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Identification of eight determinants in the hemagglutinin molecule of influenza virus A/PR/8/34 (H1N1) which are recognized by class II-restricted T cells from BALB/c mice.

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TLDR
Eight nonoverlapping regions of the hemagglutinin (HA) molecule of influenza virus A/PR/8/34 (PR8), which serve as recognition sites for class II-restricted T cells (TH) from BALB/c mice, have been identified in the form of 10- to 15-amino-acid-long synthetic peptides.
Abstract
Eight nonoverlapping regions of the hemagglutinin (HA) molecule of influenza virus A/PR/8/34 (PR8), which serve as recognition sites for class II-restricted T cells (TH) from BALB/c mice, have been identified in the form of 10- to 15-amino-acid-long synthetic peptides. These TH determinants are located between residues 110 to 313 of the HA1 polypeptide. From a total of 36 HA-specific TH clones and limiting-dilution cultures of independent clonal origins, 33 (90%) responded to stimulation with one of these peptides. The residual three TH clones appeared to recognize a single additional determinant on the HA1 polypeptide which could not be isolated, however, in the form of a stimulatory peptide. None of the motifs that have been proposed to typify TH determinants were displayed by more than half of these recognition sites. Most unexpected was the finding that none of the TH determinants was located in the ectodomain of the HA2 polypeptide that makes up roughly one-third of the HA molecule. Possible reasons for the preferential recognition of HA1 as opposed to HA2 by TH are discussed.

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Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues.

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The Kinetic Stability of MHC Class II:Peptide Complexes Is a Key Parameter that Dictates Immunodominance

TL;DR: It is found that immunodominant peptides possess extremely long half-lives with class II molecules (t(1/2) > 150 hr), whereas cryptic peptides displayed half- Lives of less than 10 hr.
References
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Journal ArticleDOI

Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.

TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
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Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation

TL;DR: Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified and at least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.
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Antigen-specific interaction between T and B cells

TL;DR: In this article, the authors have cloned and immortalized human antigen-specific B cells with Epstein-Barr virus (EBV) and analyzed their interaction with T-cell clones specific for the same antigen.
Journal ArticleDOI

Binding of immunogenic peptides to Ia histocompatibility molecules

TL;DR: A physical association of this peptide responsible for T-cell recognition of HEL is sought with purified, detergent-solubilized I–Ak molecules from B-hybridoma cells, which may explain the role of the Ia glycoproteins in cellular interactions.
Journal ArticleDOI

Antigen-Presenting Function of the Macrophage

TL;DR: The available information leads one to conclude that APC deficient in their capacity to internalize and process proteins will not be able to present them, and the macrophage is the candidate as the major APC involved in the recruitment and enlargement of clones T cells.
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