Skip to main content

Main menu

  • Home
  • Articles
    • Current Issue
    • Next in The JI
    • Archive
    • Brief Reviews
    • Pillars of Immunology
    • Translating Immunology
    • Most Read
    • Top Downloads
    • Annual Meeting Abstracts
  • Info
    • About the Journal
    • For Authors
    • Journal Policies
    • Influence Statement
    • Rights and Permissions
    • For Advertisers
  • Editors
  • Submit
    • Submit a Manuscript
    • Instructions for Authors
    • Journal Policies
  • Subscribe
    • Journal Subscriptions
    • Email Alerts
    • RSS Feeds
    • ImmunoCasts
  • More
    • Most Read
    • Most Cited
    • ImmunoCasts
    • AAI Disclaimer
    • Feedback
    • Help
    • Accessibility Statement
  • Other Publications
    • American Association of Immunologists
    • ImmunoHorizons

User menu

  • Subscribe
  • Log in

Search

  • Advanced search
The Journal of Immunology
  • Other Publications
    • American Association of Immunologists
    • ImmunoHorizons
  • Subscribe
  • Log in
The Journal of Immunology

Advanced Search

  • Home
  • Articles
    • Current Issue
    • Next in The JI
    • Archive
    • Brief Reviews
    • Pillars of Immunology
    • Translating Immunology
    • Most Read
    • Top Downloads
    • Annual Meeting Abstracts
  • Info
    • About the Journal
    • For Authors
    • Journal Policies
    • Influence Statement
    • Rights and Permissions
    • For Advertisers
  • Editors
  • Submit
    • Submit a Manuscript
    • Instructions for Authors
    • Journal Policies
  • Subscribe
    • Journal Subscriptions
    • Email Alerts
    • RSS Feeds
    • ImmunoCasts
  • More
    • Most Read
    • Most Cited
    • ImmunoCasts
    • AAI Disclaimer
    • Feedback
    • Help
    • Accessibility Statement
  • Follow The Journal of Immunology on Twitter
  • Follow The Journal of Immunology on RSS

Prominent roles of secondary anchor residues in peptide binding to HLA-A24 human class I molecules.

A Kondo, J Sidney, S Southwood, M F del Guercio, E Appella, H Sakamoto, E Celis, H M Grey, R W Chesnut, R T Kubo and A Sette
J Immunol November 1, 1995, 155 (9) 4307-4312;
A Kondo
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
J Sidney
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
S Southwood
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
M F del Guercio
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
E Appella
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
H Sakamoto
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
E Celis
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
H M Grey
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
R W Chesnut
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
R T Kubo
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
A Sette
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Info & Metrics
  • PDF
Loading

Abstract

The binding capacity of large sets of peptides corresponding to naturally occurring sequences and carrying previously defined A24-specific motifs was analyzed. It was found that only a minority (9-25%) of the motif-carrying peptides bound the relevant HLA-A molecule with good affinity (IC 50% < or = 50 nM), while the majority of them bound only weakly or not at all (IC 50% > or = 500 nM). By correlating the presence of specific residue types at each position along the peptide sequence with average binding affinity, the prominent influence of specific secondary interactions (secondary anchor residues) was revealed. Moreover, secondary interactions appeared to be size-dependent in that the specific effects detected differed in 9-mer and 10-mer peptide sets. Based on these observations, A24-specific refined motifs were also established for both 9-mer and 10-mer ligands, and their merit was verified by testing the binding capacity of independent sets of synthetic peptides. Such refined motifs should facilitate accurate prediction of potential A24-restricted peptide epitopes. It was also noted that certain crucial secondary interactions appear to be remarkably similar in the case of A24 and other HLA-A molecules previously analyzed (A*0201, A3, A11, and others). This may reflect contributions to binding affinity of relatively invariant residues located within the polymorphic pockets of the HLA binding groove.

  • Copyright © 1995 by American Association of Immunologists

Pay Per Article - You may access this article (from the computer you are currently using) for 1 day for US$37.50

Regain Access - You can regain access to a recent Pay per Article purchase if your access period has not yet expired.

Log in using your username and password

Forgot your user name or password?
PreviousNext
Back to top

In this issue

The Journal of Immunology
Vol. 155, Issue 9
1 Nov 1995
  • Table of Contents
  • Table of Contents (PDF)
Download PDF
Article Alerts
Sign In to Email Alerts with your Email Address
Email Article

Thank you for your interest in spreading the word about The Journal of Immunology.

NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.

Enter multiple addresses on separate lines or separate them with commas.
Prominent roles of secondary anchor residues in peptide binding to HLA-A24 human class I molecules.
(Your Name) has forwarded a page to you from The Journal of Immunology
(Your Name) thought you would like to see this page from the The Journal of Immunology web site.
Citation Tools
Prominent roles of secondary anchor residues in peptide binding to HLA-A24 human class I molecules.
A Kondo, J Sidney, S Southwood, M F del Guercio, E Appella, H Sakamoto, E Celis, H M Grey, R W Chesnut, R T Kubo, A Sette
The Journal of Immunology November 1, 1995, 155 (9) 4307-4312;

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Share
Prominent roles of secondary anchor residues in peptide binding to HLA-A24 human class I molecules.
A Kondo, J Sidney, S Southwood, M F del Guercio, E Appella, H Sakamoto, E Celis, H M Grey, R W Chesnut, R T Kubo, A Sette
The Journal of Immunology November 1, 1995, 155 (9) 4307-4312;
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like

Jump to section

  • Article
  • Info & Metrics
  • PDF

Related Articles

Cited By...

Similar Articles

Navigate

  • Home
  • Current Issue
  • Next in The JI
  • Archive
  • Brief Reviews
  • Pillars of Immunology
  • Translating Immunology

For Authors

  • Submit a Manuscript
  • Instructions for Authors
  • About the Journal
  • Journal Policies
  • Editors

General Information

  • Advertisers
  • Subscribers
  • Rights and Permissions
  • Accessibility Statement
  • Public Access
  • Privacy Policy
  • Disclaimer

Journal Services

  • Email Alerts
  • RSS Feeds
  • ImmunoCasts
  • Twitter

Copyright © 2019 by The American Association of Immunologists, Inc.

Print ISSN 0022-1767        Online ISSN 1550-6606