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8 Host Cell Membrane Structure and Dynamics

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Abstract:

This chapter focuses on the nature and function of these two-dimensional membrane domains and highlights several examples of microbial exploitation of host cell membrane organization. Cholesterol is an important component of most membranes of mammalian cells, and disruption of its homeostasis or distribution in intracellular membranes leads to debilitating disease in humans. For dynamic analyses of cholesterol distribution in living cells, it is necessary to have a fluorescent analogue that faithfully mimics cholesterol, as opposed to a fluorescent probe, like filipin, that binds to cholesterol and potentially perturbs its distribution. Dehydroergosterol (DHE) is a naturally occurring fluorescent sterol found in sponge and fungal cells. In a fluorescence correlation spectroscopy (FCS) experiment, a small region of the plasma membrane is monitored for fluctuations in fluorescence intensity. Fluorescence resonance energy transfer (FRET) requires two fluorophores with distinct but overlapping excitation and emission spectra; the emission spectrum of the donor fluorophore must overlap with the excitation spectrum of the acceptor fluorophore so that energy transfer can occur. Many bacterial toxins exert their action in the cytosols of host cells, but first they enter host cells by endocytosis and then they are translocated to the cytosol. Cholera toxin (CT) is a pentavalent toxin that binds to surface-expressed ganglioside GM1 and causes its aggregation. When CT is bound to GM1, it can be visualized in caveolae in several cell types, and this has led to speculation that caveolae mediate its internalization.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8

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Figures

Image of Figure 8.1
Figure 8.1

Structures of glycerolipids.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.2

Structures of a saturated and an unsaturated C fatty acid.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Image of Figure 8.3
Figure 8.3

Structures of sphingolipids.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Image of Figure 8.4
Figure 8.4

(A) Structure of cholesterol. (B) Position of cholesterol in a membrane. (C) Structure of the fluorescent sterol, dehydroergosterol (see text for details).

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Image of Figure 8.5
Figure 8.5

Diagram of the bilayer lipid structure of the plasma membrane. Note the asymmetric distribution of lipids within each leaflet.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Image of Figure 8.6
Figure 8.6

Depiction of the various ways in which proteins can associate with the plasma membrane.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.7

Schematic representation of microdomains in the plasma membrane.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.8

Representation of the plasma membrane depicting different mechanisms for compartmentalizing membrane constituents. (A) In the absence of any compartmentalization, proteins and lipids can diffuse freely within the plane of the membrane. (B) Some transmembrane proteins are prevented from moving because they interact either directly or indirectly with the underlying cytoskeleton. (C) Proteins can associate with other proteins in the membrane to form large complexes whose diffusion is restricted compared with monomeric proteins. (D) Proteins that are anchored to the cytoskeleton can coral in other proteins and lipids. (E) Membrane lipids can associate into domains that serve to trap or exclude other membrane constituents.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Image of Figure 8.9
Figure 8.9

Examples of cells with plasma membrane macrodomains. (A) The plasma membranes of epithelial cells are divided into apical and basolateral domains, which are kept segregated by protein barriers called tight junctions. (B) The plasma membranes of hepatocytes have macrodomains analogous to the apical and basolateral domains in epithelial cells; these domains are the canicular membrane and the sinusoidal/lateral membranes. (C) In migrating cells, like neutrophils, the cell front (leading lamella) represents one type of macrodomain, while the cell rear (the cell body and the uropod) represents a different type of macrodomain.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.10

Schematic representation of the outer leaflet of the plasma membrane depicting how fluorescent lipid probes insert into the membrane. (A) NBD-C-HPC; (B) BODIPY-C-SM; (C) rhodamine-PE; (D) DiIC.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.11

Principles of fluorescence recovery after photobleaching (FRAP). FRAP is used to study the diffusion properties of lipids and proteins in the plasma membranes of living cells. The diffusion rate of a protein depends on both the protein's size and environment, so physical characteristics of the plasma membrane can be inferred from the diffusion rates of its resident proteins. (A) In a FRAP experiment, first the plasma membrane is labeled with a fluorescent probe, and the initial fluorescence intensity () in a small region of the plasma membrane (dotted circle) is measured. Next, fluorescent probes within the small region of the membrane (dotted circle) are irreversibly photobleached (i.e., rendered nonfluorescent) by illumination with a strong laser; this drastically reduces the fluorescence intensity in that region ( ). The fluorescence intensity within the photobleached region is then monitored over time. As unbleached fluorescent probes from the surrounding membrane diffuse into the photobleached region, the fluorescence intensity in that region recovers (). (B) These data can be graphed to display the change in fluorescence intensity within the measurement region over time, thereby providing the rate of fluorescence recovery. (C) Both the mobile fraction () and the diffusion constant ()for the fluorescently labeled membrane constituent can be derived from the data by using equations 1 and 2, where τ is the diffusion time, ω is the radius of the focused laser beam, and γ is a correction factor.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.12

Principles of fluorescence correlation spectroscopy (FCS). FCS can be used to study protein-protein interactions in living cells. First, the plasma membrane is labeled sparsely with a fluorescent probe. It is important that the membrane is only sparsely labeled because FCS relies on detecting spontaneous fluctuations in the fluorescence intensity signal within a small detection area. Monomeric proteins (A) will diffuse rapidly in and out of the measurement region (gold circle) and this will produce spikes in the fluorescence intensity measurements (see graph A). In contrast, when one protein interacts with another (B), the complex diffuses more slowly through the measurement region and produces a more sustained rise in fluorescence intensity, causing the signal to fluctuate more slowly (see graph B). These fluctuations in fluorescence intensity over time are analyzed with an autocorrelation function. This type of analysis yields information about the concentration of the fluorescently labeled molecule and its diffusion rate. Although this figure depicts FCS measurements on membrane proteins, FCS can also be used to monitor interactions between cytosolic proteins. Also, dual-color FCS, in which two molecular species are labeled with distinct fluorophores, provides a sensitive means to detect molecular interactions. In brief, if the two molecules move independently, the fluctuations in their fluorescence will also be independent and will not correlate with each other. However, if some of the molecules move together in the same complex, then a fraction of their fluorescence fluctuations will correlate with each other.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Image of Figure 8.13
Figure 8.13

Principles of fluorescence resonance energy transfer (FRET). FRET is used to detect protein-protein interactions either at the membrane or in the cell cytosol. FRET requires two fluorescent probes with different but overlapping spectral properties. (A) The fluorescence emission of one probe, called the donor, must overlap with the absorbance of the other probe, called the acceptor. When this happens, excitation of the donor can lead to emission of the acceptor because energy is transferred from the donor to the acceptor. (B) The efficiency of energy transfer () depends on the distance () between the donor and acceptor pair and a characteristic radius ( ) for that pair. For a donor-acceptor pair with an of ∼5 nm, the efficiency of energy transfer falls to near zero by the time the distance between the pair reaches 10 nm. So when the donor and acceptor are far apart (>10 nm), excitation of the donor leads to fluorescence of the donor, but not the acceptor (C). On the other hand, as the donor and acceptor move closer together (<10 nm), excitation of the donor causes increased emission of the acceptor and decreased emission of the donor (C). This means that FRET can be detected by measuring an increase in acceptor emission, a decrease in donor emission, or both.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.14

Intracellular trafficking pathways in a nonpolarized mammalian cell. Prior to internalization, many surface receptors, such as the receptors for transferrin (TfR) and LDL (LDLR), are recruited to clathrin-coated pits, while other membrane proteins may be recruited to separate specialized membrane structures, such as caveolae (see Figure 8.15 ). Once internalized via clathrin-coated pits, receptors with different destinations are separated from each other in sorting endosomes. Those molecules that are destined for lysosomal degradation are transported to late endosomes and lysosomes, while all other molecules are delivered either directly to the cell surface or first to the endocytic recycling compartment and then to the cell surface. This sorting process can be mediated either by specific signal sequences in the cytoplasmic tails of receptors or by the morphology of the sorting endosome (see Mukherjee et al. [1997] for review). Newly synthesized proteins and lipids are trafficked along the biosynthetic route. After synthesis in the ER (not depicted), molecules are delivered to the Golgi apparatus, where posttranslational modifications occur. When lipids and proteins reach the -Golgi network (TGN), they are sorted and packed into vesicles for further transport to various destinations, including the plasma membrane, regulated secretory granules (not shown), or endosomal/lysosomal compartments. Colored areas of membrane denote putative membrane domains, and the “?” symbols indicate uncharacterized steps.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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Figure 8.15

Mechanisms of endocytosis. Endocytosis is the process by which cells sample their environment and turn over their membrane proteins and lipids. A variety of mechanisms have evolved to handle specific tasks, and each of these mechanisms has distinct molecular requirements. The best-studied endocytic pathway is clathrin-mediated endocytosis, which cells use to take up extracellular ligands that bind to specific cell surface receptors. Clathrin-coated surface invaginations (“pits”) recruit cell surface receptors (and their bound ligands) and then pinch off to form vesicles. Uptake of larger particles (>0.5 μm), such as bacteria or dead host cells, is achieved through phagocytosis, an actin-dependent, clathrin-independent process. Other clathrin-independent processes include pinocytosis, caveolar uptake, and macropinocytosis. These processes are less well understood than clathrin-mediated endocytosis and phagocytosis. Macropinocytosis involves the formation of large actin-rich membrane ruffles that capture sizeable volumes of extracellular fluid as they fold back over the cell surface. The membrane ruffles that precede macropinosome formation are analogous to those that make up leading lamellae of migrating cells or that precede some forms of phagocytosis, and so it is likely that the molecular machinery for each of these processes is similar. Pinocytosis is a constitutive process by which cells take up small volumes of extracellular fluid, including soluble molecules in that fluid, and plasma membrane. Little is understood about pinocytosis and related processes. Finally, caveolar uptake utilizes membrane invaginations that contain the integral membrane protein, caveolin. Notably, the extent to which caveolae actually pinch off from the cell surface and become internalized is controversial. However, caveolar association of the protein dynamin, which is involved in vesicle budding, supports the idea that caveolae are internalized, although it may occur infrequently.

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
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References

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1. Frye, L. D.,, and M. Edidin. 1970. The rapid intermixing of cell surface antigens after formation of mouse-human heterokaryons. J. Cell Sci. 7:319335. This work provided important information about membrane structure by demonstrating that plasma membrane lipids can mix in two dimensions.
2. Singer, S. J.,, and G. L. Nicholson. 1972. The fluid mosaic model of the structure of cell membranes. Science. 175:720731. This seminal paper in cell biology proposed a model for cell membranes that is still the basis for current models.
3. Brown, D. A.,, and J. K. Rose. 1992. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533544.
4. Brown, D. A.,, and E. London. 2000. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275:1722117224.
5. Hao, M.,, S. Mukherjee,, and F. R. Maxfield. 2001. Cholesterol depletion induces large scale domain segregation in living cell membranes. Proc. Natl. Acad. Sci. USA 98:1307213077. This characterization of the effects of cholesterol depletion on membrane organization in living cells provides crucial insights into lipid domain structure.
6. Holowka, D.,, and B. Baird. 2001. Fc(epsilon)RI as a paradigm for a lipid raft-dependent receptor in hematopoietic cells. Semin. Immunol. 13:99105.
7. Keenan, T. W.,, and D. J. Morré. 1970. Phospholipid class and fatty acid composition of Golgi apparatus isolated from rat liver and comparison with other cell fractions. Biochemistry 9:1925.
8. Maxfield, F. R. 2002. Plasma membrane microdomains. Curr. Opin. Cell Biol. 14:483487.
9. Rodgers, W.,, and J. K. Rose. 1996. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. J. Cell Biol. 135:15151523.
10. Seveau, S.,, R. J. Eddy,, F. R. Maxfield,, and L. M. Pierini. 2001. Cytoskeleton-dependent membrane domain segregation during neutrophil polarization. Mol. Biol. Cell 12:35503562.
11. Sprong, H.,, P. van der Sluijs,, and G. van Meer. 2001. How proteins move lipids and lipids move proteins. Nat. Rev. Mol. Cell Biol. 2:504513.
12. Axelrod, D.,, D. E. Koppel,, J. Schlessinger,, E. Elson,, and W. W. Webb. 1976. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16:10551069.
13. Dietrich, C.,, B. Yang,, T. Fujiwara,, A. Kusumi,, and K. Jacobson. 2002. Relationship of lipid rafts to transient confinement zones detected by single particle tracking. Biophys. J. 82:274284.
14. Feigenson, G. W.,, and J. T. Buboltz. 2001. Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: nanoscopic domain formation driven by cholesterol. Biophys. J. 80:27752788. Using advanced imaging techniques, this paper examines the complex phase behavior of model three-component membranes.
15. Kenworthy, A. K.,, N. Petranova,, and M. Edidin. 2000. High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell 11:16451655.
16. London, E.,, and D. A. Brown. 2000. Insolubility of lipids in Triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim. Biophys. Acta 1508:182195.
17. Mukherjee, S.,, X. Zha,, I. Tabas,, and F. R. Maxfield. 1998. Cholesterol distribution in living cells: fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog. Biophys. J. 75:19151925.
18. Sheets, E. D.,, G. M. Lee,, R. Simson,, and K. Jacobson. 1997. Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane. Biochemistry 36:1244912458.
19. Varma, R.,, and S. Mayor. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394:798801. FRET microscopy was used to investigate the cell surface distribution of GPI-anchored proteins. This paper shows that at least in some cases GPI-anchored proteins are clustered in domains at the plasma membrane.
20. Yechiel, E.,, and M. Edidin. 1987. Micrometer-scale domains in fibroblast plasma membranes. J. Cell Biol. 105:755760. An excellent example of the use of FRAP to study membrane organization.
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22. Mukherjee, S.,, R. N. Ghosh,, and F. R. Maxfield. 1997. Endocytosis. Physiol. Rev. 77:759803. A comprehensive review of endocytosis in mammalian cells.
23. Mukherjee, S.,, T. T. Soe,, and F. R. Maxfield. 1999. Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails. J. Cell Biol. 144:12711284.
24. Pierini, L.,, D. Holowka,, and B. Baird. 1996. Fc epsilon RI-mediated association of 6-micron beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling. J. Cell Biol. 134:14271439.
25. Sharma, P.,, S. Sabharanjak,, and S. Mayor. 2002. Endocytosis of lipid rafts: an identity crisis. Semin. Cell Dev. Biol. 13:205214.
26. Abrami, L.,, S. Liu,, P. Cosson,, S. H. Leppla,, and F. G. van der Goot. 2003. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. 160:321328.
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Tables

Generic image for table
Table 8.1

Major membrane lipids

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
Generic image for table
Table 8.2

Composition of cellular membranes

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
Generic image for table
Table 8.3

Fluorescent probes for studying membrane organization and dynamics

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
Generic image for table
Table 8.4

Fluorescence techniques for studying membrane properties

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8
Generic image for table
Table 8.5

Pathogens/toxins that exploit host cell membrane organization

Citation: Pierini L, Maxfield F. 2004. 8 Host Cell Membrane Structure and Dynamics, p 157-202. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch8

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