Abstract
Understanding the molecular mechanisms of cell-to-cell communication is one of the major challenges in today’s biology, especially in the immune and nervous systems, where such communication leads to immediate effector functions, as well as to storage of memory [1–3].
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Edelman GM (1993) Neural Darwinism: selection and reentrant signaling in higher brain function. Neuron 10:115–125
Shaw AS, Allen PM (2001) Kissing cousins: immunological and neurological synapses. Nat Immunol 2:575–576
Dustin ML, Colman DR (2002) Neural and immunological synaptic relations. Science 298:785–789
Trautmann A (2005) Microclusters initiate and sustain T cell signaling. Nat Immunol 6:1213–1214
Pike LJ (2006) Rafts defined: a report on the keystone symposium on lipid rafts and cell function. J Lipid Res 47:1597–1598
Matkó J, Szöllősi J (2005) Membrane microdomain signaling. Lipid rafts. In: Mattson MP (ed) Biology and medicine. Humana, Totowa, NJ, pp 15–46
Willig KI, Kellner RR, Medda R, Hein B, Jakobs S, Hell SW (2006) Nanoscale resolution in GFP-based microscopy. Nat Methods 3:721–723
Eggeling C, Ringemann C, Medda R, Schwarzmann G, Sandhoff K, Polyakova S, Belov VN, Hein B, von Middendorff C, Schonle A, Hell SW (2009) Direct observation of the nanoscale dynamics of membrane lipids in a living cell. Nature 457:1159–1162
Fantini J (2007) Interaction of proteins with lipid rafts through glycolipid-binding domains: biochemical background and potential therapeutic applications. Curr Med Chem 14:2911–2917
Taylor DR, Hooper NM (2007) Role of lipid rafts in the processing of the pathogenic prion and Alzheimer’s amyloid-β proteins. Semin Cell Dev Biol 18:638–648
Jolly C, Sattentau QJ (2005) Human immunodeficiency virus type 1 virological synapse formation in T cells requires lipid raft integrity. J Virol 79:12088–12094
Feldner JC, Brandt BH (2002) Cancer cell motility-on the road from c-ErbB-2 receptor steered signaling to actin reorganization. Exp Cell Res 272:93–108
Shawver LK, Slamon D, Ullrich A (2002) Smart drugs: tyrosine kinase inhibitors in cancer therapy. Cancer Cell 1:117–123
Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, Sliwkowski MX (2004) Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell 5:317–328
Andrews NL, Lidke KA, Pfeiffer JR, Burns AR, Wilson BS, Oliver JM, Lidke DS (2008) Actin restricts FceRI diffusion and facilitates antigen-induced receptor immobilization. Nat Cell Biol 10:955–963
Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I (2010) Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464(7289):783–787. doi:10.1038/nature08827
Szabó Á, Horváth G, Szöllősi J, Nagy P (2008) Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements. Biophys J 95:2086–2096
Nagy P, Jenei A, Kirsch AK, Szöllősi J, Damjanovich S, Jovin TM (1999) Activation-dependent clustering of the ErbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J Cell Sci 112:1733–1741
Citri A, Yarden Y (2006) EGF-ErbB signalling: towards the systems level. Nat Rev Mol Cell Biol 7:505–516
Nahta R, Esteva FJ (2006) Herceptin: mechanisms of action and resistance. Cancer Lett 232:123–138
Nelson AL (2010) Antibody fragments: hope and hype. MAbs 2:77–83
Filpula D (2007) Antibody engineering and modification technologies. Biomol Eng 24:201–215
Alguel Y, Leung J, Singh S, Rana R, Civiero L, Alves C, Byrne B (2010) New tools for membrane protein research. Curr Protein Pept Sci 11:156–165
Magliery TJ, Regan L (2006) Reassembled GFP: detecting protein-protein interactions and protein expression patterns. Methods Biochem Anal 47:391–405
Miyawaki A, Nagai T, Mizuno H (2005) Engineering fluorescent proteins. Adv Biochem Eng Biotechnol 95:1–15
Kampani K, Quann K, Ahuja J, Wigdahl B, Khan ZK, Jain P (2007) A novel high throughput quantum dot-based fluorescence assay for quantitation of virus binding and attachment. J Virol Methods 141:125–132
Day RN, Davidson MW (2009) The fluorescent protein palette: tools for cellular imaging. Chem Soc Rev 38:2887–2921
Herbst KJ, Ni Q, Zhang J (2009) Dynamic visualization of signal transduction in living cells: from second messengers to kinases. IUBMB Life 61:902–908
Chan FK (2004) Monitoring molecular interactions in living cells using flow cytometric analysis of fluorescence resonance energy transfer. Methods Mol Biol 261:371–382
Witternberg NJ, Haynes CL (2009) Using nanoparticles to push the limits of detection. Wiley Interdiscip Rev Nanomed Nanobiotechnol 1:237–254
Kalab P, Pralle A (2008) Chapter 21: quantitative fluorescence lifetime imaging in cells as a tool to design computational models of ran-regulated reaction networks. Methods Cell Biol 89:541–568
Willig KI, Rizzoli SO, Westphal V, Jahn R, Hell SW (2006) STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis. Nature 440:935–939
Stockl M, Plazzo AP, Korte T, Herrmann A (2008) Detection of lipid domains in model and cell membranes by fluorescence lifetime imaging microscopy of fluorescent lipid analogues. J Biol Chem 283:30828–30837
Stockl MT, Herrmann A (2010) Detection of lipid domains in model and cell membranes by fluorescence lifetime imaging microscopy. Biochim Biophys Acta 1798(7):1444–1456
Muzzey D, van Oudenaarden A (2009) Quantitative time-lapse fluorescence microscopy in single cells. Annu Rev Cell Dev Biol 25:301–327
de Almeida RF, Loura LM, Prieto M (2009) Membrane lipid domains and rafts: current applications of fluorescence lifetime spectroscopy and imaging. Chem Phys Lipids 157:61–77
Vereb G, Szöllősi J, Damjanovich S, Matkó J (2004) Exploring membrane microdomains and functional protein clustering in live cells with flow and image cytometric methods. In: Geddes CD, Lakowicz JR (eds) Reviews in fluorescence. Kluwer/Plenum, New York, pp 99–120
Brown DA, Rose JK (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533–544
Brown DA (2006) Lipid rafts, detergent-resistant membranes, and raft targeting signals. Physiology (Bethesda) 21:430–439
Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387:569–572
Nagy P, Vereb G, Sebestyén Z, Horváth G, Lockett SJ, Damjanovich S, Park JW, Jovin TM, Szöllősi J (2002) Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2. J Cell Sci 115:4251–4262
Harder T, Scheiffele P, Verkade P, Simons K (1998) Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol 141:929–942
Lingwood D, Simons K (2010) Lipid rafts as a membrane-organizing principle. Science 327:46–50
Bíró A, Cervenak L, Balogh A, Lorincz A, Uray K, Horváth A, Romics L, Matkó J, Fust G, László G (2007) Novel anti-cholesterol monoclonal immunoglobulin G antibodies as probes and potential modulators of membrane raft-dependent immune functions. J Lipid Res 48:19–29
Gombos I, Steinbach G, Pomozi I, Balogh A, Vámosi G, Gansen A, László G, Garab G, Matkó J (2008) Some new faces of membrane microdomains: a complex confocal fluorescence, differential polarization, and FCS imaging study on live immune cells. Cytom A 73:220–229
Bagatolli LA, Gratton E (1999) Two-photon fluorescence microscopy observation of shape changes at the phase transition in phospholipid giant unilamellar vesicles. Biophys J 77:2090–2101
Gaus K, Zech T, Harder T (2006) Visualizing membrane microdomains by Laurdan 2-photon microscopy. Mol Membr Biol 23:41–48
Gaus K, Gratton E, Kable EP, Jones AS, Gelissen I, Kritharides L, Jessup W (2003) Visualizing lipid structure and raft domains in living cells with two-photon microscopy. Proc Natl Acad Sci USA 100:15554–15559
Parasassi T, Gratton E, Yu WM, Wilson P, Levi M (1997) Two-photon fluorescence microscopy of laurdan generalized polarization domains in model and natural membranes. Biophys J 72:2413–2429
Jares-Erijman EA, Jovin TM (2006) Imaging molecular interactions in living cells by FRET microscopy. Curr Opin Chem Biol 10:409–416
Jares-Erijman EA, Jovin TM (2003) FRET imaging. Nat Biotechnol 21:1387–1395
Nagy P, Vámosi G, Bodnár A, Lockett SJ, Szöllősi J (1998) Intensity-based energy transfer measurements in digital imaging microscopy. Eur Biophys J 27:377–389
Vereb G, Matkó J, Szöllősi J (2004) Cytometry of fluorescence resonance energy transfer. Methods Cell Biol 75:105–152
Kusumi A, Suzuki K (2005) Toward understanding the dynamics of membrane-raft-based molecular interactions. Biochim Biophys Acta 1746:234–251
Dietrich C, Yang B, Fujiwara T, Kusumi A, Jacobson K (2002) Relationship of lipid rafts to transient confinement zones detected by single particle tracking. Biophys J 82:274–284
Suzuki K, Ritchie K, Kajikawa E, Fujiwara T, Kusumi A (2005) Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques. Biophys J 88:3659–3680
Dietrich C, Volovyk ZN, Levi M, Thompson NL, Jacobson K (2001) Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers. Proc Natl Acad Sci USA 98:10642–10647
Schutz GJ, Kada G, Pastushenko VP, Schindler H (2000) Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy. EMBO J 19:892–901
Kahya N, Scherfeld D, Bacia K, Poolman B, Schwille P (2003) Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy. J Biol Chem 278:28109–28115
Scherfeld D, Kahya N, Schwille P (2003) Lipid dynamics and domain formation in model membranes composed of ternary mixtures of unsaturated and saturated phosphatidylcholines and cholesterol. Biophys J 85:3758–3768
Bacia K, Scherfeld D, Kahya N, Schwille P (2004) Fluorescence correlation spectroscopy relates rafts in model and native membranes. Biophys J 87:1034–1043
Vereb G, Matkó J, Vámosi G, Ibrahim SM, Magyar E, Varga S, Szöllősi J, Jenei A, Gáspár R Jr, Waldmann TA, Damjanovich S (2000) Cholesterol-dependent clustering of IL-2Rα and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts. Proc Natl Acad Sci USA 97:6013–6018
Matkó J, Bodnar A, Vereb G, Bene L, Vámosi G, Szentesi G, Szöllősi J, Gáspár R, Horejsi V, Waldmann TA, Damjanovich S (2002) GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines. Eur J Biochem 269:1199–1208
Pralle A, Keller P, Florin EL, Simons K, Horber JK (2000) Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J Cell Biol 148:997–1008
Manes S, del Real G, Martinez AC (2003) Pathogens: raft hijackers. Nat Rev Immunol 3:557–568
Parton RG, Richards AA (2003) Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic 4:724–738
Carrasco M, Amorim MJ, Digard P (2004) Lipid raft-dependent targeting of the influenza A virus nucleoprotein to the apical plasma membrane. Traffic 5:979–992
Wilflingseder D, Stoiber H (2007) Float on: lipid rafts in the lifecycle of HIV. Front Biosci 12:2124–2135
Hambleton S, Steinberg SP, Gershon MD, Gershon AA (2007) Cholesterol dependence of varicella-zoster virion entry into target cells. J Virol 81:7548–7558
Stryer L, Haugland RP (1967) Energy transfer: a spectroscopic ruler. Proc Natl Acad Sci USA 58:719–726
Nagy P, Vereb G, Damjanovich S, Mátyus L, Szöllősi J (2006) Measuring FRET in flow and image cytometry. In: Robinson JP (ed) Current protocols in cytometry. Wiley, New York, pp 12.18.11–12.18.13
Szöllősi J, Damjanovich S, Nagy P, Vereb G, Mátyus L (2006) Principles of resonance energy transfer. In: Robinson JP (ed) Current protocols in cytometry. Wiley, New York, pp 1.12.11–11.12.16
VanBeek DB, Zwier MC, Shorb JM, Krueger BP (2007) Fretting about FRET: correlation between kappa and R. Biophys J 92:4168–4178
Dale RE, Eisinger J, Blumberg WE (1979) The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys J 26:161–193
Anikovsky M, Dale L, Ferguson S, Petersen N (2008) Resonance energy transfer in cells: a new look at fixation effect and receptor aggregation on cell membrane. Biophys J 95:1349–1359
Kenworthy AK, Edidin M (1998) Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer. J Cell Biol 142:69–84
Bastiaens PI, Majoul IV, Verveer PJ, Soling HD, Jovin TM (1996) Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J 15:4246–4253
Karpova TS, Baumann CT, He L, Wu X, Grammer A, Lipsky P, Hager GL, McNally JG (2003) Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J Microsc 209:56–70
Kirber MT, Chen K, Keaney JF Jr (2007) YFP photoconversion revisited: confirmation of the CFP-like species. Nat Methods 4:767–768
Roszik J, Szöllősi J, Vereb G (2008) AccPbFRET: an ImageJ plugin for semi-automatic, fully corrected analysis of acceptor photobleaching FRET images. BMC Bioinform 9:346
Rasband WS (1997) ImageJ, US National Institutes of Health, Bethesda, MD. http://res.info.nih.gov/ij
Stepensky D (2007) FRETcalc plugin for calculation of FRET in non-continuous intracellular compartments. Biochem Biophys Res Commun 359:752–758
Trón L, Szöllősi J, Damjanovich S, Helliwell SH, Arndt-Jovin DJ, Jovin TM (1984) Flow cytometric measurement of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell-by-cell basis. Biophys J 45:939–946
Sebestyén Z, Nagy P, Horváth G, Vámosi G, Debets R, Gratama JW, Alexander DR, Szöllősi J (2002) Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer. Cytometry 48:124–135
Roszik J, Lisboa D, Szöllősi J, Vereb G (2009) Evaluation of intensity-based ratiometric FRET in image cytometry – approaches and a software solution. Cytom A 75:761–767
Feige JN, Sage D, Wahli W, Desvergne B, Gelman L (2005) PixFRET, an ImageJ plug-in for FRET calculation that can accommodate variations in spectral bleed-throughs. Microsc Res Tech 68:51–58
Fazekas Z, Petrás M, Fábián A, Pályi-Krekk Z, Nagy P, Damjanovich S, Vereb G, Szöllősi J (2008) Two-sided fluorescence resonance energy transfer for assessing molecular interactions of up to three distinct species in confocal microscopy. Cytom A 73:209–219
Jovin TM, Arndt-Jovin DJ (1989) Luminescence digital imaging microscopy. Annu Rev Biophys Biophys Chem 18:271–308
Young RM, Arnette JK, Roess DA, Barisas BG (1994) Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics. Biophys J 67:881–888
Chen Y, Muller JD, So PT, Gratton E (1999) The photon counting histogram in fluorescence fluctuation spectroscopy. Biophys J 77:553–567
Brock R, Hink MA, Jovin TM (1998) Fluorescence correlation microscopy of cells in the presence of autofluorescence. Biophys J 75:2547–2557
Schwille P, Korlach J, Webb WW (1999) Fluorescence correlation spectroscopy with single-molecule sensitivity on cell and model membranes. Cytometry 36:176–182
Digman MA, Dalal R, Horwitz AF, Gratton E (2008) Mapping the number of molecules and brightness in the laser scanning microscope. Biophys J 94:2320–2332
Digman MA, Brown CM, Sengupta P, Wiseman PW, Horwitz AR, Gratton E (2005) Measuring fast dynamics in solutions and cells with a laser scanning microscope. Biophys J 89:1317–1327
Runnels LW, Scarlata SF (1995) Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys J 69:1569–1583
Bader AN, Hofman EG, Voortman J, van Bergen En Henegouwen PM, Gerritsen HC (2009) Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution. Biophys J 97:2613–2622
Lidke DS, Nagy P, Barisas BG, Heintzmann R, Post JN, Lidke KA, Clayton AH, Arndt-Jovin DJ, Jovin TM (2003) Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET). Biochem Soc Trans 31:1020–1027
Yeow EK, Clayton AH (2007) Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: theory and application. Biophys J 92:3098–3104
Gadella TW Jr, Jovin TM (1995) Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J Cell Biol 129:1543–1558
Clayton AH, Klonis N, Cody SH, Nice EC (2005) Dual-channel photobleaching FRET microscopy for improved resolution of protein association states in living cells. Eur Biophys J 34:82–90
Hoppe A, Christensen K, Swanson JA (2002) Fluorescence resonance energy transfer-based stoichiometry in living cells. Biophys J 83:3652–3664
Szabó Á, Szöllősi J, Nag P (2010) Coclustering of ErbB1 and ErbB2 revealed by FRET-sensitized acceptor bleaching. Biophys J 99(1):105–114
Mekler VM (1994) A photochemical technique to enhance sensitivity of detection of fluorescence resonance energy transfer. Photochem Photobiol 59:615–620
Mekler VM, Averbakh AZ, Sudarikov AB, Kharitonova OV (1997) Fluorescence energy transfer-sensitized photobleaching of a fluorescent label as a tool to study donor-acceptor distance distributions and dynamics in protein assemblies: studies of a complex of biotinylated IgM with streptavidin and aggregates of concanavalin A. J Photochem Photobiol B 40:278–287
Bublil EM, Yarden Y (2007) The EGF receptor family: spearheading a merger of signaling and therapeutics. Curr Opin Cell Biol 19:124–134
Klapper LN, Glathe S, Vaisman N, Hynes NE, Andrews GC, Sela M, Yarden Y (1999) The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors. Proc Natl Acad Sci USA 96:4995–5000
Lemmon MA (2009) Ligand-induced ErbB receptor dimerization. Exp Cell Res 315:638–648
Mocanu MM, Fazekas Z, Petrás M, Nagy P, Sebestyén Z, Isola J, Timar J, Park JW, Vereb G, Szöllősi J (2005) Associations of ErbB2, β1-integrin and lipid rafts on Herceptin (Trastuzumab) resistant and sensitive tumor cell lines. Cancer Lett 227:201–212
Pályi-Krekk Z, Barok M, Isola J, Tammi M, Szöllősi J, Nagy P (2007) Hyaluronan-induced masking of ErbB2 and CD44-enhanced trastuzumab internalisation in trastuzumab resistant breast cancer. Eur J Cancer 43:2423–2433
Kawashima N, Nakayama K, Itoh K, Itoh T, Ishikawa M, Biju V (2010) Reversible dimerization of EGFR revealed by single-molecule fluorescence imaging using quantum dots. Chemistry 16:1186–1192
Lidke DS, Wilson BS (2009) Caught in the act: quantifying protein behaviour in living cells. Trends Cell Biol 19:566–574
Gimpl G, Gehrig-Burger K (2007) Cholesterol reporter molecules. Biosci Rep 27:335–358
Dijkstra J, Swartz GM Jr, Raney JJ, Aniagolu J, Toro L, Nacy CA, Green SJ (1996) Interaction of anti-cholesterol antibodies with human lipoproteins. J Immunol 157:2006–2013
Swartz GM Jr, Gentry MK, Amende LM, Blanchette-Mackie EJ, Alving CR (1988) Antibodies to cholesterol. Proc Natl Acad Sci USA 85:1902–1906
Clarke MS, Vanderburg CR, Bamman MM, Caldwell RW, Feeback DL (2000) In situ localization of cholesterol in skeletal muscle by use of a monoclonal antibody. J Appl Physiol 89:731–741
Perl-Treves D, Kessler N, Izhaky D, Addadi L (1996) Monoclonal antibody recognition of cholesterol monohydrate crystal faces. Chem Biol 3:567–577
Kruth HS, Ifrim I, Chang J, Addadi L, Perl-Treves D, Zhang WY (2001) Monoclonal antibody detection of plasma membrane cholesterol microdomains responsive to cholesterol trafficking. J Lipid Res 42:1492–1500
Smart EJ, Ying Y, Donzell WC, Anderson RG (1996) A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J Biol Chem 271:29427–29435
Underwood KW, Jacobs NL, Howley A, Liscum L (1998) Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane. J Biol Chem 273:4266–4274
Steinbach G, Pomozi I, Zsiros O, Pay A, Horvath GV, Garab G (2008) Imaging fluorescence detected linear dichroism of plant cell walls in laser scanning confocal microscope. Cytom A 73:202–208
Bíró A, Horváth A, Varga L, Nemesanszky E, Csepregi A, David K, Tolvaj G, Ibranyi E, Telegdy L, Par A, Romics L, Karadi I, Horanyi M, Gervain J, Ribiczey P, Csondes M, Fust G (2003) Serum anti-cholesterol antibodies in chronic hepatitis-C patients during IFN-α-2b treatment. Immunobiology 207:161–168
Egri G, Orosz I (2006) Elevated anti-cholesterol antibody levels in the sera of non-small cell lung cancer patients. Interact Cardiovasc Thorac Surg 5:649–651
Horváth A, Banhegyi D, Bíró A, Ujhelyi E, Veres A, Horváth L, Prohaszka Z, Bacsi A, Tarjan V, Romics L, Horváth I, Toth FD, Fust G, Karadi I (2001) High level of anticholesterol antibodies (ACHA) in HIV patients. Normalization of serum ACHA concentration after introduction of HAART. Immunobiology 203:756–768
Horváth A, Fust G, Horváth I, Vallus G, Duba J, Harcos P, Prohaszka Z, Rajnavölgyi E, Janoskuti L, Kovács M, Császár A, Romics L, Karadi I (2001) Anti-cholesterol antibodies (ACHA) in patients with different atherosclerotic vascular diseases and healthy individuals. Characterization of human ACHA. Atherosclerosis 156:185–192
Gombos I, Detre C, Vámosi G, Matkó J (2004) Rafting MHC-II domains in the APC (presynaptic) plasma membrane and the thresholds for T-cell activation and immunological synapse formation. Immunol Lett 92:117–124
Poloso NJ, Roche PA (2004) Association of MHC class II-peptide complexes with plasma membrane lipid microdomains. Curr Opin Immunol 16:103–107
Pizzo P, Viola A (2004) Lipid rafts in lymphocyte activation. Microbes Infect 6:686–692
Rosenberger CM, Brumell JH, Finlay BB (2000) Microbial pathogenesis: lipid rafts as pathogen portals. Curr Biol 10:R823–R825
Yoshizaki F, Nakayama H, Iwahara C, Takamori K, Ogawa H, Iwabuchi K (2008) Role of glycosphingolipid-enriched microdomains in innate immunity: microdomain-dependent phagocytic cell functions. Biochim Biophys Acta 1780:383–392
Beck Z, Balogh A, Kis A, Izsepi E, Cervenak L, László G, Bíró A, Liliom K, Mocsár G, Vámosi G, Fust G, Matkó J (2010) New cholesterol-specific antibodies remodel HIV-1 target cells’ surface and inhibit their in vitro virus production. J Lipid Res 51:286–296
Brown BK, Karasavvas N, Beck Z, Matyas GR, Birx DL, Polonis VR, Alving CR (2007) Monoclonal antibodies to phosphatidylinositol phosphate neutralize human immunodeficiency virus type 1: role of phosphate-binding subsites. J Virol 81:2087–2091
Kozak SL, Heard JM, Kabat D (2002) Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus. J Virol 76:1802–1815
Schwille P, Haupts U, Maiti S, Webb WW (1999) Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation. Biophys J 77:2251–2265
Rawat SS, Zimmerman C, Johnson BT, Cho E, Lockett SJ, Blumenthal R, Puri A (2008) Restricted lateral mobility of plasma membrane CD4 impairs HIV-1 envelope glycoprotein mediated fusion. Mol Membr Biol 25:83–94
Rawat SS, Gallo SA, Eaton J, Martin TD, Ablan S, KewalRamani VN, Wang JM, Blumenthal R, Puri A (2004) Elevated expression of GM3 in receptor-bearing targets confers resistance to human immunodeficiency virus type 1 fusion. J Virol 78:7360–7368
Manes S, del Real G, Lacalle RA, Lucas P, Gomez-Mouton C, Sanchez-Palomino S, Delgado R, Alcami J, Mira E, Martinez AC (2000) Membrane raft microdomains mediate lateral assemblies required for HIV-1 infection. EMBO Rep 1:190–196
Nguyen DH, Giri B, Collins G, Taub DD (2005) Dynamic reorganization of chemokine receptors, cholesterol, lipid rafts, and adhesion molecules to sites of CD4 engagement. Exp Cell Res 304:559–569
Calarese DA, Scanlan CN, Zwick MB, Deechongkit S, Mimura Y, Kunert R, Zhu P, Wormald MR, Stanfield RL, Roux KH, Kelly JW, Rudd PM, Dwek RA, Katinger H, Burton DR, Wilson IA (2003) Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300:2065–2071
Kunert R, Wolbank S, Stiegler G, Weik R, Katinger H (2004) Characterization of molecular features, antigen-binding, and in vitro properties of IgG and IgM variants of 4E10, an anti-HIV type 1 neutralizing monoclonal antibody. AIDS Res Hum Retroviruses 20:755–762
Zwick MB, Komori HK, Stanfield RL, Church S, Wang M, Parren PW, Kunert R, Katinger H, Wilson IA, Burton DR (2004) The long third complementarity-determining region of the heavy chain is important in the activity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5. J Virol 78:3155–3161
Phogat S, Wyatt RT, Karlsson Hedestam GB (2007) Inhibition of HIV-1 entry by antibodies: potential viral and cellular targets. J Intern Med 262:26–43
Acknowledgments
This work was supported by research grants from the Hungarian Scientific Research Fund (K72677, K68763, K62648, T49696), from the European Commission (LSHC-CT-2005-018914), from the New Hungary Development Plan cofinanced by the European Social Fund and the European Regional Development Fund (TÁMOP-4.2.2-08/1-2008-0019), and from National Office of Research and Development (Pázmány Grant, RET-06/2006). The financial support of the Hungarian Academy of Sciences is also gratefully acknowledged.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2011 Springer Science+Business Media, LLC
About this chapter
Cite this chapter
Nagy, P., Balogh, A., Szöllősi, J., Matkó, J. (2011). Mapping and Immunomodulation of the Cell Surface Protein Architecture with Therapeutic Implications: Fluorescence Is a Key Tool of Solution. In: Geddes, C. (eds) Reviews in Fluorescence 2009. Reviews in Fluorescence, vol 2009. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-9672-5_8
Download citation
DOI: https://doi.org/10.1007/978-1-4419-9672-5_8
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4419-9671-8
Online ISBN: 978-1-4419-9672-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)