Evidence map›Paper›PMID 12810958›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Differential proteasomal processing of hydrophobic and hydrophilic protein regions: contribution to cytotoxic T lymphocyte epitope clustering in HIV-1-Nef.

Maria Lucchiari-Hartz, Viv Lindo, Niclas Hitziger, Simone Gaedicke, Loredana Saveanu, Peter M van Endert, Fiona Greer, Klaus Eichmann, Gabriele Niedermann

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

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0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

9 authors.

Maria Lucchiari-HartzDepartment of Cellular Immunology, Max Planck Institute of Immunobiology, Stübeweg 51, D-79108 Freiburg, Germany.
Viv Lindo
Niclas Hitziger
Simone Gaedicke
Loredana Saveanu
Peter M van Endert
Fiona Greer
Klaus Eichmann
Gabriele Niedermann

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HIV proteins contain a multitude of naturally processed cytotoxic T lymphocyte (CTL) epitopes that concentrate in clusters. The molecular basis of epitope clustering is of interest for understanding HIV immunogenicity and for vaccine design. We show that the CTL epitope clusters of HIV proteins predominantly coincide with hydrophobic regions, whereas the noncluster regions are predominantly hydrophilic. Analysis of the proteasomal degradation products of full-length HIV-Nef revealed a differential sensitivity of cluster and noncluster regions to proteasomal processing. Compared with the epitope-scarce noncluster regions, cluster regions are digested by proteasomes more intensively and with greater preference for hydrophobic P1 residues, resulting in substantially greater numbers of fragments with the sizes and COOH termini typical of epitopes and their precursors. Indeed, many of these fragments correspond to endogenously processed Nef epitopes and/or their potential precursors. The results suggest that differential proteasomal processing contributes importantly to the clustering of CTL epitopes in hydrophobic regions.

Indexed as

Amino AcidsAmino Acid SequenceCell LineCysteine EndopeptidasesEpitopesGene Products, nefHIV-1HumansJurkat CellsMolecular Sequence DataMultienzyme Complexesnef Gene Products, Human Immunodeficiency VirusPeptidesProteasome Endopeptidase ComplexProteinsProtein Structure, TertiaryAmino AcidsCysteine EndopeptidasesEpitopesGene Products, nefMultienzyme Complexesnef Gene Products, Human Immunodeficiency VirusPeptidesProteasome Endopeptidase ComplexProteinsRecombinant Proteins

Identifiers

PMID12810958
PMCPMC164660

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.