas Neerincx, Mark R. Wills, Maike de la Roche, and Louise H. Boyle. "Utilizing TAPBPR to promote exogenous peptide loading onto cell surface MHC I molecules." Proceedings of the National Academy of Sciences 115, no. 40 (September 13, 2018): E9353—E9361. http://dx.doi.org/10.1073/pnas.1809465115.

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The repertoire of peptides displayed at the cell surface by MHC I molecules is shaped by two intracellular peptide editors, tapasin and TAPBPR. While cell-free assays have proven extremely useful in identifying the function of both of these proteins, here we explored whether a more physiological system could be developed to assess TAPBPR-mediated peptide editing on MHC I. We reveal that membrane-associated TAPBPR targeted to the plasma membrane retains its ability to function as a peptide editor and efficiently catalyzes peptide exchange on surface-expressed MHC I molecules. Additionally, we show that soluble TAPBPR, consisting of the luminal domain alone, added to intact cells, also functions as an effective peptide editor on surface MHC I molecules. Thus, we have established two systems in which TAPBPR-mediated peptide exchange on MHC class I can be interrogated. Furthermore, we could use both plasma membrane-targeted and exogenous soluble TAPBPR to display immunogenic peptides on surface MHC I molecules and consequently induce T cell receptor engagement, IFN-γ secretion, and T cell-mediated killing of target cells. Thus, we have developed an efficient way to by-pass the natural antigen presentation pathway of cells and load immunogenic peptides of choice onto cells. Our findings highlight a potential therapeutic use for TAPBPR in increasing the immunogenicity of tumors in the future.
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Sette, A., S. Southwood, J. Miller, and E. Appella. "Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II." Journal of Experimental Medicine 181, no. 2 (February 1, 1995): 677–83. http://dx.doi.org/10.1084/jem.181.2.677.

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Major histocompatibility complex class II-associated invariant chain (Ii) provides several important functions that regulate class II expression and function. One of these is the ability to inhibit class II peptide loading early in biosynthesis. This allows for efficient class II folding and egress from the endoplasmic reticulum, and protects the class II peptide binding site from loading with peptides before entry into endosomal compartments. The ability of Ii to interact with class II and interfere with peptide loading has been mapped to Ii exon 3, which encodes amino acids 82-107. This same region of Ii has been described as a nested set of class II-associated Ii peptides (CLIPs) that are transiently associated with class II in normal cells and accumulate in human histocompatibility leukocyte antigen-DM-negative cell lines. Currently it is not clear how CLIP and the CLIP region of Ii blocks peptide binding. CLIP may bind directly to the class II peptide binding site, or may bind elsewhere on class II and modulate class II peptide binding allosterically. In this report, we show that CLIP can interact with many different murine and human class II molecules, but that the affinity of this interaction is controlled by polymorphic residues in the class II chains. Likewise, structural changes in CLIP also modulate class II binding in an allele-dependent manner. Finally, the specificity and kinetics of CLIP binding to class II molecule is similar to antigenic peptide binding to class II. These data indicate that CLIP binds to class II in an analogous fashion as conventional antigenic peptides, suggesting that the CLIP segment of Ii may actually occupy the class II peptide binding site.
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Bednarek, M. A., S. Y. Sauma, M. C. Gammon, G. Porter, S. Tamhankar, A. R. Williamson, and H. J. Zweerink. "The minimum peptide epitope from the influenza virus matrix protein. Extra and intracellular loading of HLA-A2." Journal of Immunology 147, no. 12 (December 15, 1991): 4047–53. http://dx.doi.org/10.4049/jimmunol.147.12.4047.

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Abstract Influenza virus matrix protein-derived peptides were synthesized based on the amino acid motifs for HLA-A2 bound self peptides. Among these peptides a nonamer (amino acids 58 through 66: G I L G F V F T L) was found to be 100 to 1000 times more effective than the commonly used peptide 57-68 (K G I L G F V F T L T V) in sensitizing HLA-A2+ target cells to lysis by influenza virus specific cytotoxic T lymphocytes. The sensitizing activity of the 12-mer 57-68 was not due to contamination with shorter and more active peptides. Intracellular expression of peptide 58-66 (mediated by a stable expression plasmid with DNA coding for this peptide) also sensitized HLA-A2+ cells to lysis. Peptide 58-66 stimulated human PBMC to generate CTL that recognized peptides 58-66 and 57-68 in association with HLA-A2.
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Dissertations / Theses on the topic "Peptide loading"

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Gupta, Shashank. "Identification and characterization of peptide-like MHC-ligand exchange catalyst as immune response enhancer." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2009. http://dx.doi.org/10.18452/15904.

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MHC Klasse II Moleküle präsentieren Peptidantigene für die Überwachung durch CD4+ T Zellen an der Zelloberfläche. Um Sicherzustellen, dass diese Peptidliganden möglichst genau die intrazelluläre Proteinzusammensetzung widerspiegeln, hat sich im Verlauf der Evolution ein komplexer Prozessierungsweg entwickelt, welcher möglichst stabile Peptid/MHC Komplexe an die Zelloberfläche liefert. MHC Moleküle, welche ihren Liganden verloren haben, konvertieren zudem spontan in einen ‚nichtrezeptiven’ Zustand, was als zusätzlicher Sicherheitsmechanismus dient. Diese Studie zeigt jedoch, dass Aminosäureseitenketten kurzer Peptide diesen Sicherheitsmechanismus umgehen können indem sie katalytisch einen reversiblen Ligandenaustausch auslösen. Die katalytische Aktivität von Dipeptiden, wie z.B. Tyr-Arg (YR), war dabei stereospezifisch und konnte durch zusätzliche Modifikationen verstärkt werden, welche das konservierte H-Brückennetzwerk der so genannten P1-Tasche des MHC Moleküls adressierten. Die Dipeptide verstärkten dabei sowohl die Antigenbeladung als auch den Ligandenaustausch, wobei deren relative Aktivität genau mit den bekanten Ankerpräferenzen der P1 Tasche korrelierte. Letzteres weist somit auf eine direkte Interaktion der katalytischen Seitenkette des Dipeptides mit dieser Tasche hin. Der Verstärkungseffekt war auch in CD4+ T Zellassays zu beobachten, bei denen der alleleselektive Einfluss der Dipeptide direkt in eine deutliche Erhöhung der Sensitivität der antigenspezifischen T Zellantwort führte. Durch weitere molekulardynamische Berechnungen konnte die Hypothese unterstützt werden, dass die Besetzung der P1 Tasche durch Aminosäureseitenketten einen Kollaps der leeren Bindungstasche zum ‚nichtrezeptiven’ Zustand verhindert. Während der Antigenpräsentation könnte P1 somit unmittelbar als ‚Sensor’ für die Beladung mit Peptiden dienen. Diese Annahme konnte experimentell durch spektroskopische Untersuchungen unter Verwendung des ANS-Farbstoffes (8-Anilino-1-Naphtalensulfonsäure) sowie durch Messung der intrinsischen Tryptophanfluoreszenz bestätigt werden. Darüber hinaus konnten konformationsspezifische Antikörper, welche bislang lediglich mit unbeladenen MHC Molekülen in Verbindung gebracht wurden, hier als spezifische Sonden für den nichtrezeptiven Zustand definiert werden. Als mögliche Risikofaktoren könnten katalytische kurze Peptide eine Rolle bei der Auslösung von Autoimmunerkrankungen spielen. In dieser Studie konnte gezeigt werden, dass sie die Beladung von Glutenantigenen auf das Zöliakie-assozierte HLA-DQ2 Molekül verstärken können. Zumindest in vitro konnte ihre Anwesenheit deshalb auch die antigenspezifische Antwort von CD4+ T Zellen verstärken, welche zuvor von Zöliakiepatienten isoliert worden waren. Auf der einen Seite könnten diese Peptide als ‚MHC-loading enhancer’ (MLE) deshalb als mögliche Risikofaktoren die Ausbildung entzündlicher (Auto-) Immunerkrankungen beschleunigen. Auf der anderen Seite könnten sie jedoch auch als ‚drug-like’ Vakzinadditiv zur Verbesserung von Immuntherapien führen.
MHC class II molecules present antigenic peptides on the cell surface for the surveillance by CD4+ T cells. To ensure that these ligands accurately reflect the content of the intracellular MHC loading compartment, a complex processing pathway has evolved that delivers only stable peptide/MHC complexes to the surface. As additional safeguard mechanism, MHC molecules quickly acquire a ‘non-receptive’ state once they have lost their ligand. This study shows that amino acid side chains of short peptides can bypass these safety mechanisms by triggering the reversible ligand-exchange. The catalytic activity of dipeptides such as Tyr-Arg (YR) is stereo-specific and could be enhanced by modifications addressing the conserved H-bond network near the P1 pocket of the MHC molecule. It enhanced both antigen-loading and ligand-release and strictly correlated with reported anchor preferences of P1, the specific target site for the catalytic side chain of the dipeptide. The effect was evident also in CD4+ T cell assays, where the allele-selective influence of the dipeptides translated into increased sensitivities of the antigen-specific immune response. The hypothesis that occupation of P1 prevents the ‘closure’ of the ‘empty’ peptide binding site into the ‘non-receptive’ state was further supported by molecular dynamic calculations. During antigen processing and presentation P1 may therefore function as important ‘sensor’ for peptide-load. Spectroscopic studies using ANS dye (8-aninilino-1-napthalenesulfonic acid) and intrinsic tryptophan fluorescence data, confirm the postulate by providing direct evidence for the conformational transitions. Moreover conformation specific antibodies previously described to be specific for ‘empty’ MHC could be shown to be a ‘probe’ for ‘receptive conformation’. As potent risk factors short peptides may be involved in the induction of autoimmune diseases. It could be shown here that they could enhance the loading of gluten derived antigen on celiac disease linked-HLA-DQ2 allele. At least in vitro the effect could enhance gluten specific CD4+ T cell response on T cell clones obtained from celiac disease patients. Thus, on one hand short peptides might work as ‘MHC loading enhancer’ (MLE) in the precipitation of inflammatory-‘autoimmune’ disorder, on the other hand they might be used as drug like vaccine ‘additive’ in various therapeutic settings.
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Urban, Sabrina. "Die Rolle von Aminopeptidasen in der MHC Klasse I Antigenprozessierung des HLA-A2-restingierten HCMV pp 65 495-503 Epitops im Zusammenhang mit dem peptide-loading complex." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2009. http://dx.doi.org/10.18452/15996.

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Das Ubiquitin Proteasom System generiert die Mehrheit der antigenen Peptide, die zusammen mit MHC Klasse I Molekülen präsentiert werden, wobei durch Kooperation mit alternativen proteolytischen Systemen die Vielfalt der möglichen MHC I Liganden erhöht wird. In diesem Zusammenhang, insbesondere im Rahmen einer Immunantwort, ist die Rolle von Aminopeptidasen bislang nur ungenügend charakterisiert. In der vorliegenden Arbeit wurde der modulatorische Einfluss von zytosolischen und im ER lokalisierten Aminopeptidasen auf die Generierung des HCMV pp65495-503 Epitops durch Prozessierung von proteasomal generierten Peptidprodukten untersucht. Dafür wurde in pp65 exprimierenden Zellen die Expression einzelner Aminopeptidasen mittels siRNA inhibiert und der Effekt auf die Epitoppräsentation über die Aktivierung pp65495-503 spezifischer CTL bestimmt. Es zeigte sich, dass TPPII, LAP, AP-B und POP limitierend auf die Epitoppräsentation wirken. Damit wurden die Peptidasen AP-B und POP erstmalig in direkten Zusammenhang mit der MHC Klasse I Antigenprozessierung gebracht. Analysen weiterer zytosolischer Peptidasen wie TOP, BH und PSA zeigten keinen signifikanten Effekt auf die Epitoppräsentation, so dass diese Peptidasen an der zellulären Prozessierung des pp65 Antigens nicht beteiligt sind. Die Trimmaktivität von ERAPI und ERAPII im ER hingegen hatte einen bedeutenden Anteil an der pp65495-503 Epitopgenerierung. In Immunpräzipitationsexperimenten konnte zudem die Interaktion der ER Aminopeptidasen mit dem peptide-loading complex zum ersten Mal nachgewiesen werden. Die vorliegenden Daten geben Hinweise darauf, dass die Interaktion von ERAPI und ERAPII mit dem Komplex unabhängig von dessen vollständiger Assemblierung mit dem TAP Transporter stattfinden kann und vermutlich über Tapasin vermittelt wird. Da diese Assoziation durch IFNgamma induziert wird, könnte sie zu einer effizienteren Antigenprozessierung und -Präsentation, vor allem unter Infektionsbedingungen, beitragen.
The ubiquitin proteasome system is responsible for the generation of the majority of MHC class I presented antigenic peptides. By cooperation with alternative proteolytic systems the diversity of MHC class I ligands is increased. In this context, especially during immune response, the role of aminopeptidases is barely characterised. In this project the effect of cytosolic and ER-resident aminopeptidases on processing of proteasomal generated peptides was investigated with regard to HCMV pp65495-503 epitope generation. Therefore, expression level of single aminopeptidases was down regulated by siRNA in pp65 expressing cells and the effect of down regulation on epitope presentation was analysed by activation of pp65495-503 specific CTLs. It could be demonstrated that TPPII, LAP, AP-B and POP have negative effects on pp65 epitope presentation. With AP-B and POP two additional cytosolic aminopeptidases with a functional role in epitope processing were identified. Other aminopeptidases, that have been characterised as part of the antigen processing machinery, namely TOP, BH and PSA, did not affect pp65 epitope generation. In contrast, trimming by ERAPI and ERAPII in the ER resulted in an efficient epitope presentation. For the first time, experimental evidence was provided that the two ER-resident peptidases interact with the MHC class I peptide-loading complex (PLC). The obtained results indicate that this association takes place independently of the assembly of the entire complex including TAP and is probably mediated by tapasin. The observation that this complex formation is inducible by IFNgamma suggests that the association of ERAPI and ERAPII to the PLC accounts for a better antigen processing and presentation mainly at the site of infection.
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Du, Tingting. "Dissecting Small RNA Loading Pathway in Drosophila melanogaster: A Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/356.

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In the preceding chapters, I have discussed my doctoral research on studying the siRNA loading pathway in Drosophila using both biochemical and genetic approaches. We established a gel shift system to identify the intermediate complexes formed during siRNA loading. We detected at least three complexes, named complex B, RISC loading complex (RLC) and RISC. Using kinetic modeling, we determined that the siRNA enters complex B and RLC early during assembly when it remains double-stranded, and then matures in RISC to generate Argonaute bearing only the single-stranded guide. We further characterized the three complexes. We showed that complex B comprises Dcr-1 and Loqs, while both RLC and RISC contain Dcr-2 and R2D2. Our study suggests that the Dcr-2/R2D2 heterodimer plays a central role in RISC assembly. We observed that Dcr-1/Loqs, which function together to process pre-miRNA into mature miRNA, were also involved in siRNA loading. This was surprising, because it has been proposed that the RNAi pathway and miRNA pathway are separate and parallel, with each using a unique set of proteins to produce small RNAs, to assemble functional RNA-guided enzyme complexes, and to regulate target mRNAs. We further examined the molecular function of Dcr-1/Loqs in RNAi pathway. Our data suggest that, in vivo and in vitro, the Dcr-1/Loqs complex binds to siRNA. In vitro, the binding of the Dcr-1/Loqs complex to siRNA is the earliest detectable step in siRNA-triggered Ago2-RISC assembly. Futhermore, the binding of Dcr-1/Loqs to siRNA appears to facilitate dsRNA dicing by Dcr-2/R2D2, because the dicing activity is much lower in loqslysate than in wild type. Long inverted repeat (IR) triggered white silencing in fly eyes is an example of endogenous RNAi. Consistent with our finding that Dcr-1/Loqs function to load siRNA, less white siRNA accumulates in loqs mutant eyes compared to wild type. As a result, loqs mutants are partially defective in IR trigged whitesilencing. Our data suggest considerable functional and genetic overlap between the miRNA and siRNA pathways, with the two sharing key components previously thought to be confined to just one of the two pathways. Based on our study on siRNA loading pathway, we also elucidated the molecular function of Armitage (Armi) protein in RNAi. We showed that armi is required for RNAi. Lysates from armi mutant ovaries are defective for RNAi in vitro. Native gel analysis of protein-siRNA complexes suggests that armi mutants support early steps in the RNAi pathway, i.e., the formation of complex B and RLC, but are defective in the production of the RISC.
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Chen, Yan. "Identification of new components of the MHC class I peptide loading complex." 2006. http://link.library.utoronto.ca/eir/EIRdetail.cfm?Resources__ID=450472&T=F.

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Chu, Ya-Chun, and 朱雅郡. "Preparation of gelation nanocarrier with gp91 peptide loading for corneal neovascularization treatment." Thesis, 2017. http://ndltd.ncl.edu.tw/handle/d9bdhk.

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碩士
國立臺北科技大學
生化與生醫工程研究所
105
Healthy cornea is a transparent, avascular tissue that allows light to pass through. The process of abnormal vessels growing into the cornea from limbus, is called corneal neovascularization (CNV). CNV may disturb the light go through the cornea, which can result in decreased vison or even blindness. Type 2 nicotinamide adenine dinucleotide phosphate-oxidase (Nox2) is the subunit of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase that plays a role in angiogenesis. A peptide called gp91-ds-tat (gp91) is a specific and effective inhibitor for Nox2. The gp91 peptide can decrease the generation of reactive oxygen species (ROS) and the expression of vascular endothelial growth factor (VEGF). Therefore, in this study, we selected gp91 peptide as the drug to inhibit the angiogenesis. Eye drops are the most common way to treat ocular diseases due to its low bioavailability on ocular surface resulted in unsatisfied therapeutic effect. Nowadays, nanomedicine as eyedrop can increase drug retain on eyes, then improve therapeutic effect drawing attention for eye disease treatment including CNV. In this study, we developed gelatin nanoparticles loaded with gp91 peptide (GNP-gp91) as a nanomedicine to inhibit angiogenesis in eyes. Firstly, GNP-gp91 nanoparticles were synthesized, and its particle size/zeta potential were exanimated. In vitro study, we co-culture the GNP-gp91 with the human umbilical vein endothelial cells (HUVEC) to evaluate the cell viability by WST-8 and live/dead staining methods. The inhibitory effect for HUVECs of GNP-gp91 was tested by cell migration, transwell cell migration, tube formation and ROS generation assays. In vivo test, we observed the retention of nanomedicine on ocular surfaces of mice by non invasion in vivo imaging system (IVIS). We established a mouse CNV model to evaluate the therapeutic effect of GNP-gp91 as eyedrop by every two days treatmen. In conclusion, we successfully prepared the GNP-gp91 in the size of 550.6 ± 61.2 nm, and the zeta potential of 21.7 ± 1.8 mV which is good for ocular drug delivery. The TEM images showed that these particles have spherical morphology. In the in vitro study, we found that GNP-gp91 was non-cytotoxicity and can significantly inhibit cell viability at the peptide concentration of 100 μg/mL. Cell migration demonstrated that GNP-gp91 was more effective for inhibiting HUVEC cells migration than the gp91 in solution at 6 and 8 hours. From the in vivo study, the retention time of GNP-gp91 on ocular surface is longer then solution form in normal cornea. We successfully established the CNV model and the therapeutic effect of GNP-gp91 is greater than gp91 in solution. And VEGF expression of total cornea lysis showed decreasing after ocular surface treatment with GNP-gp91. Overall, GNP-gp91 was produced in nano-size, and it can effectively inhibit the migration/tube formation of HUVEC at peptide concentration of 100 μg/mL. In vivo evaluation shows that mice treated with GNP-gp91 as eye drop had better anti-angiogenesis in corneal at day 7 after every-two days treatment. We believe that GNP-gp91 nanomedicine as eye drop has the potential to treat CNV as eye drop in an easy way in the future for clinical application.
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6

Sever, Lital. "A Functional Study of the Major Histocompatibility Class I Antigen Presentation Pathway in Rainbow Trout (Oncorhynchus mykiss)." Thesis, 2014. http://hdl.handle.net/10012/8135.

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Major Histocompatibility Complex (MHC) class I receptors are glycoproteins which play a critical role in anti-viral immunity by displaying foreign peptides to cytotoxic T cell lymphocytes. The loading of high affinity peptides into the MHC class I receptor in mammals is coordinated by a multiple proteins that are collectively referred to as the peptide loading complex (PLC). To date, the composition of the peptide loading complex in fish is unknown and therefore the characterization of the molecules which may exist in this putative complex was pursued. This thesis includes the cloning and functional characterization of ERp57 and calnexin in rainbow trout which, in mammals, are known to interact with the MHC class I receptor either during its early biogenesis or later in the assembly of the PLC. Trout ERp57 and calnexin cDNA sequences are ubiquitously expressed in trout tissues and both the ERp57 and calnexin genes appear in at least two copies each in the trout genome. Interestingly, despite their high sequence identity with their mammalian homologues, some structural discrepancies were identified. ERp57 does not contain an endoplasmic reticulum (ER) retention signal or a nuclear localization signal, while one of the two isolated cDNA clones for calnexin does not contain an ER (endoplasmic reticulum) retention signal and lacks a conserved C-terminal serine phosphorylation site. These findings suggest that in trout, there may be unique versions of these proteins that have acquired different cellular functions. Through the production of polyclonal antibodies against trout ERp57, the conserved protein induction of ERp57 during ER stress was demonstrated concurrently with calnexin. In addition, this study shows for the first time that ERp57 can be induced transcriptionally by phytohemagglutinin and synthetic double stranded RNA, which implies its possible regulatory role during viral infection and the activation of the immune response. Furthermore, the functional characterization of the MHC class I specific chaperone tapasin, a key element in the PLC of mammals was pursued. Tissue and cell line distribution revealed that tapasin is expressed in high levels in immune system organs and in the rainbow trout macrophage cell line RTS11, at a relative molecular weight of 48 kDa with an additional 20 kDa band detected by the tapasin antibody. Tapasin protein was significantly up regulated upon exposure to synthetic double stranded RNA and during infection with two fish viruses: chum salmon virus and viral hemorrhagic septicemia virus genotype IVa, whereas the expression of the 20 kDa band was not affected by these stimuli. This study also examined the regulation of the MH class I heavy chain,β2 microglobulin and their associated machinery upon exposure to viral hemorrhagic septicemia virus genotype IVa at permissive and non-permissive temperatures. β2 microglobulin secretion into the cell media, a marker of MH class I receptor turnover, was detected in the conditioned media of RTS11 cells under normal conditions and was shown to be significantly enhanced during viral hemorrhagic septicemia virus genotype IVa infection. Furthermore, when RTS11 cells were maintained at cold temperatures, the secretion of β2 microglobulin was significantly reduced in both infected and non-infected cultures, while the cellular levels of β2 microglobulin remained unchanged. These results suggest that cold temperature can alter the expression of the MH class I molecule on the cell surface and therefore may be contributing to host susceptibility to viral hemorrhagic septicemia virus genotype IVa during the winter. Lastly, Co-immunoprecipitation demonstrated the interaction of the lectin chaperones: calnexin and calreticulin with the glycosylated MH class I receptor supporting their conserved role during MH class I receptor folding in fish. Concurrently, tapasin's interaction with transporter associated with antigen processing (TAP) and with the glycosylated form of the MH class I was revealed for the first time in fish, which supports their role in antigen presentation as in mammals. This study demonstrated that ERp57 and tapasin form a conserved disulfide linked heterodimer of 110 kDa, however unlike mammals, an additional 75 kDa heterodimer was detected which suggests a possible novel interaction of ERp57 with a 20 kDa tapasin version alternately regulating antigen presentation in fish. Overall, this study suggest that the interactions involved in antigen presentation in mammals are conserved in fish, however the presence of different protein versions of calnexin, ERp57 and tapasin might dictate a different mode of regulation for MH class I assembly in fish, as opposed to mammals. Elucidating these interactions during various viral infections in fish can help to uncover possible viral strategies to manipulate the host immune response and will provide information needed to assist in designing novel tools to prevent fish viral diseases.
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Urban, Sabrina [Verfasser]. "Die Rolle von Aminopeptidasen in der MHC-Klasse-I-Antigenprozessierung des HLA-A2-restingierten HCMV- pp65495-503-Epitops im Zusammenhang mit dem peptide-loading complex / von Sabrina Urban." 2009. http://d-nb.info/999433946/34.

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Mácha, Hynek. "Vývoj metody pro stanovení loadingu aminokyselin při syntéze peptidů na pevné fázi." Master's thesis, 2018. http://www.nusl.cz/ntk/nusl-380289.

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A simple method has been developed to determine amino acid loading in solid phase peptide synthesis. The method is applicable for the most common type of synthesis, which use FMOC as protective group and piperidine as a deprotecting agent. Both products of deprotection reaction are separated by HPLC and determined using an UV detector; an internal standard is added. The method gives true values that have been verified by an independent method. The RSD is 1.52%. The method is more accurate than the published methods and allows the determination from the waste of synthesis. The employing of the internal standard eliminated the necessity of dilution accuracy or known volumes.
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9

Huang, Wei-Ting, and 黃唯婷. "Fabrication of Gold Nanoparticles-Based Platforms for Assaying Peptidase Activity and Loading Drugs." Thesis, 2011. http://ndltd.ncl.edu.tw/handle/08854534097367288843.

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碩士
國立交通大學
分子醫學與生物工程研究所
99
Gold nanoparticles (AuNPs) have received interests due to their characteristics, especially optical and physical properties. In this research, the optical biosensing and fluorescent platforms were developed. Both AuNPs-based biosensing platforms were set up based on the surface plasmon resonance (SPR) property of AuNPs to detect certain peptidase activity. Additionally, the surface-modified techniques of AuNPs were also utilized on the drug load and delivery. The AuNPs-based optical biosensing system was established by means of the varied SPR spectra of AuNPs, while AuNPs changed their sizes, included aggregation or modified with functional molecules. According to the mechanism, AuNPs modified with peptide (AuNP/peptide) that was used as a peptidase (matrix metalloprotease-2; MMP-2) substrate and also a shelter to protect AuNPs from aggregation. After MMP-2 digested, AuNPs became aggregation because of decreasing the steric repulsion among AuNPs. The aggregation of AuNPs was measured via the red-shift of SPR absorption. Therefore, the MMP-2 activity could be quantitatively estimated by the absorption ratio, A625 nm/A530 nm. The results show that the detection limit of the established platform was 100 ng/mL, a linear correlation between MMP-2 was ranging from 100 to 1,500 ng/mL, and the changes of A625 nm/A530 nm was observed (R2 = 0.9703). For improving the sensitivity of AuNPs-based platform, the peptide was exchanged with peptide-FITC as substrate modified on AuNPs to establish AuNPs-based fluorescence platform. The FITC would be quenched by AuNPs when the peptide-FITC modified on AuNPs surface. The fluorescence intensity of FITC was detected after MMP-2 digested the peptide leading peptide-FITC released from AuNPs surface. According to the concept, the MMP-2 activity could be analyzed by measuring the change of fluorescence intensity (at emission of FITC, 515 nm). The AuNPs-based fluorescence platform performed a detection limit as 0.01 ng/mL, with a linear correlation ranging from 0.01 to 2 ng/mL of MMP-2 (R2 = 0.9759). Additionally, both AuNPs-based optical and fluorescence platforms showed the ability to assay the efficiency of MMPs inhibitors with high specificity. Especially, the AuNPs-based fluorescence platform could apply in cellular peptidase activity analysis through bio-image (confocal) that revealed a promising potential to utilize in in vivo peptidase detection. On the other hand, the AuNPs-based delivery platform was fabricated due to the biocomplementary and various surface modifications of AuNPs through special molecules with their functional groups. Based on the concept, the AuNPs were conjugated with human growth hormone protein (hGH) used to target the hGH receptor of HepG2 cells, and Raman reporter (malachite green isothiocyanate; MGITC) as tags. After incubating the AuNPs-complexes with HepG2 cells, the AuNPs specifically targeted to the cells and could be traced in cells by surface-enhanced Raman scattering through Raman confocal. In addition, AuNPs were also used as drug delivery carrier by modifying AuNPs with hGH and anticancer drug, doxorubicin. Using AuNPs/hGH-doxorubicin could bind HepG2 cells precisely and inhibit the growth of cancer cells at the same time. This result indicates that the multifunctional AuNPs improved the effective of the medicine in vitro according to selective targeting and treating drug to the objective in once.
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Jao, Chia-Ai, and 饒佳艾. "Association Between Periodontal Disease and Alzheimer’s Disease--From Amyloid-β Peptide Loading：A Systematic Review and Meta-Analysis." Thesis, 2019. http://ndltd.ncl.edu.tw/handle/fy67x8.

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Books on the topic "Peptide loading"

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Yan, Chen. Identification of new components of the MHC class I peptide loading complex. 2006.

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Book chapters on the topic "Peptide loading"

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Kim, AeRyon, Isabel Emiko Ishizuka, Isamu Z. Hartman, Yuri Poluektov, Kedar Narayan, and Scheherazade Sadegh-Nasseri. "Studying MHC Class II Peptide Loading and Editing In Vitro." In Antigen Processing, 343–55. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9450-2_24.

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Kim, AeRyon, Isabel Ishizuka, Isamu Hartman, Yuri Poluektov, Kedar Narayan, and Scheherazade Sadegh-Nasseri. "Studying MHC Class II Peptide Loading and Editing In Vitro." In Antigen Processing, 447–59. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-218-6_33.

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Bouvier, Marlene. "Studying MHC Class I Peptide Loading and Exchange In vitro." In Antigen Processing, 81–91. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-218-6_7.

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Bouvier, Marlene. "In Vitro Studies of MHC Class I Peptide Loading and Exchange." In Antigen Processing, 71–81. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9450-2_6.

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Margulies, David H., Jiansheng Jiang, and Kannan Natarajan. "Structure and Function of Molecular Chaperones that Govern Immune Peptide Loading." In Subcellular Biochemistry, 321–37. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-28151-9_10.

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Wearsch, Pamela A., and Peter Cresswell. "In Vitro Reconstitution of the MHC Class I Peptide-Loading Complex." In Antigen Processing, 67–79. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-218-6_6.

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Hou, Tieying, Cornelia Rinderknecht, Debopam Ghosh, Andreas V. Hadjinicolaou, Robert Busch, and Elizabeth D. Mellins. "Pulse–Chase Analysis for Studies of MHC Class II Biosynthesis, Maturation, and Peptide Loading." In Antigen Processing, 315–41. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9450-2_23.

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Hou, Tieying, Cornelia H. Rinderknecht, Andreas V. Hadjinicolaou, Robert Busch, and Elizabeth Mellins. "Pulse–Chase Analysis for Studies of MHC Class II Biosynthesis, Maturation, and Peptide Loading." In Antigen Processing, 411–32. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-218-6_31.

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Sambhi, M., M. Kohno, and K. Clegg. "Salt Loading in Spontaneously Hypertensive Rats Further Elevates Blood Pressure Despite Enhanced Release of Atrial Natriuretic Peptides and Exaggerated Natriuresis." In Diuretics: Basic, Pharmacological, and Clinical Aspects, 140–44. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-2067-8_34.

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Call, Melissa J. "Peptide Loading of MHC." In Handbook of Biologically Active Peptides, 687–96. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-385095-9.00093-2.

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Conference papers on the topic "Peptide loading"

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Piehowski, Paul D., Yang Wang, James A. Sanford, Joshua R. Hansen, Marina A. Gritsenko, Vladislav A. Petyuk, Karl K. Weitz, et al. "Abstract 5125: Evaluation of differential peptide loading on TMT-based proteomic on phosphoproteomic data quality in an AML model." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-5125.

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Chen, Jing, and Sihong Wang. "Thermal Effects on Osteogenesis of Human Mesenchymal Stem Cells." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80885.

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Intensive studies were reported on the osteogenesis of mesenchymal stem cells (MSC) using chemicals and mechanical loading. However, the maturity of differentiated osteoblasts is not same as that of isolated adult osteoblasts. Thermal treatment could be a missing factor in stem cell differentiation. It was reported that mild heat stimulated bone growth in animal experiments [1–2]. Thermal treatment is also used as a therapy to promote bone repair after injury [3]. In addition, hot shower daily is recommended to osteoarthritis patients. However, the mechanisms for the heat-induced osteogenesis are not completely known and the thermal regulation of human mesenchymal stem cells (hMSCs) differentiation is not well studied. In this study, the direct effects of mild heat shock (HS) on the differentiation of hMSCs into osteoblasts in self-assembling peptide hydrogel were investigated.
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Keten, Sinan, and Markus J. Buehler. "Elasticity and Strength of Beta-Sheet Protein Materials: Geometric Confinement and Size Effects." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205464.

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Elasticity and strength of proteins influence their biological functions. Under external forces, many proteins exhibit entropic elasticity with a characteristic stiffening elastic behavior and unravel due to the rupture of interstrand H-bonds. We develop a fracture mechanics based theoretical framework that considers the free energy competition between entropic elasticity of polypeptide chains and rupture of peptide hydrogen bonds, which we use here to provide an explanation for the intrinsic strength limit of protein domains at vanishing rates [1, 2]. Our analysis predicts that individual protein domains stabilized only by hydrogen bonds cannot exhibit rupture forces larger than 100–300 pN in the asymptotic quasi-static limit. This result explains earlier experimental and computational observations that suggest such a universal, asymptotic strength limit at vanishing pulling rates. We show that the rupture strength of H-bond assemblies in beta-sheets is governed by geometric confinement effects, suggesting that clusters of at most 3–4 H-bonds break concurrently, even under uniform shear loading of a much larger number of H-bonds. These strength, elasticity and size effect predictions all agree well with recent experimental findings and proteomics data. Our model confirms that fracture mechanics concepts, previously primarily applied to macroscale fracture phenomena, can also be directly applied at nanoscale, to be used for describing failure mechanisms in protein materials. Our strength and optimal size predictions lead to a key hypothesis: confined H-bond clusters are prevalent in alpha helices, beta-sheets and beta-solenoids, perhaps as an evolutionary design principle that derives from generic mechanical properties of the fundamental building blocks of life.
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Downie, LS, LM Work, and SA Nicklin. "10 Endogenous and exogenous loading of extracellular vesicles for therapeutic delivery of renin-angiotensin system peptides in cardiomyocyte hypertrophy." In The Scottish Cardiovascular Forum 2018, 3rd February 2018, Trinity Biomedical Science Institute, Trinity College Dublin Ireland. BMJ Publishing Group Ltd and British Cardiovascular Society, 2018. http://dx.doi.org/10.1136/heartjnl-2018-scf.10.

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