Analysis of antigen processing and presentation

 
Principal Investigator :  Satyajit Rath

Project Associates / Assistants
Deepa Rajagopal
Madhuchhanda Mohanty

Ph D Students
Anita Garg
Ebenezer Chitra
Smita Srivastava
Ashutosh Chaudhry
Varanasi Vineeth

Collaborators
Vineeta Bal
Anna George
Dinakar M Salunke
Jeannine M Durdik, Univ Arkansas, USA
Shahid Jameel, ICGEB, New Delhi
Kanury V Rao, ICGEB, New Delhi
Satyajit Mayor, NCBS, Bangalore
Apurva Sarin, NCBS, Bangalore
B Ravindran, RMRC, Bhubaneswar
A Rudensky, Univ Washington, USA
Ranjan Sen, Brandeis Univ, USA
Tushar Vaidya, CCMB, Hyderabad

The aim of the ongoing linked projects in this group is to examine the generation and activation of T and B cells through a variety of linked experimental approaches. A variety of experimental approaches are taken to address the theme issues. The approaches in current use examine APCs and pathways involved in antigen presentation to MHC class I and class II-restricted T cells; and analyse the consequences of intracellular signal transduction modulation for both development and responses of B cells, T cells and macrophages using both genetic and pharmacological tools.

Role of Bruton’s tyrosine kinase (Btk) in myeloid cell development and function

We have shown previously that macrophages from X-linked immunodeficient (xid) mice lacking functional Bruton’s tyrosine kinase (Btk) show poor induction of macrophage effector functions such as NO induction, bactericidal activity and secretion of proinflammatory cytokines (TNF-alpha, IL-1beta), but show unchanged T cell priming functions such as induction of costimulatory molecule expression (CD80, CD86) and enhanced induction of the T cell-directed cytokine IL-12. Induction of some transcriptional regulators of the NF-kappaB family, crucial for the expression of proinflammatory cytokines, is also poor in Btk-deficient macrophages. Thus, Btk appears to be involved in signaling for inducible effector functions, but not APC functions, in macrophages.

Btk is expressed in all cells of myeloid lineage, and in B cells, but not in T cells. Therefore, we have examined the development and function of another major cell of the myeloid lineage, the polymorphonuclear neutrophil granulocyte (PMN), in Btk-deficient mice. We find that PMNs from xid mice show deeply compromised functions. The induction of reactive oxygen species is poor, as is the induction of NO. On the other hand the induction of costimulatory molecule expression such as CD80 and CD86 is unchanged, analogous to the findings on macrophages in these mice. Phagocytosis is relatively little affected in these cells, as it is in macrophages. Even more interesting is the finding that the numbers of PMNs in peripheral blood are reduced by 2-3-fold in xid mice, and the PMNs observed are predominantly small regular cells rather than the large irregular PMNs seen in wild-type mice. In keeping with these findings, the maturation of PMNs in the bone marrow appears to be hampered in xid mice, since irregular cells with high levels of the granulocytic marker molecule Gr-1 are seen at lesser frequencies in them. Btk is thus likely to be involved in granulocyte development as well as function.

Role of cAMP-mediated and reactive species (RS)-mediated pathways in controlling death pathways relevant to T cell memory

We have shown previously that pentoxifylline (PF), a phosphodiesterase (PDE) inhibitor in common clinical use, enhances long-term persistence of T cell responses, including protective responses to a bacterial immunogen, Salmonella typhimurium (Stm), via a cAMP-dependent protein kinase A (PKA)-mediated effect on T cells if given to mice for a brief period during immunization, by inhibiting post-activation T cell apoptosis. The pathways involved in the death pathway which are affected by PF are thus of major importance. Data from our group have shown that this death pathway is not mediated by death receptors, but are mitochondrial, and are likely to be mediated by reactive species (RS), - both oxygen intermediates and nitric oxide (NO). To examine if the prevention of T cell death by PF operates via RS-mediated death, we have now tested mice deficient in inducible nitric oxide synthase (iNOS). While the secondary T cell responses generated in vitro by alloimmunisation are markedly enhanced by PF for wild-type mouse T cells, PF has no effect on such a memory response of iNOS-null T cells. These data indicated that PF probably affects NO-mediated induction of post-activation T cell death. In keeping with this, it would be expected that iNOS-null mice mount better memory T cell responses than wild-type mice do, and our data with antigen-specific immunization in vivo now demonstrate that, as late as six weeks after immunization, about three-fold greater numbers of memory T cells, both CD4 and CD8, can be identified in iNOS-null than in wild-type mice.

Unnatural peptide mimics as T cell immunogens

The retro-D-peptidic epitopes we have used for MHC class I binding and CD8 T cell stimulation (designed by the structural biology group) have now been examined in immunogenicity studies in vivo in terms of the bulk T cell repertoire crossreactivity in immunised mice as well as the quantitative immunogenicity. When mice are immunised with the native L-Oap [SIINFEKL; H-2-K-b-restricted], CD8 T cell responses can be recalled efficiently in vitro with L-Oap itself, as well as with retro-D-Oap, indicating that there is substantial crossreactivity between Oap and its retro-D mimic even at the level of an oligoclonal T cell repertoire triggered in vivo. However, contrary to expectations, retro-D-Oap by itself does not appear to be a good immunogen in preliminary experiments, since CD8 T cells from mice immunised with retro-D-Oap do not yield efficient recall responses in vitro even with retro-D-Oap itself. The basis for the poor immunogenicity is therefore of great potential interest.

Antigen presentation pathway analyses

We have shown previously that proteins introduced into or synthesized in the cytosol of antigen-presenting cells (APCs) such as macrophages can be processed by proteasomal pathways and presented on MHC class II (MHCII) by these cells. We have also shown a role for non-proteasomal proteolytic cytosolic molecules such as tripeptidyl peptidases in this process. The pathway by which peptides generated in the cytosol reach vesicular compartments for loading onto MHCII has been thus an issue of interest. In this connection, we have now observed that, while APCs from mice deficient in the cytosol-to-ER transporter complex TAP do present cytosolically introduced proteins well on MHCII, this presentation is not dependent on proteasomal function, since pharmacological inhibition of proteasomes does not inhibit this presentation to the degree observed in APCs from wild-type mice. This finding suggests that there may be alternate pathways of protein processing and peptide transport from the cytosol to vesicular compartments accessible for MHCII loading, - one requiring proteasomes and TAP while the other may be independent of these. We have also found that geldanamycin, an inhibitor of HSP90, can substantially inhibit presentation of both exogenous and cytosolic proteins on MHCII, implicating the HSP90 chaperone molecule in MHCII-mediated antigen presentation.

Publications

Original peer-reviewed articles

1.     John B, Rajagopal D, Pashine A, Rath S, George A and Bal V (2002) Role of IL-12-independent and IL-12-dependent pathways in regulating generation of the IFN-g component of T cell responses to Salmonella typhimurium. J Immunol 169:2545-2552.

2.     Suresh R, Vig M, Bhatia S, Goodspeed EPB, John B, Kandpal U, Srivastava S, George A, Sen R, Bal V, Durdik JM and Rath S (2002) Pentoxifylline functions as an adjuvant in vivo to enhance T cell immune responses by inhibiting activation-induced death. J Immunol 169:4262-4272.

3.     Vig M, George A, Sen R, Durdik J, Rath S and Bal V (2002) Commitment of activated T cells to secondary responsiveness is enhanced by signals mediated by cAMP-dependent protein kinase A-I. Mol Pharmacol 62:1471-1481.

4.     Nair DT, Kaur KJ, Singh K, Mukherjee P, Rajagopal D, George A, Bal V, Rath S, Rao KV, Salunke DM (2003) Mimicry of native peptide antigens by the corresponding retro-inverso analogs is dependent on their intrinsic structure and interaction propensities. J Immunol 170:1362-1373.