S. Munir Alam, PhD

Professor in Medicine
Professor of Pathology
Member of the Duke Human Vaccine Institute
Campus mail 2 Genome Ct, MSRB II - Room 4004, Durham, NC 27710
Phone (919) 668-6372
Email address alam0004@mc.duke.edu

Research Interests.
Biophysical analysis of coreceptor modulation of TCR-MHC interactions. One of our research interests is to study the molecular mechanisms of T cell recognition. We have particular interest in understanding the trimolecular interactions between membrane bound T cell receptor (TCR-CD3 complex) and its ligand, the peptide-MHC complex (pMHC), and co-receptor molecules. We are using different biophysical approaches which include surface plasmon resonance, isothermal titration calorimetry and atomic force spectroscopy to study the influence of co-stimulatory molecules on the kinetics and thermodynamics of TCR-pMHC binding. The 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.
Energetics and kinetics of monoclonal antibody binding to soluble HIV Envelope proteins. An additional interest of our lab involves biophysical characterization of soluble, recombinant human HIV-1 Envelope proteins (gp120 and gp140). We have employed surface plasmon resonance, analytical sedimentation equilibrium analysis, isothermal titration calorimetry and atomic force spectroscopy to characterize the antigenicity and study the energetics, kinetics and single molecule force measurements of the binding of anti-gp120 and anti-gp41 antibodies to several recombinant HIV-1 Envelope proteins. These studies have relevance in immunogen design for generating anti-HIV vaccines.

Education and Training

  • Ph.D., University of Glasgow (Scotland), 1992

Publications

Friedman, James, S Munir Alam, Xiaoying Shen, Shi-Mao Xia, Shelley Stewart, Kara Anasti, Justin Pollara, et al. “Isolation of HIV-1-neutralizing mucosal monoclonal antibodies from human colostrum..” Plos One 7, no. 5 (2012). https://doi.org/10.1371/journal.pone.0037648.

PMID
22624058
Full Text

Tomaras, Georgia D., James M. Binley, Elin S. Gray, Emma T. Crooks, Keiko Osawa, Penny L. Moore, Nancy Tumba, et al. “Polyclonal B cell responses to conserved neutralization epitopes in a subset of HIV-1-infected individuals..” J Virol 85, no. 21 (November 2011): 11502–19. https://doi.org/10.1128/JVI.05363-11.

PMID
21849452
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Liu, Pinghuang, R Glenn Overman, Nicole L. Yates, S Munir Alam, Nathan Vandergrift, Yue Chen, Frederik Graw, et al. “Dynamic antibody specificities and virion concentrations in circulating immune complexes in acute to chronic HIV-1 infection..” J Virol 85, no. 21 (November 2011): 11196–207. https://doi.org/10.1128/JVI.05601-11.

PMID
21865397
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Alam, S Munir, Hua-Xin Liao, S Moses Dennison, Frederick Jaeger, Robert Parks, Kara Anasti, Andrew Foulger, et al. “Differential reactivity of germ line allelic variants of a broadly neutralizing HIV-1 antibody to a gp41 fusion intermediate conformation..” J Virol 85, no. 22 (November 2011): 11725–31. https://doi.org/10.1128/JVI.05680-11.

PMID
21917975
Full Text

Liao, Hua-Xin, Xi Chen, Supriya Munshaw, Ruijun Zhang, Dawn J. Marshall, Nathan Vandergrift, John F. Whitesides, et al. “Initial antibodies binding to HIV-1 gp41 in acutely infected subjects are polyreactive and highly mutated..” J Exp Med 208, no. 11 (October 24, 2011): 2237–49. https://doi.org/10.1084/jem.20110363.

PMID
21987658
Full Text

Bonsignori, M., X. Wu, M. A. Moody, H. Liao, K. Hwang, J. A. Crump, S. H. Capiga, et al. “Isolation of CD4-Binding Site and V2/V3 Conformational (Quaternary) Broadly Neutralizing Antibodies from the Same HIV-1 Infected African Subject.” In Aids Research and Human Retroviruses, 27:A120–A120. MARY ANN LIEBERT INC, 2011.

Scholars@Duke

Bonsignori, Mattia, Kwan-Ki Hwang, Xi Chen, Chun-Yen Tsao, Lynn Morris, Elin Gray, Dawn J. Marshall, et al. “Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors..” J Virol 85, no. 19 (October 2011): 9998–10009. https://doi.org/10.1128/JVI.05045-11.

PMID
21795340
Full Text

Verkoczy, Laurent, Yao Chen, Hilary Bouton-Verville, Jinsong Zhang, Marilyn Diaz, Jennifer Hutchinson, Ying-Bin Ouyang, et al. “Rescue of HIV-1 broad neutralizing antibody-expressing B cells in 2F5 VH x VL knockin mice reveals multiple tolerance controls..” J Immunol 187, no. 7 (October 1, 2011): 3785–97. https://doi.org/10.4049/jimmunol.1101633.

PMID
21908739
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Cale, Evan M., Heidi S. Bazick, Tony A. Rianprakaisang, S Munir Alam, and Norman L. Letvin. “Mutations in a dominant Nef epitope of simian immunodeficiency virus diminish TCR:epitope peptide affinity but not epitope peptide:MHC class I binding..” J Immunol 187, no. 6 (September 15, 2011): 3300–3313. https://doi.org/10.4049/jimmunol.1101080.

PMID
21841125
Full Text

Ma, Ben-Jiang, S Munir Alam, Eden P. Go, Xiaozhi Lu, Heather Desaire, Georgia D. Tomaras, Cindy Bowman, et al. “Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies..” Plos Pathog 7, no. 9 (September 2011). https://doi.org/10.1371/journal.ppat.1002200.

PMID
21909262
Full Text

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