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

S. Lu; V. E. Reyes; C. M. Bositis; T. G. Goldschmidt; V. Lam; R. R. Torgerson; T. Ciardelli; L. Hardy; R. A. Lew; R. E. Humphreys

doi:10.1016/0264-410X(92)90410-L

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

S. Lu
, V. E. Reyes
, C. M. Bositis
, T. G. Goldschmidt
, V. Lam
, R. R. Torgerson
, T. Ciardelli
, L. Hardy
, R. A. Lew
, R. E. Humphreys

Research output: Contribution to journal › Short survey › peer-review

8 Scopus citations

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 α-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 possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.

Original language	English (US)
Pages (from-to)	3-7
Number of pages	5
Journal	Vaccine
Volume	10
Issue number	1
DOIs	https://doi.org/10.1016/0264-410X(92)90410-L
State	Published - 1992
Externally published	Yes

Keywords

Antigen processing
MHC molecules
T cell-presented epitope
peptide vaccines
α-helix

ASJC Scopus subject areas

Molecular Medicine
General Immunology and Microbiology
General Veterinary
Public Health, Environmental and Occupational Health
Infectious Diseases

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10.1016/0264-410X(92)90410-L

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title = "Biophysical mechanism of the scavenger site near T cell-presented epitopes",

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 α-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 possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.",

keywords = "Antigen processing, MHC molecules, T cell-presented epitope, peptide vaccines, α-helix",

author = "S. Lu and Reyes, \{V. E.\} and Bositis, \{C. M.\} and Goldschmidt, \{T. G.\} and V. Lam and Torgerson, \{R. R.\} and T. Ciardelli and L. Hardy and Lew, \{R. A.\} and Humphreys, \{R. E.\}",

note = "Funding Information: This work was supported by NIH grant CA-37645 and ACS grant IM-582 and by a grant from the Scientific Council at the University of Massachusetts Medical Center for instrumentation in the Molecular Graphics Facility. C.M.B., from Dartmouth College, was an undergraduate research fellow of the Scientific Council of U.M.M.C. and subsequently was an Alvin T.-Viola D. Fuller fellow of The American Cancer Society, Massachusetts Division. T.G.G. was a medical student research fellow of the Howard Hughes Medical Institute, V.L. was a fellow of Immunobiology Training Grant AI-07349 and of the Scientific Council of U.M.M.C. V.E.R. was a fellow of immunovirology Training Grant AI-07272. R.R.T., from Williams College, was an undergraduate research fellow of the Juvenile Diabetes Foundation. The authors our grateful to Patricia J. Downe and Erik R. Jones for typing this manuscript.",

year = "1992",

doi = "10.1016/0264-410X(92)90410-L",

language = "English (US)",

volume = "10",

pages = "3--7",

journal = "Vaccine",

issn = "0264-410X",

publisher = "Elsevier Ltd",

number = "1",

}

TY - JOUR

T1 - Biophysical mechanism of the scavenger site near T cell-presented epitopes

AU - Lu, S.

AU - Reyes, V. E.

AU - Bositis, C. M.

AU - Goldschmidt, T. G.

AU - Lam, V.

AU - Torgerson, R. R.

AU - Ciardelli, T.

AU - Hardy, L.

AU - Lew, R. A.

AU - Humphreys, R. E.

N1 - Funding Information: This work was supported by NIH grant CA-37645 and ACS grant IM-582 and by a grant from the Scientific Council at the University of Massachusetts Medical Center for instrumentation in the Molecular Graphics Facility. C.M.B., from Dartmouth College, was an undergraduate research fellow of the Scientific Council of U.M.M.C. and subsequently was an Alvin T.-Viola D. Fuller fellow of The American Cancer Society, Massachusetts Division. T.G.G. was a medical student research fellow of the Howard Hughes Medical Institute, V.L. was a fellow of Immunobiology Training Grant AI-07349 and of the Scientific Council of U.M.M.C. V.E.R. was a fellow of immunovirology Training Grant AI-07272. R.R.T., from Williams College, was an undergraduate research fellow of the Juvenile Diabetes Foundation. The authors our grateful to Patricia J. Downe and Erik R. Jones for typing this manuscript.

PY - 1992

Y1 - 1992

N2 - 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 α-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 possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.

AB - 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 α-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 possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.

KW - Antigen processing

KW - MHC molecules

KW - T cell-presented epitope

KW - peptide vaccines

KW - α-helix

UR - https://www.scopus.com/pages/publications/0026604535

UR - https://www.scopus.com/pages/publications/0026604535#tab=citedBy

U2 - 10.1016/0264-410X(92)90410-L

DO - 10.1016/0264-410X(92)90410-L

M3 - Short survey

C2 - 1371632

AN - SCOPUS:0026604535

SN - 0264-410X

VL - 10

SP - 3

EP - 7

JO - Vaccine

JF - Vaccine

IS - 1

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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