This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ovsyannikova, I. G.
Right arrow Articles by Poland, G. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ovsyannikova, I. G.
Right arrow Articles by Poland, G. A.

 Previous Article  |  Next Article 

Journal of Virology, January 2004, p. 42-51, Vol. 78, No. 1
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.1.42-51.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of Novel, Naturally Processed Measles Virus Class II HLA-DRB1 Peptides

Inna G. Ovsyannikova,1 Kenneth L. Johnson,2,3 David C. Muddiman,2,3 Robert A. Vierkant,4 and Gregory A. Poland1*

Mayo Vaccine Research Group,1 The W. M. Keck FT-ICR Mass Spectrometry Laboratory, Mayo Proteomics Research Center,2 Department of Biochemistry and Molecular Biology,3 Department of Biostatistics, Mayo Clinic and College of Medicine, Rochester, Minnesota 559054

Received 18 August 2003/ Accepted 24 September 2003

Previously, we identified a naturally processed and presented measles virus (MV) 19-amino-acid peptide, ASDVETAEGGEIHELLRLQ (MV-P), derived from the phosphoprotein and eluted from the human leukocyte antigen (HLA) class II molecule by using mass spectrometry. We report here the identification of a 14-amino-acid peptide, SAGKVSSTLASELG, derived from the MV nucleoprotein (MV-N) bound to HLA-DRB1*0301. Peripheral blood mononuclear cells (PBMC) from 281 previously vaccinated measles-mumps-rubella II (MMR-II) subjects (HLA discordant) were studied for peptide recognition by T cells. Significant gamma interferon (IFN-{gamma}) responses to MV-P and MV-N peptides were observed in 55.9 and 15.3% of subjects, respectively. MV-P- and MV-N-specific interleukin-4 (IL-4) responses were detected in 19.2 and 23.1%, respectively, of PBMC samples. Peptide-specific cytokine responses and HLA-DRB1 allele associations revealed that, for the MV-P peptide, the allele with the strongest association with both IFN-{gamma} (P = 0.02) and IL-4 (P = 0.03) secretion was DRB1*0301. For MV-N, the allele with the strongest association with IFN-{gamma} secretion was DRB1*1501 (P = 0.04), and the alleles with the strongest associations with IL-4 secretion were DRB1*1103 and DRB1*1303 (P = 0.01). These results indicate that HLA class II MV proteins can be processed, presented, and identified, and the ability to generate cell-mediated immune responses can be demonstrated. This information is promising for new vaccine design strategies with peptide-based vaccines.

* Corresponding author. Mailing address: Mayo Vaccine Research Group, Mayo Clinic, Guggenheim 611C, 200 1st St., S.W., Rochester, MN 55905. Phone: (507) 284-4456. Fax: (507) 266-4716. E-mail: poland.gregory{at}mayo.edu.

Journal of Virology, January 2004, p. 42-51, Vol. 78, No. 1
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.1.42-51.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»