Analysis of the structure of naturally processed peptides bound by Class I and Class II major histocompatibility complex molecules

Appella, Ettore; Ea, Padlan; Df, Hunt

doi:10.1007/978-3-0348-9061-8_6

Cited by 18 publications

(16 citation statements)

References 41 publications

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“…Additionally, we were unable to identify HEV-specific CD8 + T cells, probably due to the usage of 16-mer peptides and HEV protein in the propagation of the HEV-specific T cell line. Long peptides (>15 mer), and protein antigens preferentially stimulate CD4 + T cells (Appella et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Characterization of hepatitis E-specific cell-mediated immune response using IFN-γ ELISPOT assay

Shata

Barrett

Shire

et al. 2007

Journal of Immunological Methods

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In developing countries, hepatitis E (HEV) and hepatitis A (HAV) are the major causes of acute viral hepatitis with similar fecooral modes of transmission. In contrast to the high seroprevalence of hepatitis A infection, a low seroprevalence of HEV among children in endemic areas has been reported. These data suggest the possibility that silent HEV infection is undiagnosed by the current available methods. Many of the serological tests used for HEV diagnosis have poor specificity and are unable to differentiate among different genotypes of HEV. Moreover, the RT-PCR used for HEV isolation is only valid for a brief period during the acute stage of infection. Cell-mediated immune (CMI) responses are highly sensitive, and long lasting after sub-clinical infections as shown in HCV and HIV. Our objective was to develop a quantitative assay for cell-mediated immune (CMI) responses in HEV infection as a surrogate marker for HEV exposure in silent infection. Quantitative assessment of the CMI responses in HEV will also help us to evaluate the role of CMI in HEV morbidity. In this study, an HEV-specific interferon-gamma (IFN-γ) ELISPOT assay was optimized to analyze HEV-specific CMI responses. We used peripheral blood mononuclear cells (PBMC) and sera from experimentally infected chimpanzees and from seroconverted and control human subjects to validate the assay. The HEV-specific IFN-γ ELISPOT responses correlated strongly and significantly with anti-HEV ELISA positive/negative results (rho=0.73, p=0.02). Moreover, fine specificities of HEV-specific T cell responses could be identified using overlapping HEV ORF2 peptides.

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Section: Discussionmentioning

confidence: 99%

Characterization of hepatitis E-specific cell-mediated immune response using IFN-γ ELISPOT assay

Shata

Barrett

Shire

et al. 2007

Journal of Immunological Methods

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“…As the median length of an active site is 11 amino-acid residues (Khazanov and Carlson, 2013), designed ligands should also be longer. While historically six-residue positional scanning could identify ligands of receptors or epitopes of monoclonal antibodies (Dooley and Houghten, 1993), in our experience receptor agonists are 9–12 residue long (Otvos et al, 2008, 2011a) much like major histocompatibility complex binding peptides (Appella et al, 1995). Antagonists acting on the same receptor binding sites are somewhat shorter ( vide infra ).…”

mentioning

confidence: 91%

Current challenges in peptide-based drug discovery

2014

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“…The instrument control software can then select individual ions for a tandem mass spectrometry experiment (MS/MS) whereby the ions are fragmented to yield daughter ions that are then measured and displayed in the resulting MS/MS spectrum. Because of the high capacity of reverse-phase columns and the analytical power of electrospray ionization (ESI)-MS, the analysis of very complex mixtures of peptides is achievable by LC-MS, and was first demonstrated for peptides displayed by the MHC (Appella et al , 1995;Hunt et al , 1992a;Hunt et al , 1992b;Henderson et al, 1992). The utility of these LC-MS based approaches has been increased through the implementation of additional dimensions of chromatography prior to the final reverse-phase LC-MS (see section 3).…”

Section: Proteomics Backgroundmentioning

confidence: 98%

How Much of the Proteome Do We See with Discovery-Based Proteomics Methods and How Much Do We Need to See?

Patterson¹

2004

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Despite the recent advances in parallel protein-based analyses the proportion of the protein composition of any specific tissue or organism that is currently being analyzed is still unknown. The ultimate aim of proteomics is to characterize all of the proteins in a biological system under study, but much has been gained from knowledge of smaller subsets of the proteome. Therefore, while techniques and instrumentation are being improved to increase the sensitivity of analysis, it is just as important to answer the question of what depth of analysis is required for reasonable conclusions to be reached. The questions to be answered and the resulting depth of analysis required will vary depending upon whether the understanding is required for diagnostic markers, therapeutic targets or biological systems. The issues associated with increasing the depth of analysis of proteins in the context of these areas will be discussed. However, it should be noted that merely increasing the amount of data acquired will not necessarily increase the amount of knowledge of a particular system and as such careful implementation of proteomic methods is required to advance these fields of research.

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Analysis of the structure of naturally processed peptides bound by Class I and Class II major histocompatibility complex molecules

Cited by 18 publications

References 41 publications

Characterization of hepatitis E-specific cell-mediated immune response using IFN-γ ELISPOT assay

Characterization of hepatitis E-specific cell-mediated immune response using IFN-γ ELISPOT assay

Current challenges in peptide-based drug discovery

How Much of the Proteome Do We See with Discovery-Based Proteomics Methods and How Much Do We Need to See?

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