专肽生物_定制多肽合成服务_多肽合成定制服务_多肽合成厂家_多肽合成公司

"Peptide H-QYDPVAALF-OH is a Research Peptide with significant interest within the field academic and medical research. Recent citations using H-QYDPVAALF-OH include the following: Identification of HLA-A2 or HLA-A24-restricted CTL epitopes for potential HSP105-targeted immunotherapy in colorectal cancer YU Sawada, H Komori, Y Tsunoda - Oncology , 2014 - spandidos-publications.comhttps://www.spandidos-publications.com/10.3892/or.2013.2941 Characterization of cytomegalovirus pp65-HLA-A24 peptide-specific CTL lines from metastatic melanoma patients Y Akiyama, S Tai, M Komiyama - Oncology , 2009 - spandidos-publications.comhttps://www.spandidos-publications.com/or/22/1/185 Identification of HLA-A24-restricted CTL epitope encoded by the matrix protein pp65 of human cytomegalovirus Y Akiyama, K Maruyama , T Mochizuki, K Sasaki - Immunology letters, 2002 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0165247802000731 Analysis of HLA-A24-restricted CMVpp65 peptide-specific CTL with HLA-A* 2402-CMVpp65 tetramer Y Akiyama, K Kuzushima, T Tsurumi, K Yamaguchi - Immunology letters, 2004 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0165247804002007 A Unique Immunotherapeutic Atrategy by Using a Leukemic Plasmacytoid Dendritic Cell Line (PMDC05) as Potent Antigen Presenting Cells. T Nakamura, M Narita, A Yamahira, N Watanabe - Blood, 2009 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0006497119579174 Efficient cross-presentation by heat shock protein 90-peptide complex-loaded dendritic cells via an endosomal pathway T Kurotaki, Y Tamura, G Ueda, J Oura - The Journal of , 2007 - journals.aai.orghttps://journals.aai.org/jimmunol/article/179/3/1803/79146 Correlations of programmed death 1 expression and serum IL-6 level with exhaustion of cytomegalovirus-specific T cells after allogeneic hematopoietic stem cell T Kato, T Nishida, Y Ito , M Murase, M Murata - Cellular immunology, 2014 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0008874914000331 Correlation of serum IL-6 level with exhaustion of cytomegalovirus-specific T cells after hematopoietic stem cell transplantation T Kato, T Nishida, M Murase, Y Ito, M Murata, T Naoe - Blood, 2011 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0006497119582921 Exhaustion of CMV specific T cells with enhanced PD-1 expression in persistent cytomegalovirus infection after allogeneic stem cell transplantation T Kato, T Nishida, M Murase, M Murata, T Naoe - Blood, 2010 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0006497119459788 Phase I clinical trial of the vaccination for the patients with metastatic melanoma using gp100-derived epitope peptide restricted to HLA-A* 2402 T Baba, M Sato-Matsushita, A Kanamoto, A Itoh - Journal of translational , 2010 - Springerhttps://link.springer.com/article/10.1186/1479-5876-8-84 Identification of a novel HLA-A* 24: 02-restricted adenovirus serotype 11-specific CD8+ T-cell epitope for adoptive immunotherapy N Imahashi, T Nishida, Y Ito, J Kawada - Molecular , 2013 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0161589013004008 Identification of a novel HLA-A24-restricted cytotoxic T lymphocyte epitope peptide derived from mesothelin in pancreatic cancer M Tsukagoshi, S Wada , S Hirono, S Yoshida, E Yada - Oncotarget, 2018 - ncbi.nlm.nih.govhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6101134/ Analysis of memory T lymphocyte activity following stimulation with overlapping HLA-A* 2402, A* 0101 and Cw* 0402 restricted CMV pp65 peptides M Ghei, DF Stroncek, M Provenzano - Journal of Translational Medicine, 2005 - Springerhttps://link.springer.com/article/10.1186/1479-5876-3-23 Analysis of Memory T Lymphocytes Activity Following Stimulation with HLA-A24, A1 and Cw4 Restricted 9-and 10-mer Cytomegalovirus pp65 Overlapping Peptides. M Ghei, DF Stroncek, M Provenzano - 2004 - ashpublications.orghttps://ashpublications.org/blood/article-abstract/104/11/2876/55187 Phase I clinical trial of human vascular endothelial growth factor receptor 1 peptide vaccines for patients with metastatic renal cell carcinoma K Yoshimura, T Minami, M Nozawa - British journal of cancer, 2013 - nature.comhttps://www.nature.com/articles/bjc201390 The forkhead box M1 transcription factor as a candidate of target for anti-cancer immunotherapy K Yokomine, S Senju, T Nakatsura, A Irie - journal of cancer, 2010 - Wiley Online Libraryhttps://onlinelibrary.wiley.com/doi/abs/10.1002/ijc.24836 Efficient identification of HLA-A*2402-restricted cytomegalovirus-specific CD8+ T-cell epitopes by a computer algorithm and an enzyme-linked immunospot assay K Kuzushima, N Hayashi, H Kimura - Blood, The Journal of , 2001 - ashpublications.orghttps://ashpublications.org/blood/article-abstract/98/6/1872/134109 Improved expression of HLA-A* 2402-BSP in Escherichia coli and its tetramer preparation JIA Qian-Tao, XU Li-Hui, LI Feng-Yao - Chinese Journal of , 2007 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1872207507600259 Reconstitution of HLA-A* 2402-restricted cytomegalovirus-specific T-cells following stem cell transplantation H Gondo, D Himeji, K Kamezaki, A Numata - International journal of , 2004 - Springerhttps://link.springer.com/article/10.1532/IJH97.04109 Identification of novel CTL epitopes of CMV-pp65 presented by a variety of HLA alleles E Kondo , Y Akatsuka, K Kuzushima, K Tsujimura - Blood, 2004 - ashpublications.orghttps://ashpublications.org/blood/article-abstract/103/2/630/17819 Generation of CMV-specific T lymphocytes using protein-spanning pools of pp65-derived overlapping pentadecapeptides for adoptive immunotherapy D Trivedi, RY Williams, RJ OReilly, G Koehne - Blood, 2005 - ashpublications.orghttps://ashpublications.org/blood/article-abstract/105/7/2793/20239 Peptide intra-tumor injection for cancer immunotherapy: enhancement of tumor cell antigenicity is a novel and attractive strategy D Nobuoka, T Yoshikawa, T Fujiwara - Human vaccines & , 2013 - Taylor & Francishttps://www.tandfonline.com/doi/abs/10.4161/hv.23990 Recognition and Killing of Brain Tumor Stem-Like Initiating Cells by CD8+ Cytolytic T Cells CE Brown , R Starr, C Martinez, B Aguilar, M DApuzzo - Cancer research, 2009 - AACRhttps://aacrjournals.org/cancerres/article-abstract/69/23/8886/552748"

Definition
The commonly used cytomegalovirus (CMV) peptides used for therapeutic approaches are pp65 and pp71. pp65 is also known as glycoprotein 64 or UL83 is a virion tegument protein and the main component of the enveloped subviral particle of CMV. The human cytomegalovirus (HCMV) tegument protein pp71 is an upper matrix protein  involved in gene regulation and is encoded by gene UL82.

Discovery
The identification of DNA sequences coding for a virion phosphoprotein of 71 kDa and a viral 65-kDa polypeptide was done by Nowak B et.al, in early in 1980s1.

Structural Characteristics
CMV pp65 belongs to the herpesviridae pp65 family. HCMV contains a phosphorylated matrix protein of 65,000 apparent molecular weight (65K phosphoprotein; pp65) and a related phosphoprotein of 71,000 molecular weight (pp71). The 65K phosphoprotein is usually by far the most abundant structural component found in culture-grown purified virus particles. The 65K phosphoprotein is coded for by the 5'-terminal part of an abundant 4-kilobase (kb) mRNA. The structural protein pp65 forms about 95% of the protein mass in dense bodies. The nucleotide sequence of the entire coding domain for pp65 and pp7l,identifies separate translational reading frames and transcripts for each protein, and analyzes their RNA structures. CMV pp65 contains elements of the prototypic nuclear localization signal (NLS) in which arginine and lysine predominate within a bipartite motif in which short regions of basic amino acids are separated by 10 or more nonconserved amino acids. The nuclear localization signals of CMV pp65 consist of at least two such motifs located in the carboxy-terminal region of the polypeptide.A second NLS of CMV pp65 consists of a basic region of amino acids between aa 537 and 561; this region was termed the C-D motif by Schmolke et al,2, 3. The primary sequence of HCMV is Asn-Leu-Val-Pro-Met-Val-Ala-Thr-Val.

Mode  of Action
CMV pp65 as a nucleotropic protein which enters the nucleus immediately after infection. It binds to polo-like kinase 1 (PLK-1), an enzyme important in mitosis and it is likely that the protein has specific effects on cell cycle events 4. CMV pp65 has been shown to have protein kinase activity. CMV pp65 is an immunodominant target of CD4+ and CD8+ Tcell response in CMV. CMV pp65 specific T cell predominantly produces cytokines like IFN-γ, IL-2, and TNF-α. HCMV pp71 is delivered directly to cells by infecting HCMV virions. At the start of lytic infections, it travels to the nucleus and stimulates viral IE gene expression by displacing the chromatin remodeling protein ATRX from Daxx and by mediating Daxx degradation through a rare ubiquitin-independent, proteasome-dependent process5.

Functions
CMV pp65 has been the prototypic antigen for the demonstration of CMV-specific T-cell immunity, it is likely that other proteins of CMV will be necessary for the development of a vaccine that generates humoral and cellular protection. CMV pp65-specific T-cell responses have been used for the development of other immunotherapeutic approaches to the control of CMV infection.

HCMV protein pp65 is an efficient protein carrier system into human dendritic cells 6. It is also major target for the cellular immune response. HCMV Protein pp71 disrupts major histocompatibility complex class I cell surface expression. HCMV tegument protein pp71 (ppUL82) enhances the infectivity of viral DNA and accelerates the infectious cycle. Human CMV pp65 virion protein inhibits antiviral gene expression in infected cells. HCMV pp65 mediates accumulation of HLA-DR in lysosomes and destruction of the HLA-DR α-chain 7.

References

1.     Nowak B, Gmeiner A, Sarnow P, Levine AJ, Fleckenstein B (1984). Physical mapping of human cytomegalovirus genes: identification of DNA sequences coding for a virion phosphoprotein of 71 kDa and a viral 65-kDa polypeptide. Virology, 134(1):91-102.

2.     Rüger B, Klages S, Walla B, Albrecht J, Fleckenstein B, Tomlinson P, Barrell B (1987). Primary structure and transcription of the genes coding for the two virion phosphoproteins pp65 and pp71 of human cytomegalovirus. J Virol., 61(2):446-453.
3.     Schmolke S, Drescher P, Jahn G, Plachter B (1995). Nuclear targeting of the tegument protein pp65 (UL83) of human cytomegalovirus: an unusual bipartite nuclear localization signal functions with other portions of the protein to mediate its efficient nuclear transport. J Virol., 69(2):1071-1078.
4.     Zaia JA, Li X, Franck AE, Wu X, Thao L, Gallez-Hawkins G (2009). Biologic and immunologic effects of knockout of human cytomegalovirus pp65 nuclear localization signal. Clin Vaccine Immunol., 16(6):935-943.
5.     Hwang J, Kalejta RF (2009). Human cytomegalovirus protein pp71 induces Daxx SUMOylation. J Virol., 83(13):6591-6598.
6.     Scheller N, Furtwängler R, Sester U, Maier R, Breinig T, Meyerhans A (2008). Human cytomegalovirus protein pp65: an efficient protein carrier system into human dendritic cells. Gene Ther.,15(4):318-325.
7.     Browne EP, Shenk T (2003). Human cytomegalovirus UL83-coded pp65 virion protein inhibits antiviral gene expression in infected cells. PNAS., 100(20):11439-11444.