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Professor;
Ph.D., Tulane University, 1974

Research and Professional Interests:

We have two major projects in the lab at this time:

1. Structural analysis of the AIDS viruses and neutralizing antibodies
2. Characterization of food allergens
3. Structural analysis of immunoglobulins and immune complexes

1. AIDS Structural Research:

Electron microscopic analysis of recombinant AIDS virus envelope (Env) proteins. The Env spikes on the surface of HIV-1 and related viruses foster viral fusion with target T-helpers cells and macrophages and are the targets for neutralizing antibodies. We have analyzed several molecular forms that are being considered as vaccine candidates. We are particularly interested in using well characterized neutralizing antibodies to map the surface of gp120 and its precursor molecule, gp160. Extensive use is made of negative stain electron microscopic for these analyses.

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AIDS virus (SIV) envelope spike model derived by cryoelectron microscopy tomography of over 6,000 spikes. Zhu, et al. Nature 441: 847-852, 2006.		Averaged electron microscopic image and X-ray model of the HIV-1 neutralizing antibody, 2G12, showing a unique domain-exchanged structure of the heavy chains such that the Fab arms are locked together. Calarese et al., Science 300: 2065–2071, 2003.

Tomographic analysis of HIV-1 and SIV. We were the first to publish a detailed look at the surface features of the AIDS viruses by using negative stain and cryoelectron microscopic tomography techniques to generate 3-D images of viruses. The envelope spikes were found to be few in number and somewhat clustered on the surface of HIV-1. By averaging the spike images on SIV, we generated a 3-D image of the spike and tentatively fitted the know crystal structures of the gp120 and gp41 subunits within the spike density. We have now extended our findings to include models of the spikes on HIV-1 and were surprised to find that the spikes are rather flexible. We are particularly interested in viewing the binding of neutralizing antibodies and CD4 in complex with the envelope spikes on the surface of virions.

3-D tomogram (serial layers) of a single SIV virus particle showing surface envelope spikes. Zhu et al., Proc. Natl. Acad. Sci. USA, 100: 15812-15817, 2003.

2. Characterization of food allergens:

About 3% of the population has some sort of allergic response to one or more foods and 0.5% are specifically allergic to tree nuts. Other patients have IgE antibodies to nut proteins but don’t show allergic symptoms. We have been identifying allergies in cashew, walnut, almond, chestnut, and pistachio using serum from allergic patients to screen cDNA expression libraries. Once cloned and expressed, the offending proteins are subjected to epitope mapping techniques and mutagenesis to generate hypoallergenic version. At the same time, we are developing polyclonal and monoclonal antibodies to tree nut allergens to be used by the food industry in testing suspected foods for contamination with allergens.

Model of cashew 11S globulin, a potent trimeric allergen, in which the IgE-binding sites (colored residues) are highlighted on one subunit (grey).

3. Structural Analysis of Immunoglobulins and Immune Complexes:

A long standing interest of the lab has been the structural analysis of immunoglobulins and immune complexes. More recent studies have included biochemical and electron microscopic analyses of unique domain-exchanged anti-HIV-1 carbohydrate antibodies and lamprey antibodies that are structurally and genetically unrelated to any other vertebrate immunoglobulins.

AIDS Publications

Ping Zhu, P. Winkler, H., Chertova, E., Taylor, K. A., and Roux, K. H. Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathogens. 4: e1000203. doi:10.1371/journal.ppat.1000203. 2008
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Winkler, H., Zhu, P., Liu, J., Ye, F., Roux, K. H., and Taylor, K. A. Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes. (in press, J. Struct. Biol.)

Crooks, E. T, Moore, P. L., Franti, M., Cayanan, C. S., Zhu, P., Jiang, P., de Vries, R. P., Wiley, C., Zharkikh, I, Schülke, N., Roux, K. H., Montefiori, D. C., Burton, D. R, and Binley, J. M. A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and soluble monomeric gp120. Virology 366:245-262. 2007.
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Iyer, S. P. N., Franti, M., Krauchuk, A. A., Fisch, D. N., Ouattara, A. A., Roux, K. H., Krawiec, L., Dey, A. K., Beddows, S., Maddon, P. J., Moore, J. P., and Olson, W. C. Purified, proteolytically mature HIV type 1 SOSIP gp140 envelope trimers. AIDS Res. Human Retroviruses 23:817-828. 2007.
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Roux, K. H. and Taylor, K. A. AIDS virus envelope spike structure. Current Opinion in Structural Biology. 17: 244-252. 2007.
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Zhu, P. Liu,J., Bess Jr., J., Chertova, E., Lifson, J. D., Grise, H., Ofek, G., Taylor, K. A., and Roux, K. H. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature, 441:847-852, 2006.
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Moore,.P. L., Crooks, E. T. Porter, L, Zhu, P., Cayanan, C. S., Grise, H, Corcoran, P., Zwick, M. B., Franti, M., Morris, L., Roux, K. H.,. Burton, D. R., and Binley, J. M. Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type-1. J. Virol. 80:2515-2528, 2006.
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Pancera, M., Lebowitz, J., Schön, A., Zhu, P., Freire, E., Kwong, P. D., Roux, K. H., Sodroski, J. and Wyatt, R. Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis. J. Virol., 79:9954-9969, 2005.
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Roux, K. H., Zhu, P. Seavy, M., Katinger, H., Kunert, R., Seamon, V. Electron microscopic and immunochemical analysis of the broadly neutralizing HIV-1-specific, anti-carbohydrate antibody, 2G12. Mol. Immunol. 41:1001-1011. 2004.
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Zhu, P., Chertova, E., Bess, J., Jr., Lifson, J. D., Arthur, L. O., Liu, J., Taylor, K. A., and Roux, K. H. Electron tomography analysis of envelope glycoprotein trimers on HIV and SIV virions. Proc. Natl. Acad. Sci. USA, 100:15812-15817. 2003.
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Calarese, D. A., C. N. Scanlan, M. B. Zwick, S. Deechongkit, Y. Mimura, R. Kunert, P. Zhu, M. R. Wormald, R. I. Stanfield, K. H. Roux, J. W. Kelly, P. M. Rudd, R. A. Dwek, H. Katinger, D. R. Burton, and I. A. Wilson. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300:2065-2071. 2003.
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Srivastava, I. K., L. Stamatatos, E. Kan, Y. Lian, S. Hilt, L. Martin, C. Vita, P. Zhu, K. H. Roux, L. Vojtech, M. Wininger, J. B. Ulmer, and S. W. Barnett. Purification and characterization of a soluble trimeric envelope protein containing a partial deletion of the V2 loop derived from SF162, an R5-tropic HIV-1 isolate. J. Virol., 77:11244-11259. 2003.
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Schülke, N., M. S. Vesanen, R. W. Sanders, P. Zhu, M. Lu, D. J. Anselma, A. R. Villa, P. W. H. I. Parren, J. M. Binley, K. H. Roux, P. J. Maddon, J. P. Moore, and W. C. Olson. Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus type 1 gp140 envelope glycoprotein. J. Virol. 76:7760-7776. 2002.
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Zhu, P., W. C. Olson, and K. H. Roux. Structural flexibility and functional valency of CD4-IgG2 (PRO 542): potential for crosslinking HIV-1 envelope spikes. J. Virol. 75:6682-6686. 2001.
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Allergy Publications

Willison, L. N., Tawde, P., Robotham, J. M. Penney, R., Teuber, S. S., Sathe, S. K., Roux, K. H. Pistachio vicilin, Pis v 3, is IgE-reactive and cross-reacts with the homologous cashew allergen, Ana o 1. Clin. Exp. Allergy 38:1220-1238. 2008.
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Comstock, S. S., Robotham, JM, Tawde, P., Kshirsagar H, Sathe, S. K. Roux, K. H., Teuber, S. S. IgE-reactive proteins in cashew (Anacardium occidentale) apple juice concentrate. J. Agric. Food Chem. 56:5977-5982. 2008.
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Venkatachalam, M., Monaghan, E. K., Kshirsagar, H. H., Robotham, J. M., O’Donnell, S. E., Gerber, M. S., Roux, K. H., and Sathe, S. K. Effects of processing on antigenic stability of cashew nut (Anacardium occidentale L.) proteins. J. Agric. Food Chem. 56:8998-9005. 2008.
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Tawde, P., Venkatesh, Y. P., Wang, F., Teuber, S. S., Sathe, S, K., and Roux, K. H. Cloning and characterization of profilin (Pru du 4), a cross-reactive almond (Prunus dulcis) allergen. J. Allergy Clin. Immunol. 118:915-922. 2006.
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Robotham, J. M., Wang, F., Seamon, V, Teuber, S. S., Sathe, S. K., Beyer, K, Sampson, H. and Roux, K. H. Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family. J. Allergy Clin. Immunol. 15:1284-1290, 2005.
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Sathe, S. K., Teuber, S. S., Roux, K. H. Effects of food processing on the stability of food allergens. Biotech. Adv. 232:423-429, 2005.
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Wallowitz, M. L., Comstock, S. S., Roux, K. H., Sathe, S. K., and Teuber, S. K. Walnut Allergens. Food Allergy and Intolerance, 5:187-195, 2004.

Roux, K. H., S. S. Teuber, and S. K. Sathe. Tree nut allergens. Int. Arch. Allergy Immunol., 131:234-244. 2003.
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Teuber, S. S., S. S. Comstock, S. K. Sathe, and K. H. Roux. Tree nut allergy. Curr. Allergy Asthma Rep. 3:54-61. 2003.

Wang, F., J. M. Robotham, S. S. Teuber, S. K. Sathe, and K. H. Roux. Ana o 2, a major cashew nut (Anacardium occidentale L.) allergen of the legumin family. Int. Arch. Allergy Immunol., 132:27-39. 2003.
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Wei, Y., K. Shridhar, S. K. Sathe, S. S. Teuber, and. K. H. Roux. A sensitive sandwich ELISA for the detection of trace amounts of cashew (Anacardium occidentale) nut in foods. J. Agric. Food Chem. 51:3215-3221. 2003.
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Robotham, J. M., Teuber, S. S., Sathe, S. K., and Roux, K. H. Linear IgE epitope mapping of the English walnut (Juglans regia) major food allergen, Jug r 1. J. Allergy Clin. Immunol. 109:143-149, 2002.
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Wang, F., J. M. Robotham, S. S. Teuber, P. Tawde, S. K. Sathe, and K. H. Roux. Ana o 1, a cashew (Anacardium occidentale) allergen of the vicilin seed storage protein family. J. Allergy Clin. Immunol. 110:160-166. 2002.
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Roux, K. H., S. S. Teuber, J. M. Robotham, and S. K. Sathe. Detection and stability of the major almond allergen in foods. J. Agric .Food Chem. 49:2131-2136. 2001.
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Laffer, S., Hogbom, E., Roux, K. H., Sperr, W. R., Valent, P., Bankl, H. C., Vangelista, L., Kricek, F., Kraft, D., Gronlund, H., and Valenta, R. A molecular model of type I allergy: Identification and characterization of a nonanaphylactic anti-human IgE antibody fragment that blocks the IgE-Fc epsilon RI interaction and reacts with receptor-bound IgE. J. Allergy Clin. Immunol. 108:409-416, 2001.
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Antibody Structural Study Publications

Herrin, B. H., Alder, M. N., Roux, K. H., Sina, C., Ehrhardt, G. R., Boydstron, J. A., Turnbough C. L. Jr., and Cooper, M. D. Structure and specificity of lamprey monoclonal antibodies. PNAS 105:2040-2045. 2008
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Roux, K. H., Zhu, P. Seavy, M., Katinger, H., Kunert, R., Seamon, V. Electron microscopic and immunochemical analysis of the broadly neutralizing HIV-1-specific, anti-carbohydrate antibody, 2G12. Mol. Immunol. 41:1001-1011, 2004
[PDF]

Calarese, D. A., Scanlan, C. N., Zwick, M. B., Deechongkit, S., Mimura, Y., Kunert, R., Zhu, P., Wormald, M. R., Stanfield, R. L., Roux, K. H., Kelly, J. W., Rudd, P. M., Dwek, R. A., Katinger, H., Burton, D. R., and Wilson, I. A. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300:2065–2071, 2003
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Johansson, A., Erlandsson, A., Eriksson, D., Ullen, A., Holm, P., Sundstrom, B. E., Roux, K. H., and Stigbrand, T. Idiotypic-anti-idiotypic complexes and their in vivo metabolism. Cancer 94:1306–1313, 2002.
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Laffer, S., Hogbom, E., Roux, K. H., Sperr, W. R., Valent, P., Bankl, H. C., Vangelista, L., Kricek, F., Kraft, D., Gronlund, H., and Valenta, R. A Molecular model of type I allergy:identification and characterization of a nonanaphylactic anti-human IgE antibody fragment that blocks the IgE-Fc epsilon RI interaction and reacts with receptor-bound IgE. J. Allergy Clin. Immunol. 108:409–416, 2001
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Roux, K. H. Immunoglobulin structure and function as revealed by electron microscopy. Int. Arch. Allergy Immunol. 120:85–99, 1999
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Zhu, P., Olson, W. C., and Roux, K. H. Structural flexibility and functional valency of CD4- IgG2 (PRO 542): potential for cross-linking human immunodeficiency virus type 1 envelope spikes. J. Virol. 75:6682–6686, 2001

Roux, K. H., Greenberg, A. S., Green, L., Strelets, L., Avila, D., McKinney, E. C., and Flajnik. M. F. Structural analysis of the nurse shark (new) antigen receptor (NAR): molecular convergence of NAR and unusual mammalian immunoglobulins. Proc. Natl. Acad. Sci. USA 95:11804–11809, 1998

Roux, K. H., Strelets, L., Brekke, O. H., Sandlie, I., and Michaelsen, T. E. Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE and IgA2 to form small immune complexes: a role for flexibility and geometry. J. Immunol. 161:4083–4090, 1998

Dutta, Moumita
Xia, Lixin

Graduate Students:

Dhole, Bodhana
Grisé, Henry C
Willison, Leanna

Technicians:

Belcher, Sarah

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