GSBS Student Publications

Title

Biophysical mechanism of the scavenger site near T cell-presented epitopes

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Pharmacology

Date

1-1-1992

Document Type

Article

Medical Subject Headings

Amino Acid Sequence; Animals; Chemistry, Physical; Epitopes; Humans; Major Histocompatibility Complex; Molecular Sequence Data; Protein Conformation; T-Lymphocytes

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

We seek to identify consensus sequences in digested fragments of antigenic proteins regulating selection and major histocompatibility complex (MHC)-restricted presentation to T cells of epitopes within those fragments. One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hydrophobic strip when a sequence is coiled as an alpha-helix, is found in or near most T cell-presented epitopes. Such recurrent hydrophobicity may lead to protease-protected coiling of the fragment against endosomal membranes and transfer to MHC molecules. This concept leads to better identification of T cell-presented sequences and possible to engineering of T cell-presented vaccines to affect their potency and MHC restriction.

Rights and Permissions

Citation: Vaccine. 1992;10(1):3-7.

Related Resources

Link to article in PubMed

Journal Title

Vaccine

PubMed ID

1371632