C-terminal epitope tagging facilitates comparative ligand mapping from MHC class I positive cells

Hickman, Heather D.; Batson, Casey L; Prilliman, Kiley R.; Crawford, D. L.; Jackson, K. L.; Hildebrand, William H.

doi:10.1016/s0198-8859(00)00216-0

Cited by 21 publications

(23 citation statements)

References 25 publications

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“…Soluble HLA-B*0702 transfectants were produced as described (6) using Sup-T1 cells (7). Transfectants were cultured in a Unisyn CP2500 bioreactor unit (Biovest International, Minneapolis, MN) for 2 mo with continuous peptide collection.…”

Section: Soluble Hla Productionmentioning

confidence: 99%

“…Fractionated peptides were mapped by mass spectrometry as described (7). Peptides were nanoelectrosprayed (Protana, Odense, Denmark) into a Q-Star QTOF mass spectrometer (PerSeptive Sciex, Foster City, CA).…”

Section: Mass Spectrometric Analysismentioning

confidence: 99%

“…We previously described a bioreactor-HLA-protein production method and a mass-spectrometric-ion-mapping system for comparatively screening class I-eluted peptide ligands (6,7). In this study, we extend this approach to test the hypothesis that HIV infection alters the presentation of host-encoded peptides.…”

mentioning

confidence: 99%

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Cutting Edge: Class I Presentation of Host Peptides Following HIV Infection

Hickman

Luis

Bardet

et al. 2003

The Journal of Immunology

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Class I MHC molecules bind intracellular peptides for presentation to cytotoxic T lymphocytes. Identification of peptides presented by class I molecules during infection is therefore a priority for detecting and targeting intracellular pathogens. To understand which host-encoded peptides distinguish HIV-infected cells, we have developed a mass spectrometric approach to characterize HLA-B*0702 peptides unique to or up-regulated on infected T cells. In this study, we identify 15 host proteins that are differentially presented on infected human T cells. Peptides with increased expression on HIV-infected cells were derived from multiple categories of cellular proteins including RNA binding proteins and cell cycle regulatory proteins. Therefore, comprehensive analysis of the B*0702 peptide repertoire demonstrates that marked differences in host protein presentation occur after HIV infection.

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Section: Soluble Hla Productionmentioning

confidence: 99%

Section: Mass Spectrometric Analysismentioning

confidence: 99%

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Cutting Edge: Class I Presentation of Host Peptides Following HIV Infection

Hickman

Luis

Bardet

et al. 2003

The Journal of Immunology

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“…Peptides in the naïve and infected RP-HPLC fractions were mapped by MS with each fraction sprayed 3 times via nanospray into a Qstar Elite quadrupole time-of-flight mass spectrometer to create reproducible MS ion maps for the peptides in each HPLC fraction. To detect peptides unique to infected fractions, corresponding uninfected/infected MS ion maps were aligned at 20-amu increments and visually assessed for the presence of ions unique to infected MS spectra (39). Peptides exhibiting a Ն1.5-fold increase during infection were identified by summing the intensity values for each ion in the three uninfected/infected MS ion maps and calculating the normalized fold increase of each infected ion over uninfected.…”

mentioning

confidence: 99%

HLA class I molecules consistently present internal influenza epitopes

Wahl¹,

Schafer²,

Bardet³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…Initial studies using sHLA showed a tight correlation between sHLA and mHLA peptide repertoires (19); however, these sHLA were isolated from cultured cells and not plasma. Extending these findings, BassaniSternberg et al (4) compare peptides eluted from sHLA shed from multiple myeloma cells in vitro with those recovered from mHLA from the same cells, finding 40% of the sHLA peptides in the mHLA repertoire.…”

mentioning

confidence: 99%