Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo

Eric F. Tewalt, Jason C. Maynard, Julie Jo Walters, Amanda M. Schell, Brent L. Berwin, Christopher V. Nicchitta, Christopher Norbury

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

CD8+ T cells (TCD8+) differentiate into effector cells following recognition of specific peptide-major histocompatibility complex (MHC) class I complexes (pMHC-I) on the surface of professional APCs (pAPCs), such as dendritic cells. Antigenic pMHC-I can be generated from two spatially distinct sources. The direct presentation pathway involves generation of peptide from protein substrate synthesized within the cell that is presenting the pMHC-I. Alternatively, the cross presentation pathway involves presentation of antigen that is not synthesized within the presenting cell, but is derived from exogenous proteins synthesized within other donor cells. The mechanisms by which cross presentation of exogenous antigens occur in vivo remain controversial. The C-type lectin scavenger receptor A (SR-A) has been implicated in a number of potential cross presentation pathways, including the presentation of peptide bound to heat shock proteins, such as glycoprotein 96 (gp96), and the transfer of pMHC-I from a donor cell to the pAPC. We demonstrate here that initiation of TCD8+ responses is normal in mice lacking SR-A, and that the redundancy of ligand binding exhibited by the SR family is likely to be an important mechanism that ensures cross presentation in vivo. These observations emphasize the requirement to target multiple receptors and antigen-processing pathways during the rational design of vaccines aimed at eliciting protective TCD8+.

Original languageEnglish (US)
Pages (from-to)480-491
Number of pages12
JournalImmunology
Volume125
Issue number4
DOIs
StatePublished - Dec 1 2008

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Cross-Priming
Scavenger Receptors
Glycoproteins
Antigen Presentation
Peptides
C-Type Lectins
Heat-Shock Proteins
Major Histocompatibility Complex
Dendritic Cells
Proteins
Vaccines
Ligands
T-Lymphocytes
Antigens

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology

Cite this

Tewalt, E. F., Maynard, J. C., Walters, J. J., Schell, A. M., Berwin, B. L., Nicchitta, C. V., & Norbury, C. (2008). Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo. Immunology, 125(4), 480-491. https://doi.org/10.1111/j.1365-2567.2008.02861.x
Tewalt, Eric F. ; Maynard, Jason C. ; Walters, Julie Jo ; Schell, Amanda M. ; Berwin, Brent L. ; Nicchitta, Christopher V. ; Norbury, Christopher. / Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo. In: Immunology. 2008 ; Vol. 125, No. 4. pp. 480-491.
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Tewalt, EF, Maynard, JC, Walters, JJ, Schell, AM, Berwin, BL, Nicchitta, CV & Norbury, C 2008, 'Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo', Immunology, vol. 125, no. 4, pp. 480-491. https://doi.org/10.1111/j.1365-2567.2008.02861.x

Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo. / Tewalt, Eric F.; Maynard, Jason C.; Walters, Julie Jo; Schell, Amanda M.; Berwin, Brent L.; Nicchitta, Christopher V.; Norbury, Christopher.

In: Immunology, Vol. 125, No. 4, 01.12.2008, p. 480-491.

Research output: Contribution to journalArticle

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AU - Maynard, Jason C.

AU - Walters, Julie Jo

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AU - Norbury, Christopher

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