S. MUNIR ALAM
Assistant Research Professor, Human Vaccine Institute, Department of Medicine

Contact Information
301 Sands Building
Duke University Medical Center
(PH) 919-684-6995
(FX) 919-684-5230
alam0004@mc.duke.edu

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Education

	PhD	Studies on human metastatic breast carcinoma, Immunology, University of Glasgow, Glasgow, United Kingdom, 1992
	MSc	A succinate dehydrogenase inhibitor from V. cholerae, Biochemistry, University of Dhaka, Dhaka, Bangladesh, 1986
	BSc	Biochemistry, University of Dhaka, Bangladesh, 1983

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Experience

	2000-present	Assistant Research Professor, Department of Medicine, Duke University
	1999-2000	Assistant Professor, Department of Immunology, The Scripps Research Institute
	1996-1998	Sr. Research Associate, Department of Immunology, The Scripps Research Institute
	1992-1996	Postdoctoral Fellow in the Dept. of Immunology, The Scripps Research Institute
	1988-1992	Commonwealth Scholar, Department of Biochemistry, University of Glasgow
	1987-1988	Lecturer, Department of Biochemistry, University of Dhaka, Bangladesh

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Selected Publications

1. Alam, S.M., Travers, P.J., Wung, J.L., Jameson, S.C., Carbone, F.R., & Gascoigne, N.R.J. T cell receptor affinity and thymocyte positive selection. 1996, Nature, 381:616-620.
2. Alam, S.M. & N.R.J. Gascoigne. Post-translational regulation of TCR V? allelic exclusion during T cell differentiation. 1998, J. Immunol., 160:3883-3890.
3. Alam, S.M., M. Davies, W. Nasholds, S.C. Jameson, K. Hogquist, N.R.J. Gascoigne & P.J. Travers Qualitative and quantitative differences in T-cell receptor binding kinetics for agonist and antagonist ligands. 1999, Immunity, 10(2):227-37.
4. Gascoigne, N.R.J. & Alam, S.M. Allelic exclusion of the T cell receptor ? chain: developmental regulation of a post-translational event. Semin. Immunol. 1999, 11(5):337-347.
5. Redpath, S., Alam, S.M., Lin, C. & Gascoigne, N.R.J. Cutting edge: Trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC:peptide ligands. J. Immunol. 1999, 163(1): 6-10.
6. Gascoigne, N.R.J., Alam, S.M., Lin, C.M., McGuire, M.V., Marine, S., Neiderberger, N., Redpath, S., Sim, B-C, Travers, P., Yachi, P., Zal, A. & Zal, T. T cell receptor binding kinetics and the special role of Valpha in T cell development and activation. Immunologic Res. 2000;21(2-3):225-31.
7. Rosette, C., Werlen, G., Daniels, M.A., Holman, P.O., Alam, S.M., Travers, P.J., Gascoigne, N.R., Palmer, E., Jameson, S.C. The impact of duration versus extent of TCR occupancy on T cell activation: a revision of the kinetic proofreading model. Immunity, 2001, 15(1):59-70.
8. Fong, A.M., Alam , S.M., Imai, T., Haribabu, B. & Patel, D. CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. 2002. J. Biol. Chem., 277(22):19418-23..
9. Richard, E., Alam, S.M., Arredondo-Vega, F.X., Patel, D.D. & Hershfield, M.S. Clustered charged amino acids of human adenosine deaminase comprise a functional epitope for binding the adenosine deaminase complexing protein CD26/dipeptidyl peptidase IV. 2002. J. Biol. Chem. 277:19270-26.
10. Alam, S.M. & Gascoigne, N.R.J. Binding Kinetics of Superantigen with TCR and MHC Class II. In “Methods in Molecular Biology: Superantigen Protocols.” 2002, Krakauer, T. Ed. Humana Press, New Jersey.

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Short Research Interest Descriptor

Biophysical analysis of coreceptor modulation of TCR-MHC interactions and energetics and kinetics of monoclonal antibody binding to soluble HIV Envelope proteins

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Research Interest

One of our research interests is to study the molecular mechanisms of T cell recognition. This involves the use of a biosensor based assay to study the interactions of membrane bound T cell receptor (TCR-CD3 complex) with its ligand, the peptide-MHC complex (pMHC). Using surface plasmon resonance and isothermal titration calorimetry measurements, we are studying the influence of co-stimulatory molecules on the kinetics and thermodynamics of TCR-pMHC binding. The ultimate goal is to use integrated molecular and biophysical approaches to study membrane TCR-MHC interactions and to understand how these interactions are modulated by co-receptors during T cell development and activation.
We are also interested in the biophysical characterization of soluble, recombinant Envelope proteins (gp120 and gp140) from human HIV viruses. We have employed surface plasmon resonance, analytical sedimentation equilibrium analysis and isothermal titration calorimetry to characterize and study the energetics and kinetics of the binding of anti-gp120 and anti-gp41 antibodies to several recombinant Envelope proteins. These studies have relevance in immunogen design for generating anti-HIV vaccines.

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